Datasets:
Synthyra
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TremblNLP

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ids
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10
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16
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117
4.4k
A0A6S4QS93
MRKTTIASNIKPISNIIAITGPTACGKTALVQKIARKEDIIINADSRQLYKHLNIGVAKPSTPEQIAYPYRLIDHQPLHKPFTAYDFLEHVKTTVLEQQHNPHSSRIFIVGGTLFYFSALENGLIDLKVDDSLSEQLNREYMSYGLPKLRAELKERDLDHFNQIDKNNPRRIIRALALLRTHQQPLKTLQRKRLPFPYRLHKIILIPPKQTLWKTIETRAENMFINDRLIHEVKQILKQGISKSVLLKHKTIGYLEITEYLNGFYSRETALAKIIKRTKLLAKHQITWLKKQQHAHFIFLGAPTDFITPHHTANTPHHTSTGHPPTTCHFSSTKQKSPRHATNKKSQQKRSATSTSLIENWSLTPDNIVMNNNKVYFAKTSDQCRAIAVKLCEECSHYPHSQV
Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A). EC: 2.5.1.75 Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA Sequence Length: 403 Sequence Mass (Da): 46381
A0A6G0AFZ1
MVTQNGFSILAHLSDIELYYTPAELIRDDKLILSGDEFHHSTNVMRNKIGDTLYVTDGQGIIYTSKIISIQKSELSALIVDSKKQLNESGNIWFCIPSLKKPDRLKFAFEKCVELGIINFILFTSRNAVSTKVIPHKFQKTVLAAMKQSLRAFIPQILSSSFGEIMNLDGNKFLFDQSAGKKYDGTVNNKETTYFLFGPEGGFHKSEIEKVNSENQFTLSPHRLRSETAVVKCASLLNLT
Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit. Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine EC: 2.1.1.193 Subcellular Location: Cytoplasm Sequence Length: 240 Sequence Mass (Da): 26979
A0A972R7J3
MKRNNNYQKYLNLRQEFDFFEYQSYKINLIDGVLKIEFSFNMSDKYFFKPKMELRLPDGIKLESTKMLNSAVFNIGMVELISYWKTACPPNIIVKPHKLDDEQAGWWKKLYFNGLGEFFYLNCIDVPIDGFVDIESCGQAAEAVKAEMNFEKVIVPVGGGKDSVVSLEILKRASVDVIPMMLNPNPARIRTIENADLKIGDSLVVNRFLDKTLLELNDKGFLNGHTPFSALLGFTNVLLSLLTGVGYIALSNENSANESTVPGTDINHQYSKSYEFERDFNFYVKKHINNSISYFSFLRPLNEIQIGLLFSRFSRHFMSFRSCNVGSKEDKWCAGCPKCLFTYLILSPFISTDRLTAIFGKNLLDDAELESVLMELSGNAKFKPFECVGTVDEVKSVIDNILKSGDGNFTGLRLLNNPRLLKLGNATKLSSLLSAFNRENNLPPEFEEILKKALNE
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis. Function: Cell wall formation. Catalyzes epimerization of the terminal L-glutamate in UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-L-glutamate. EC: 5.1.1.23 Catalytic Activity: ATP + H2O + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-L-glutamate = AMP + diphosphate + H(+) + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate Sequence Length: 456 Sequence Mass (Da): 51724
A0A316Z7V1
FDDGPYDWHAEIAQMFHDNQMKTTYFVNGNNWRCIYDEPQVTAMQTALATGSVMYASHSWSHPNFTQLTMDEIDTQVSLLEDALFATIGRVPRLIRPPFGETNLKINQHLKDRWGLEVVQWKQDAGDGLGATVAQEKAQYKSFKKGDDILILQHETHETSIHQVIPYALKQFKKKGIKSVTAAKCLTKQPSPYKVTAKPGTRNDNWTCVGKPQPGSN
Catalytic Activity: [(1->4)-N-acetyl-beta-D-glucosaminyl](n) + n H2O = n acetate + chitosan EC: 3.5.1.41 Subcellular Location: Cell membrane Sequence Length: 217 Sequence Mass (Da): 24537 Location Topology: Lipid-anchor
A0A841R3Z1
MARLFGTDGVRGVVNETLTPELAFHLGRAAAVFFVRGDDACARPRFLIGFDTRISGTMLAAALAAGVCSAGGDVDIVGVIPTPGVAYLTRTGDYKAGVVISASHNPYPDNGIKFFDCDGFKLTDAAEDEIEAMLRGDALDNNARPTADAVGRIQLIPEAAQRYADYIAASAPCRLDGLKIIVDAAHGAASAVTPAVLRKLGAEVIAIASEPNGVNINSGVGSTHPELLRERVLAEGADAGVANDGDSDRCLLIDETGAVLDGDHILLLAAQQLKSQNKLKNDTVVATVMSNIGFKKALEKMGLKAVFTSVGDRYVLEEMRAHDYVLGGEQSGHVIFLDYNTTGDGVLTAVQTLAIMKQSGRKLSELAQLMTTYPQILRNVRVYDKESWQDNPFIMAAIGEAEDELGENGRVLVRASGTEPLLRVMAEGPDHDQLERIVTDICTIIQREIGSEE
PTM: Activated by phosphorylation. Cofactor: Binds 1 Mg(2+) ion per subunit. Function: Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. EC: 5.4.2.10 Catalytic Activity: alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate Sequence Length: 453 Sequence Mass (Da): 48266
K2D7D7
MTASYFQKFKKFRPLFFSLMAISFIAITVGAIKKAGYHITYSATPSMPQGFYLVVPTKKIERYDVVEFIPPKPVLNFLKERKWVPQSGLIIKYVFAVPGDDVCVRDEAVWVNGKRVGDVYRFYAPEKILPRTKICGKLNADQYLLLSTKRRRSFDGRYFGAISSSDILGRAVPVFITDVGL
Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins. EC: 3.4.21.89 Subcellular Location: Membrane Sequence Length: 181 Sequence Mass (Da): 20590 Location Topology: Single-pass type II membrane protein
A0A9E7I3G0
MGIPKNRTALKEFEEFKEEGEAKYVISSCYGISPAFPGRSSPTRPLLLPWPTAVQVALLLSLFFSLRVPRPDLASHLGAKSHDGQRFRARARSLRGMRLLFHPTTLCRDQIGILRDRSFQKSIGRMAARKPGVFDVDGTLTAPRKVFRFDFRDHAANAGVHAATQGGNQIQIFNLYTTMIIKWPSCSQKWGINWSTACDPIVSMMEQLSHDEMIAYLIFLKSLKSFLGEDKLKEFINFTLHYIAGLDISIKRGTFIELRSGMLNVSPIGQNCSQEEHDEFEKYDKACSCFGFPMRLGQDLQFKIPWGGMTMKFMNQNELLVIQ
Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2. Function: Catalyzes the interconversion of mannose-6-phosphate to mannose-1-phosphate, the precursor for the synthesis of GDP-mannose. GDP-mannose is an essential sugar nucleotide for the synthesis of D-mannose-containing cell wall polysaccharides (galactomannans and glucomannans), glycolipids, glycoproteins and the antioxidant L-ascorbate. Catalytic Activity: alpha-D-mannose 1-phosphate = D-mannose 6-phosphate EC: 5.4.2.8 Subcellular Location: Cytoplasm Sequence Length: 323 Sequence Mass (Da): 36653
F6W9C3
MLGPLWNFLKRHRRKCIFVGTFLGGVYLLGKYGQKKIKEIQEREAAEYIAQARRQYHFESNQRTCNMTVLSMLPALRDALMQQLNSESLTALLKSRPSNKLEIWDDLKIISFTRSIVAVYSTCMLVVLLRVQLNIIGGYIYLDNAAVGKNGTMLLAPPDVQQQYLSSIHHLLGDGLTELITVVKQAVQKILGSVSLKHSMSLLDLEQKVKEIRKITEEQKPPSWVDTTGPRSLLCHYMMPDEETPLATQACGLTAGDVTTIKLLNETRDMLESPDFSTVLNTCLNRGFSRLLDNMAEFFRPTEQDLQRKDSMNSLSSVSLPLAKIIPIINGQVHAVCSETPSHFVQDLLMMEQVKDFAANVYEAFSTPQQLEK
Function: Involved in peroxisome biosynthesis and integrity. Assembles membrane vesicles before the matrix proteins are translocated. As a docking factor for PEX19, is necessary for the import of peroxisomal membrane proteins in the peroxisomes. Subcellular Location: Peroxisome membrane Sequence Length: 373 Sequence Mass (Da): 42081 Location Topology: Multi-pass membrane protein
A0A920AAI7
MPKIPHQSSATGMQAIPTTGVAMGVQYLEQQNIAEEFGKNKPVVVCSIGDAAMTEGEISEALHMAALKQFPILYFVQDNEWDISAHASEIRANDVSQYIQGFKGIELRTIEGNNFIESYTTIKEVLETIRKERRPFMIHAKVPLWGIILQGT
Function: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). EC: 1.2.4.4 Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] + 3-methyl-2-oxobutanoate + H(+) = (R)-N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] + CO2 Sequence Length: 152 Sequence Mass (Da): 16964
A0A660T6S2
MNCIVTEFSGFCHGVKNTISTIEKLLKDESQPVSCIGLPVHNSQITEKLITQGLNVVDKVEDIQSGILIIRAHGLPPERIEYAKKRGLKIVDTTCNIVVRVQNIAKTLHSEGYTVLITGEHEHPEVRAIYGCTQEEGIVCSSVNDVRALKLDGKVGVVSQTTFSESIFRKIVTALIERNFSELRVFDTICSTLAKRNTAAQITASQVDMMLVVGGKMSSNTKRLYEACKKINPNTYHIETKEEFSDEWFTGVETVGITAGASTPQWIIHDICNAVKAR
Cofactor: Binds 1 [4Fe-4S] cluster per subunit. Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1. Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis. EC: 1.17.7.4 Catalytic Activity: H2O + isopentenyl diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin] = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin] Sequence Length: 278 Sequence Mass (Da): 30723
A0A9E7KFL0
AGVNGDGFIAQDIGFENTAGPEKHQAVALRSSADRSVFYRCSFKGYQDTLYIHTNRQWYRNCDIYGTVDIIFGDAAVVLQNPNIYVRKPMDKQKNTVTSHGRDDFHENTGIVMHAAFVMAAPDLKPVQGSFQTFLGRPWRQYSRTVYLLSRLDDLIDPAGWHAWNETMSVSNLYYAEFQSKGDRADTSKRVNWPGYHVLTTDQEAEPFTAGNFLSGDSWVLATGVPYASGLYGYDVGGNN
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5. EC: 3.1.1.11 Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol Sequence Length: 240 Sequence Mass (Da): 26888
A0A9E7F0X3
MAGRYDSDPFQEEDVNPFAETGRRGKVAGSNYGGGPLSSAVRDLKKKERELQVKEAELDKREKLALLWMTKIGHLFFPIIHHDIASEIPVHLQRLQYLAFASLLGLTACLFWNVIVVTTAWIKREGFKIWFLAIIYFISGVPGDALDGVNFTIISSQKVYSYFRGSGKTAETKREAARGAMRAAI
Function: Probably involved in membrane trafficking. Subcellular Location: Cell membrane Sequence Length: 185 Sequence Mass (Da): 20725 Location Topology: Multi-pass membrane protein
A0A660T6F2
MNVEIYSYSVFTTVIGMTVVFLFLWFLSLLMSFLKILFKEKKKGMEQEAVLEDERVIVESEKRTDWIVAAVSAYLTAEEEELYPHSAKSWKPVSNEKFDPWVIGGKLLKRWSGV
Function: Catalyzes the decarboxylation of oxaloacetate coupled to Na(+) translocation. Catalytic Activity: H(+) + 2 Na(+)(in) + oxaloacetate = CO2 + 2 Na(+)(out) + pyruvate EC: 7.2.4.2 Subcellular Location: Cell membrane Sequence Length: 114 Sequence Mass (Da): 13257 Location Topology: Single-pass membrane protein
A0A345UJI5
MLNSTKTITAKDVATSYVEVSKSALQQNVRTLTELAGDRIKTMAIVKANAYGHGAAIVAEALEGKVTALGVATVEEAINLRKSGIIAPILVFAPVRKETVGDYKSFNLVATVGSFEELGMITPSMSFHLEFDTGMGRLGFYPEDWPEIRDFVTANMLKPSGIMTHFACADSPSHPMTIRQNAAFEDLLRTMDTFTRGKVIHASNSGGLLFYPQARYSMVRFGLSLYGYSPSPTYALPGLKPVLSWKTRICASRAIHAGATVSYEATWSAPEDGWLLVLPVGYADGIPRALSNQIVMRCNGQLLPQAGTVTMDYTMLFCRNYIGPGTEVTILGDEAMTADQWATLTDTIPYETLCGIHAKIERRLVV
Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids. EC: 5.1.1.1 Catalytic Activity: L-alanine = D-alanine Sequence Length: 366 Sequence Mass (Da): 39866
A0A920DSG6
MTRLVFESKMEAKKSINFDSNFTKGWFVNSAISFLSKRKRAYIFSSLLIVLGIASLSTRGLNQGVDFVGGRTYVVRFDQDVVTQDVRSSLAAPLETAPEVKTFGKANQVKITTKFMIDEKGSDELVNVKLNEGLKALGINYEVMSSQLVGPTIADDIKQSAVWAVLFSLVVIFLYILIRFRKMSYSIGAVAAVFHDVLIVLALFSILYGRLPFSLEIDQAFIAAILTVIGYSLNDTVVVFDRVREYFGVKSGSREEIVNTALNSTLSRTINTSLTTFFVLLIIFLFGGEVIRGFMFALMIGVVVGTYSSLFIATPIMVDTLKNDSKE
Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA. Subcellular Location: Cell membrane Sequence Length: 327 Sequence Mass (Da): 36216 Location Topology: Multi-pass membrane protein
A0A923XL85
MQMLVTGLSFKTAAVGIREAVSFSESDLSESLLKLSFYEAINEVVILSTCNRTEFYVITNDLDIAQKSIISFIEKEKKINFAQLESCFYNYYNKFAAEHLYRVISGIDSLIVGEGEILSQMKNAYAKAHEVGSSGKIFNALFRFVIETGKKVRTDTTIAQRPTSTGSVVAKLTKQTFGDLSTKTALLIGTGKIGTITAKNLRANNIGKLIVINRTHQKAKDLAEELGGIAFEFEHLDSVIEQADVTIVCTGSQGYLITNNNCPSKKEVLMIDLSIPRNIDSEITKNKNIKLYDIDSLESVVELNKEERTEIIGEVEMIIKEEMSKFVQWYNSLDVSPVISSMSDMFESVRENEVARTVKKYKLEDEQKKIIDIVTKSIIQKIIHYPITNIKMTDDTDLKKRYSDDLKYLFQLDQDDMSQKYFRKKEKLSPSLQLEKVFNDEGGSTNPNNIKKNEIIINKQDKKSSCPFASI
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2. Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). EC: 1.2.1.70 Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH Sequence Length: 471 Domain: Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization. Sequence Mass (Da): 53225
K8Z8P0
MEVEVNTQPNYQVKIENHLFQTIGKEIRHYWTPRKVMVVTDYTVQALYYDELQEQLQKEGFEVFLFSFPEGERNKSLEIAEQLYEGLAEQGFNRGDGIIALGGGVVGDLTGFVAATYMRGIPFLQIPTTLLAQVDSSIGGKTAVNLPFGKNLVGAFYQPDAVFIDPIMLQTLEWPYLAEGLAEVIKMAMIGDKELWEHLQTLPLEKEAFFAQLPYIITRACQQKADIVRQDPYDYGLRRKLNFGHTIAHALEAIDDYKGLRHGAAVAIGMVAILQLAYKEQWIENETMIEELIQLLEKFHLPTEYDEVGMDEIFEYIVRDKKGMKDEITLVLVNEIGQSFFKTISYEELWEILE
Cofactor: Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+). Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. Function: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). EC: 4.2.3.4 Subcellular Location: Cytoplasm Catalytic Activity: 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate Sequence Length: 354 Sequence Mass (Da): 40507
A0A059XEQ3
MNRGKYIVIEGAEGVGKTTMVQLIAGHLQSAGLPVKIMREPDSQNDVTARSIRRLTQDPRFPMNTRTEVLLYNAARSQSLEVIRGLVEQGVICLVDRSYLTTLAIQYYGRGDVTDYERINDIIDFAVGDMQPDLMLVLDAPVSTLRERVRGRYQGERFDNLDEAFLERVRAGYLWEAKQRELPVIYANEDIDDVFKQVWQHITAILSSRSKDASTGPQSVAEVLAAKPPIKSAPVVQPAATQPELPPAETNGQPDTALRYIVPKRVTGKLAREYRRSLDAILDTRAVLMEAVEEDDPARDIITRALLPVAAYGATDTAAARELVIAADDPFATLARQELQESQGAADEPVQLVHYWPRSELSLLPDMLYRYSGLERSELSRQTDSWSYQQKTDVFYRYLRSGGSALAACSYTVELLTDYDSLLVLRDHGVHSQHQRLTPRYGYAVPTSIEKAGLVERLESCFDLSLTLHSKLQAAGLESEAQFATLLGHKLRVTCTITAAQLFALRSTSATEPRLRPLLADLYTAVADVHPLLASRLLPAKTKTS
Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis. EC: 2.7.4.9 Catalytic Activity: ATP + dTMP = ADP + dTDP Sequence Length: 545 Sequence Mass (Da): 60658
A0A9E7INM0
MRMTSFAATELGRLFPSLLATPRNPRPVLSPLGRSPETLVSFSSSIRAAPAALELCVRNGRAPVVAAGTKHLIGSLTKTEGLKFAVVVARFNEIITNLLLEGALETFGRYSVDDDDITVVKVPGSFEVPVVAQCLGKSGKFDAILCIGAVIRGDTSHYDAVANSAASGVLNAGLSSGVPCIFGVLTCDDMEQALNRAGGKSGNKGAEAAVTARRETGEVGNGEAVARREQRGTDDGQGSRPWPSNLRLARSPSDPVAESNPTHRKRPFLFGTCTLSSIAPEEDAMHPPPTASALSLLLSLFFSARPPPKPRTSSLFFPVGSSPSMTPRHHFLLVIVSCIDRYSNISYLCVKKWPCAGEGQSDELCWVAAMEGRARKDGFTTDSRTECRGASPPKYLSADSLLLLLCLAASLLLLPVMLPSLPPPPPVVLLLPTGILVLLMVLAFTPSDVRKLATPL
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. EC: 2.5.1.78 Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate Sequence Length: 456 Sequence Mass (Da): 48338
A0A369A779
MKFLLLAGEPSGDLHGANLLRHLKKFFPDGAFYCFGGDKMAANGAHLLLHYREMAFMGFWEVISNLPKILKNLRFCKNWISKNRPDVVIFIDFPGFNLRVAEFSKKQGCRNIYYISPQIWAWKESRVYQIIRNIDLMITILPFERDFYRKYNYEVKFAGHPLLDALYLDKQSVEKSDADKDIDVVLLPGSRLQEVRHILPVMTEVAVHFPDRKFVVAAAPNLPDEIFQLCIKGKSNVEIIKEKTYELIRRSKAAIVTSGTATLETALLGTPLIVVYKGNSISYWIARQLVKVKYISLINLILDHPAVPELIQYQVTPSKIKEHLSMLLTDPKVVEEQHQNFSRLHKLLGGSGASQRAAIFIKEYITEHGKQV
Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. EC: 2.4.1.182 Catalytic Activity: a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a lipid A disaccharide + H(+) + UDP Sequence Length: 372 Sequence Mass (Da): 42618
A0A6P3DQM0
MARYAEDVYYEFAIKLTHDAAQILKAAINGAKNVDEKQDNWDLVTEYDRKIEEVVIGQLKSKFPGHRFIGEESTGKDLPELTDDPTWIIDPIDGTTNFIHGLPLTCVVIGLAINKEMVIGIVYNPVLEQLFTARKGRGAFLNNKPIKVSNVQDLSKALVCMESGFIKVHHMREKTIERMRTIALEAQGIRTLGVAALTLCYVAMGTVEAYYIEGPGISTWDIAAASLIISEAGGVVVDRETGEKINIMQPRAIGACNEKIADKLVKLIHEADQRAK
Pathway: Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 2/2. EC: 3.1.3.25 Catalytic Activity: a myo-inositol phosphate + H2O = myo-inositol + phosphate Sequence Length: 276 Sequence Mass (Da): 30511
A0A257ACG5
MKVGVIAFQGAIEEHKIALERAIKKMGKKGEVFLIRERLKEIDALVIPGGESTTISNLMKKTGIFDEIKRIADEIPIMGTCAGCILLAKEVRDKVETLKIMDMEVERNAFGRQKESFECPLSIKGFEKPFPGVFIRAPIIKRTWGNCKPLAKIGEGIVMAKQGNKIALAFHPELTDDLRIHQYFLEMI
Pathway: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis. Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS. EC: 4.3.3.6 Catalytic Activity: H2O + L-glutamine = L-glutamate + NH4(+) Sequence Length: 188 Sequence Mass (Da): 21127
A0A257A514
MKRRDIQKLLKEAEAEEGDLIEIRKGNEIYKGILMPHHSFSSEDVIIIKLENGYNIGIKIDDECEIHLIKKRKEKEKRKKKISFNKKKPIVSLIGTGGTIASYVDYLTGAVHPATSAEELALSVPEIFDICNVKAKILFQTFSENITPEHWKAMAKEVAEELNKDAEGVIISHGTDTLAYTSAALSFMLKNLSGAVVLVGSQRSSDRPSSDSFHNLLGAARVAISDIGEVVVVMHSNISPPLCTIHRGTKVRKMHSSRRDAFQTINENPIGFVDKGLKIIGKYRKKTDGMTEADVSIDSNVSLVYHHPALTPDDFMSIVEGKNGVVIAGTGLGHVNEKLIPCIDELTSRGIPVVVTTQCLWGRVNLNVYSTGRKLKKAGVISGEDMLPETALVKLMWALGHDDAIAIMKKNIAGEMTERSVYNAYQKNYIP
Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). The GatDE system is specific for glutamate and does not act on aspartate. EC: 6.3.5.- Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate Sequence Length: 431 Sequence Mass (Da): 47520
A0A151F606
MDGTVIEFYKMNGAGNDFVVIDNREDIIPERCKSEFAENVCRRRVSVGADGILLVEPSEKATFKMRHFNADGSEGEMCGNGARCIARFAFLKGIADKKMSIETMSGIIKAEIVNSHVKINVNPVTEKELHKKITVDGDEISVYYLEEGTPGLPHTVVFKDDLTMEEDIEDVGRKIRYHSAFSKGTNVNFCRVKGRDTIVNRTYERGVERETLACGTGSAAAACVAYLLGKCGKKVNVETKGGILEVSILDENLENIYLTGDAEIVYKSTLEERQVF
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1. Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine. Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate EC: 5.1.1.7 Subcellular Location: Cytoplasm Sequence Length: 276 Sequence Mass (Da): 30580
A0A8E3YDR0
SLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTILNMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGQP
Pathway: Energy metabolism; oxidative phosphorylation. Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O EC: 7.1.1.9 Subcellular Location: Membrane Sequence Length: 208 Sequence Mass (Da): 22334 Location Topology: Multi-pass membrane protein
A0A6I8NFZ3
MPIVDKLKEALKPGRKDSADDAELGKLLASSAKKVLLQKIEFEPASKSFSYQLEALKSKYVLLNPKSEGAGRHKTWEDAPVRRQGSDHGLGSSSGGDGVPAPQKVLFPTERLSLRWERVYRVGAGLHNLGNTCFLNSTIQCLTYTPPLANYLLSKEHSRSCAPGGFCMLCVMQNHMIQTFANSGNAIKPFSFIRDLKKIARHFRFGSQEDAHEFLRYTIDAMQKACLNGHAKLDRQTQATTLVHQIFGGYLRSRVKCSLCKSVSDTYDPYLDVALEIRQTANIVRALELFVKPDVLSGENAYMCAKCKKKVPASKRFSIHRASNVLTLSLKRFANFCGGKITKDVGYPEFLNIRPYMSQSSGDPVMYGLYAVLVHSGYSCHAGHYYCYVKASNGQWYQMNDSSVHSSNIKVVLNQQAYVLFYLRIPGFKKSPEGPISSPPDPRQPSIGPDHVKKIISNGALSSPLIGKRQDGGPRKKPQVTEETGVVVPRSSVTAGPRPQNGTPQSKLPPRCPSPKPSAKPSPASPEEPGKKVKKPVPPRSTGTAP
Function: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes. EC: 3.4.19.12 Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal). Sequence Length: 546 Sequence Mass (Da): 60046
K1XNQ5
MNHFSANIKEPDIVKLKHDLKQKSFEFKELPYGHFQAINSSLKITINVYHSLKCLIQGKGTEEFVRYYFEPEILKTFDLDYGHLNFKEKIGMDESGKGDYFGPLVVASAYVSNENFHQLKKNGVVDSKKINDKRIHVIAETIKKICPIHFISISPEKYNELYAKFNNLNSLLAWAHSACLKEILTKCNTTNATIDKFAQSAVLNKYLKIKNITIDVEQIVRGEQDIAVAAASIIARSNFLNQIENLSKKYGIQLPKGGGESTHSAGKEFIAKHGIENLGKVAKLHFKNTEKIQN
Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding. Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. EC: 3.1.26.4 Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester. Subcellular Location: Cytoplasm Sequence Length: 294 Sequence Mass (Da): 33261
A0A5P9NPC7
MAKLIVIMGPAGCGKSVVAARIAAARSATALDADDFHSRENIAHMAGGNPLTDAQREPWIAAMEKELHARLGNNENIVLAYSGLRRAHRARIRACAQRSLFIKLQVPIAQLQERVAKRQNHFMSAQMLPSQLAAMESPASEETIVQIAAHGSLDDVVESTLNAIRETFS
Pathway: Carbohydrate acid metabolism. EC: 2.7.1.12 Catalytic Activity: ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+) Sequence Length: 169 Sequence Mass (Da): 18350
A0A1B1YW16
MSAVCALRWQGGALELLDQRLLPAQQLWLRCASAAEVADAIRDMVVRGAPAIGIAAAYGAVLAARAAYAGHGTGWRDVIVADLDLIAAARPTAVNLAWAVQRMAGCLAELAGDPEPALLAAARAIHDQDIAANHAMAAYGAALIEPGSRVLTHCNTGALATGGHGTALGVIRTAHAQGRIREVFVDETRPWLQGARLTAWELQQDGIPARLVVDGAAAWLFARLRPAWLIVGADRIAANGDTANKIGTYTAALAARAHGARVMVVAPLSTFDPATPDGSAIEVEERPAQELTCLAGQAIAPAGFAAWNPVFDVTPADLIDAIVCEHGVIERPDAARIADFLAALGP
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 1/6. Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P). EC: 5.3.1.23 Catalytic Activity: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate Sequence Length: 346 Sequence Mass (Da): 35912
A0A651GKV7
MISPQEALEYIRKATPATAAEHKSPGEAHLQTLAEDVAAPHHHPFFDQSAMDGYAARFEDLVSGQALRIAAHLPAGSTTLPTIQPGEAARIFTGSAIPPGADTVIMQEHCSTENDLLVVERLPEKPGTHIRRCGEQIARGEVALPKGKVLNSSAIGFLASIGVQRVSVWKRPTAAIITTGSEFIRPGEELMPGKIFESNGIMLQTALQEQGIASERHICEDDPEKLTALINQLAEKTDLLLLTGGVSVGDHDHTPSALSSAGFNILFHKVNQKPGKPLLFATRKDCMAFGLPGNPRSVLMCYHVYVKAMLGQWTGQQEISWFSGRLRLTDELINRSGKTVFVTGKRTDQGVEPLRGQNSHMLQSFARADTIIVHPPEAPQLSAGSTVTVIPL
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis. Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. EC: 2.10.1.1 Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin Sequence Length: 392 Sequence Mass (Da): 42358
K2E1D5
MISVRTVTFAPNHPILMADLALYRKYRPARFNHLMGQNHVQKTILNAIKSGHLSHAYLFCGPRGTGKTSTARLVAKAINCITPDPEGESCNQCDYCLMMNQGSLVDLIEIDAASNRGIDEIRDLREKIRFAPNQAPHKVYIIDEVHMLTTPAFNALLKTLEEPPPHAYFILATTEIHKVPDTIISRCQRFDFRRIDQETLVDRLRYISQQENVEAEEAALELISRSSQGGMRDAISLFEQTLREGKLHLSVVQEVLGLVGNEGAIHLFSALEQKETSLALSEIQKLHEEGHNLYQFNREFLEFLRARLLEDLEKPEKVAQRLYWIDLFQKASVELKNTLIPQLPLEIAAIKACFWGQEQKNESWFSGLWQHKKEEPAPVTAPSSVSAGPSPLRHVASTSSDALPAPQEEGLKQVPQEGPSLADIKTNLPRVIEKIVTPSIRQSLNTALLHGLNKNVVQFQFQSKFHLEKVSSNTGKMEIESALETVFGAKLKVECDMSQVDNLLNKTLEIFGGELIE
Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. EC: 2.7.7.7 Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1) Sequence Length: 517 Sequence Mass (Da): 58154
A0A9E7ECZ4
MDFPSYSTSKEQARIYNEWFSFADSDGDGRITGNDAIKFFSMSNLSRPDLKQLVALAQAGNEITQDTLTNADLEKLNPPVMEGLDTLLSRNKASTKKIDPEIDVNSKPQSPPSTVQWFSSKSAKKIPLSQVTSIIDGLKRLYVEKLKPLEVTYRFNDFVSPLLTNSDFDAKPMVMLLGQYSTGKTTFIKHLLKTSYPGAHIGPEPTTDRFVVVMSGPDERTIPGNTIAVQADMAFSGLTMFGTAFLSKFECSQMPNPLLEHITFVDSPGVLSGEKQRTQRSYDFTGVTSWFAAKCDLILLLFDPHKLDISDEFKRVIGSLRGHDDKIRVVLNKSDQVDTQQLMRVYGALMWSLGKVLNTPEVMRVYIGSFNDKPINEAAVGPLGKELFEREQDDLLSDLKDIPKKACDRRINEFVKRARAAKIHSYIISHLRNEMPAMLGKAKAQQRLIDNLEDEFAKVQREYHLPAGDFPNAEHFREILGGFSIDKFEKLKPKMIQAVDDMLAYDIPELLRNFRNPYERKINETKDVMKRKASEIDKSKIEKNKGDKGGFMALSGPRRVESSFSDMSISSTGSGFGSGSGIGLSTDVESLTSKPKGRPPASATAPPKGLGMKLGKTQRTNQFLESLKAEGEVILEDVQPIAAQSKPSLPPTDPITLTIEERLNVVIRRDGGLNNFDIQGTLSLQILNQEDGFVQFQIENQDVHGLSFKTHPNINKELFNSKHIIGLKDPNRPFPTGQNDVGLMKWRIQGMDEASLPLTVNCWPSVSSGETFVNIEYEASEMFDLRNVVISIPLPALREPPNVSQIDGEWKYDSRNSTLEWSLLLIDHSNRSGSMEFVLPPADSSLFFPIAISFTAASTYSDVKVVNVMPLRGNAPPKYSQRIQLIADTYQ
Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. Subcellular Location: Cell membrane Sequence Length: 891 Sequence Mass (Da): 99458 Location Topology: Peripheral membrane protein
A0A1J5E9U1
MVTVSLGVLVSGRGSNLQAIIDAINGGKLNAAIRIVISNKKDAYALERAKKAGIKTIFIDPKDFLSWQDYEQQMVSQLKANGVELVILAGFMRILTPYFVNAYKDRILNIHPALLPSFPGLHAQQQALEYGVKVTGITVHVVDEGMDTGRIILQRVVDVLSNDTVKSLSERMLRIEHQVYPEAIALYCK
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1. Function: Catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate. EC: 2.1.2.2 Catalytic Activity: (6S)-10-formyltetrahydrofolate + N(1)-(5-phospho-beta-D-ribosyl)glycinamide = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide Sequence Length: 189 Sequence Mass (Da): 20935
A0A7J4V897
MKVVTVDIGNSKIKTGEFYNSELIRTMVIDDPLEIKPLIYGSHIEVVVSSVVPKQTSLLESILRNQSNTDIFLLDHSLDFGFNVTYSPLNSLGLDRLCSVAGAKHLLEIDNALHDHDFVISIDFGTATTVNVLQVGKPSVFTGGMIAPGLRIMNSALNQFTAKLPLIESYQSGSFLGNSTENSIRSGILNSTVGLVERVFDHFTTISQDIKIFVTGGYAPQLMPHLQVPFQYEPFLNLIGIYSVYYRNKR
Cofactor: A monovalent cation. Ammonium or potassium. Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5. Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis. EC: 2.7.1.33 Subcellular Location: Cytoplasm Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+) Sequence Length: 250 Sequence Mass (Da): 27660
A0A7J4VCQ7
MQESNLQETLKKAFVSDDLLTQCMHCGMCLPTCPTYNITKLESSSPRGRIRLIKSVAEGKLEINDTFINEINYCLDCQACETACPAGVKYGAIVEAAREEVSRNDLEPFKNRFLRRFGLNFILANQSLLKIVARMIYFYQNTGLQGFLHRMGVFKILGTGLEKADQLSPAISKRFSSDVMDEVYSPAGPVRYRVLLPLGCLMDVAFADIHSDTLNVLLQHGCEVIIPRNQGCCGSLHAHNGEQKKGRELAQRTYDLFSRYEYDFIVSNSAGCGAYMKEYGHILSDPGVGGVSPLTTHHSPLIFSSKVKDLSEFLAETGFMAENYDFAGKVTYHDACHLAHTQKVTKQPRDIIRSVKNVSYTELEEASWCCGSAGIYNVSRYDDALKFLVRKMDNLDKTGSEVVVMANPGCMGQIKHGTEKFNQPVEVMHLATFLNRAYRPAKK
Cofactor: Binds 2 [4Fe-4S] clusters. Function: Component of a complex that catalyzes the oxidation of glycolate to glyoxylate. EC: 1.1.99.14 Catalytic Activity: (R)-lactate + A = AH2 + pyruvate Sequence Length: 443 Sequence Mass (Da): 49514
A0A972R3H7
MTSNETTQYDTIIIGGGVSGLVTAVRLKYAGQSVLVIEKKDQAGGAISTSHAEGFLFEGGPNSALDSNPLISELFQSLDIQGERCNAAPESSNRYILKHGELIPLPMSPPAFFATRLFPLRAKLRLFREPFIKPSPPDADETVADFVLRRLGRDFLDYAIDPFIAGIFAGKPDQLSVRAAFPKLFELEQKYGSLIKGQIKGKKERKKRLEKSKQTAGMFSFFNGMETLPRAMHRYLGNAVLLSTTVEAFSRSDGLFRVDLGERTVTAPRLVISAPADATAKFIKELAPDLGREFTAIPYPPVAIVGMGFKREDVKHPLDGFGFLVPQVEGREILGTIFSSTLFPFRAPEGRVLLTTFVGGMRQPENALLPESKLFELVLKEIRDLLGVRGAPVFQASRAWKRAIPQYVPGHLDIMQRVQELEERIPGLFFCANYRGGISVGDCIKSAYALADRIAARASQEEPEPKQA
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis. Function: Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin III. Catalytic Activity: coproporphyrinogen III + 3 O2 = coproporphyrin III + 3 H2O2 EC: 1.3.3.15 Subcellular Location: Cytoplasm Sequence Length: 468 Sequence Mass (Da): 51579
A0A345UIG3
MRSAMNLRITLLFFFLGMMVLSGCRSQRDTVRTGTVFERGEASWYGPGFHGQATANGERYDQEALTAAHRTLPFDTVVGVRNLHNGKKVVVRINDRGPYANNRIIDLSRAAAREIDMIQSGIAPVELTILRSPVPVQRAAIARELFTVQVASFNTRQEATAHARSIRGARVAEGRVQGQTVYRVYVGEFRNQRDAERQRRRLSRQGINGFVKQVQN
Function: Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides. EC: 4.2.2.- Subcellular Location: Cell membrane Sequence Length: 216 Sequence Mass (Da): 24301 Location Topology: Lipid-anchor
A0A151F9Z7
MKNKFAQAMKEKESQLCVGLDPRPEQVQRDSIYEFCMNIVEQTSEHCFCYKPNTQYIMPLGFSEIKKLNEYIHEKGCLSISDHKLSDIGSTNKAALHWLSKMGFDAVTYSPFPGNIKETIDNAQNYDLGVITLTLMSNPEADFFMKSVIQGKLGYEFIAEQIAKYDGFGAVIGATCRVEDIKRIHSLLTDQLILSPGVGAQGGGLDIVRIFKERTMVNVSRDIITRDNPGERAQYYKELINNTLQE
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. EC: 4.1.1.23 Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP Sequence Length: 246 Sequence Mass (Da): 27780
A0A1L5KQL0
SRQHLAPVSLVESSIMDTITLTGVHANGTHGVLAFEHERPQTFVVDATLHLNLTRAGQSDDLNDTIDYGRVAKDIVAVIEGPHVGLIERLAQLIADRILADAPAVMQIDVTVHKPHAPIVVAFDDVSVSITRVRDGACGDAEQALSEQLHEPASSVVSPVIPSMHSAVVALGGNVSEVESTLRAAVREIDALPGTQVTGISPLYRTAAWGMADGTPDFLNAVVEL
Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4. Function: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin. Catalytic Activity: 7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde Sequence Length: 225 Sequence Mass (Da): 23767
A0A971GPB9
MKIKGLDNAVLLLDKPAGITSFDFISKIRRIARIKKIGHSGTLDKFASGLLVICTGQATKLTRYFLESNKRYTGKIRLGIVTDTCDITGEVVSRNDLQNINEFTIREAMARFIGDSVQVPPEYSSLKIRGERASDRVRRGETVTLEGRNITITRADIIAIDCDNGTVDFDIACSKGTYIRSIARDLGEVLGTGACLQELRRTESGKFLVENAASAEDVEAYAGCKIPAFFALDPAAALCSFGRIILDEAGAAKVLNGACFKRDEVVDHEIKALETYLVFDSHEELIAIADMDIDSWWINYHSVFNKMESY
Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. EC: 5.4.99.25 Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA Sequence Length: 310 Sequence Mass (Da): 34266
A0A930X755
MTLPEDSQQDPLELTIDALTVLPRTASLLERQNPEAVLSGASYQVLSKLGEGAMGMVHLVRDLHLEREVAFKQLIGASGSQSEAVRRFLGEVQITAQLSHPSIVPVYSLEQTDKGLGYTMKQVQGDTFKELIQAARAAVSAGTRRPPHLSRQTLIAHFLKVCDALAYAHYRGVIHRDLKPANLMLGAHQEVYVMDWGIARPFGAAAAAYPFEAEEAGKLIGTPRYASPEQARGLNAQLDPRSDIFALGLILHELLCLQPAYTGKGREAMLERVRQAQRDPCTALPGDEPLPPALIAIVDKATAWKRAHRYASVQELAADLQRYLRDEPVQAAPDPPLEALLRGFRRHRVRVLSGVFVSLLLSAGLSLGSLWQRQQTLAAAAAEEARQAQFWEHLLQQGQQAERQLQMIPRVLAGLAGAGLQALESPPRGRPLYYLDDASWPQKVPDQIDSSFYKAPVSIDWTGFSIAYTRSEADLQQQLWQLAPLRHRFRQLMLRSAGPEAAADPRQSLTVTGAPVMFASLATEEGLLQYFPGISYNTPNYDPRQRPFYTLAAHKQGLQCGNPYLDRLVGSLLPCSLPLYDASGRFRGVAVADSQFNQLARTVLSLPDASYREAFLLDAEGRILLRSSDRDRQIQKQDQIQGAHTLQPFADSALQQAIAAREGAGYLENRQRRLGYLRLNFQGWYYVLLADTPGLPL
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] EC: 2.7.11.1 Subcellular Location: Membrane Sequence Length: 697 Sequence Mass (Da): 77152 Location Topology: Multi-pass membrane protein
A0A364K3N9
MIILEGAGVMKHWRVIYSFILVIAWLGLGYFYFAYSLDPPKRDKDVVIDIPPNTSTDKVVQMLKEQKVVNQDWFLSFYIKYKNYEIKAGTYHVKPNEHVYYLLPRLAKGKEDRVHVTVVPGATIPEIANSLKAKGFDSEGFLKALKNRQPKYEFEKEIPDNPDAYHKLEGYLMPQTYLLTKGQNPEEIVDQMLGEFDKYHQKNKEKFRSIKLQNGKPLGVSGVVSIASMIQKEAFKQEEYPLIAGVIYNRLNNPSTYPYLNIDATSVFANKMEGNKYKTPYDAIQNIKQYNTYKSKGLPPGPIGNPGEATLNAALNPDKHVYCFYTARLDGSNLHYFAKTLKEQSQNNERAKANLEKFRKNNKSN
Function: Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation. EC: 4.2.2.- Subcellular Location: Cell membrane Sequence Length: 365 Sequence Mass (Da): 41888 Location Topology: Single-pass membrane protein
A0A7C2PQA2
MMEEDSKRLLILAAGQSSRMGSLGQKQFLELQGLPIFLWSIKTALALSSNYSLTIVLVHSVGDREKYKDSLIKNLDSSSLPSISLVEGGASRSQSVYNGLQSISHDAEPNDSIIIHDSARPFLGVQDLLKVIDSLKHYSAVTLSYPVTNTIKLLKADTQEIQAHLKRDDLRAILTPQGFRFSVLWKAYREFIRSPYPVTDDTEIVAKMGHPIQCIDGKKSNIKITNPEDLLYAEFYCQKYNLKPSEKP
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6. EC: 2.7.7.60 Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate Sequence Length: 248 Sequence Mass (Da): 27787
K2C0B9
MQMKNFPSLRLLLHDWVTLSKTQDITCEKITLDSRTVEPGSIFFAIPGLKEHGKIFMEEALSKGARAVVSDSLDENHVDILNYAEKKIPLIYIQNLKKYLGCIASRFYQHPQHTLDLIGITGTNGKTSCSHFIANALRDYGTPCGVIGTLGYGIGAHLHPLNNTTPDIFTLYHILRELHDQGARCVAMEVSSHALKQERIQGLKFKVGIFTNLTQDHLDYHGTMEDYAQCKKSLFHDYPVQSAILNIDDPHGLTWLDTIPEEIKKQAYSLHEKASSSYPLTHVQSFNSNKDGVFAAIKTPWGDGVFHSPLLGKFNLSNLLATLCVLGTYPIPLPEILHLLSQLDPVPGRMEKIGSKNQPFIIVDYAHTPDALQKTLETLRPYCQGALWCVFGCGGNRDKMKRSMMGCIAEKNADNVILTDDNPRDEDPKEIIHEILRGFKNKNNIVVEHDRRRAIFHAINCAKNEDIVLIAGKGHEHYQQLGNKKIPFNDSLEAKLALENRTT
PTM: Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP. Pathway: Cell wall biogenesis; peptidoglycan biosynthesis. Function: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. EC: 6.3.2.13 Subcellular Location: Cytoplasm Catalytic Activity: ATP + meso-2,6-diaminoheptanedioate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate Sequence Length: 503 Sequence Mass (Da): 56468
K2CMH0
MVIVGLTGGIASGKTTVAHLFSQWGVDVIDADLVGREILEKNKIVSSEIKKKFGKEICKTSGKLDTKKLRKIIFENKNKKIWLEKLLHPIILEKIKKKIKKIKSSYGIVVIPLLLETGPFPFIDHVLLVDVSPATQIKRLRARDGLTVSEARAALANQLSRRARLLGAQDIILNEDSTSFSELAKQAKKLHKRILAADDIEKMKRYTPHAGKLHLFKE
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5. Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A. Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+) EC: 2.7.1.24 Subcellular Location: Cytoplasm Sequence Length: 218 Sequence Mass (Da): 24462
K1YK09
MSTEIETIQKTAQAASEAVEATGGIGSLGINLKIFIAQAINFLIVVLVLWRWVYKPLVAILEKRQAHIEKSLKEAKEIEERLALVEKERSLVVAQARKQSADLLAKAEEQSKEQAQKMALSAKEEVQKILNNAKIALVAEKQAMIHDAKSELAKIAVLAAEKILSENIDKKKNELIAEKAIKDLV
Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). Subcellular Location: Cell membrane Sequence Length: 185 Sequence Mass (Da): 20445 Location Topology: Single-pass membrane protein
A0A5P9NN57
MVFSRQHCRVHIVLLLILCACRVSAVSAGEWLSGGRAIMGTEVRVELWADDADVGRALQAQVFAEFERLDTMMSPWKPASEISRVNREAARSPQKVSAEMFNVVLRSLHYSQLSNGAFDISFAAAGQHYDYRSGKRPERETLKAAQAAIDFRSIVLDAQGQTIAFARPGMALDLGGIAKGYAVDRGISILVAAGITSAVVSAGGDSRILGDMGDRPRMIGVRHPREEGEYAAIIPLVDTAVSTSGDYERFFEEEGVRYHHILDPATGESADGLQSATVIAPLSLDCDALSTTVFVLGIERGLALVNSLEGVDAILIDADGKLHYSDELLLSTTE
Cofactor: Magnesium. Can also use manganese. Function: Flavin transferase that catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein. EC: 2.7.1.180 Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H(+) Subcellular Location: Cell inner membrane Sequence Length: 334 Sequence Mass (Da): 35997 Location Topology: Lipid-anchor
A0A9E5XVS3
MDIISVFIIAAGLSADSFAVSAADGLANPDIKLKNVLQIALIFAIFQALMSVTGFFAAYSFSDYLKVIDHWIAFILLSFIGTKMIYESLKKDNDDFLNLKLTPLTIAAQSFAASIDALIAGVSFAFIKINIGLTATIIGIVTFLFSLSGFYAGKKIGNRFSGKAEIFGGIVLILLGTKILIEHIRY
Function: Probably functions as a manganese efflux pump. Subcellular Location: Cell membrane Sequence Length: 186 Sequence Mass (Da): 20102 Location Topology: Multi-pass membrane protein
A0A924E1R0
MSLSEDAVSPRRSTLVFYLTALCWLALDQWSKSQVVQHIPLGSSMPVIAQYFALTHVTNTGGAWSLLAGKTIALGILSLAVCVGIMVYEQRLRQRVLVQTLGLAFLLGGAAGNMIDRLRLQHVVDMFDLQWHGHNIFPIFNVADIGIDVGVGLLLLVSFLERPQVQAQPAAPESAT
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage). Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins. Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains. EC: 3.4.23.36 Subcellular Location: Cell membrane Sequence Length: 176 Sequence Mass (Da): 19164 Location Topology: Multi-pass membrane protein
A0A345UH61
MSSHYKALTRKYRPVRFSDIVSQEHVSSTLQNAIESGRISHAYLFCGPRGVGKTTMARVLARTLNDIGDDVDGEMLNQTLNIIEVDAASNNKVDDAHRIRESVRVPPQSGNYKIYIIDEVHMLSKQAFNALLKTLEEPPAYAIFIFATTEPHKVLPTILSRVQRFDFKPISVQQSVDRLRFICEREDITIDEDSLHMIAVKADGALRDALGILDQVIALCGTDIQYEALMKAFNAVGLERLFELTGYIDSGDSVAGIQLISDLLMEGHDISEFLGSLTGFMRNLLLARDPSNFYAIETSKDVKLRLNKAAQSFSDDDLMRMLHIVHEAQFRLRDARQPRILLEMTVLKLIRMEKTAGLSGLMQELERLRNAFSTGGGSGKSAASVQGSTASEPAPYKTQSPASPSATPAASNPSTAAPAPAPTQAPAAPKAAVDIPGAPPVSGLRRKPGMRNKQAVSGQPTPSIAVKAPASPPSHTETGAATNKARTNSDSDSNSGSETKAQTASAPADLPPENAILATQPARKPTSQAAKPQSTPAPAVQLMNSGAPDPSTADKPVYLHQVVQVWDTFIKNLHPPVSQSLILALDRVKPSDLKGRLLTLETPDPFVLDMLETNSRFLSEQLEPHLGQRFKIQGRLIQVGNTEQTEEDPFAKFERLQKQDPKLRQIVELFGAEIDWNYR
Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. EC: 2.7.7.7 Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1) Sequence Length: 679 Sequence Mass (Da): 74186
A0A6P3DNL0
MARILILFLINLMFPNLLLGDVISSQVDDLSYRLPIEIKPNFYELNLTVNLNSNLSETDFKFTGEVKIDIVAETQDVRSITLNMKNLTIKNISLYHSNKTAIKLDSTVYDDVHEFLIIMLDDKLKKGNNYLLTVSYSGVVNDQLRGFYRSRSADKNGNLIYVAATHFEPTGARLAFPCWDEPAFKARFNISITHSKSYHAISNMPVEELKVENDMKTTKFKTTPRMSTYLVAFIVSNYECNEDGMFRVCTKPQAVNQTHYALEKGKKLLDALNEYTAINFSHYLPKMDQVSLKDFSAGAMENWGLVTYRESALLYQDGVTTTRTKQSITTIIAHEFTHQWFGNLVSPEWWTWIWLNEGFADYFQYIITHKVLPEWRLDEVFVVDNIQGNAFIADAGENPRPMNKNAKTSQEISRLFDNIAYQKAGSVIRMMSHILTENVFHEGLKEYLKQNALNVANSTNLFEHLGKNKKWDGASFGKIMDGWVNNAGYPVVNVKRNHDDELQLSQERFSFYETKNDANWWVPITYVNSSSMNFNNTTPIIWLKPGRNETIKFNKAERWIIVNTQQAGYYRVNYEPEMWKLLSMQLNSDNYENIHVVNRAQLIDDALNMARTNRLNYTVALTLTLYLERETDYVPWQTTFRNMQFLHNMLRTSVQYNNFMSYIRKIMKSVTSQVRYKPYQKGEELDIVKLLRINAMEWACRAGVDECKDYTNREFNAWLSNSSRSFDIDLKNNILCDGIRSANKKVWNYTLTELLKTKDEDEKKSLLSLLACSESVDLLKEYLHMSIQENATVTFNNAVLNVVSQNPKGVSIALEVLTNEIEKIKKLNKAEDVIKSSVDIIASAITNKDQLTQLIMFLTKERLKPNTLQTILLKATRNLEWLNVHQETIENWLYTHRNYFNSSSSLTFATLLIIFSIFITRFY
Cofactor: Binds 1 zinc ion per subunit. EC: 3.4.11.- Subcellular Location: Cell membrane Sequence Length: 923 Sequence Mass (Da): 107007 Location Topology: Lipid-anchor
A0A920AB92
MNLVAIFIGGGLGSLCRYGMGKFIMSYDSSVLAYATLFSNVLSTIVLALFVYFFQEKIDLNEVWKLLVVTGFCGGFSTFSTFSFETFEMLKNGQTALAFANLFLSVLLCLFVLYIIYKKSII
Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity. Subcellular Location: Cell membrane Sequence Length: 122 Sequence Mass (Da): 13617 Location Topology: Multi-pass membrane protein
A0A1S8G2Z7
MSKSTVKRIEQINHSVKQISKGNLEVHIPVLKSDEIGELATNINGMAESLKESIEKEKRSQEMKNEMIHNISHDLRTPVTSLIGYVDLVESKLHSNVEECNQYVAVLKRKSDELKNQIDDLLEYCHINYKEIQLHKEIIGVKALIEQIMIDFVPQLDEAKLHFEIECKQNLQIEADIHVIVRLIQNVISNSISYGKSGKKIIIQILQKKPNVEIKIKNYGQCISKEDLPYIFEKFYRGEKSRNAHTGGKGMGLAIAKSIAQLHEGDITVCSSNEETTFTILLPEYKEEL
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. EC: 2.7.13.3 Subcellular Location: Membrane Sequence Length: 289 Sequence Mass (Da): 32979 Location Topology: Multi-pass membrane protein
A0A924E1A1
MAAPRLFVDPAALHHGMAHLNKDERRYLITVLRLDIGAKVTILDGVGGLYQSTIAQVGKEAVVCELGPLETATGESEREVHLWMACIKSDRMEWLIQKATELGVAAIHLMDTARTVMHHPDGKMDRWRKIAREAAEQSERGRIPAILDSRPLAGRSLPLGAFYCAERRPDVPSIRTAAGKNAGEALHVLVGPEGGWTEAECAMFAEKGAGPVSLGTRILRAETAAIAALALLLLE
Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit. Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine EC: 2.1.1.193 Subcellular Location: Cytoplasm Sequence Length: 235 Sequence Mass (Da): 25426
A0A6S4QG54
MIEIDFAGIPFKTPLVGVSGTAGYITDFKPFTDMNAFGGIAFKSITPLKRQGSPPPRVCECEAGFINSIGLQNDGIEAFLTCHYPRAQAIPVQKIVNLAAFSIADFTHLVRKVAELDDIALIELNVSCPNVDYNGRDFASDSGLLRELIVSCTPLKKDKPLMIKLSPHGAVISELALLCEKYGADALSLVNTFRGMKINIDTWQPFIKKIVGGYSGIGIKPISLAMVYEAAQTVSIPILGIGGVTSYEDVIEYMLAGASLVGIGTASLMNPRIPKRILKRFKAYLHNRGIVAADLIGAMKECP
Cofactor: Binds 1 FMN per subunit. Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway. Function: Catalyzes the conversion of dihydroorotate to orotate. EC: 1.3.-.- Subcellular Location: Cytoplasm Catalytic Activity: (S)-dihydroorotate + A = AH2 + orotate Sequence Length: 303 Sequence Mass (Da): 32679
A0A933UYJ2
MELTLPALLTAAILGLVQGLTEFLPVSSSTHLRFLHALFSFDAGASSVAFDVTLHAGTLCAVVIVLWRPQIIQKTPALRTVCMLAVSLASTVIVYIILKKAGITMKDSAVGADEHAVLIMFAAGLLVTGVLLIATRFIKNNTRDALSLGLVFAVVVGSAQGLALLPGISRSGITIISSLFLGAAPGFAGTYSFLLSIPAILGAAAMDIRHIAALDPLVLAVGFICAFISGFAALKLLITLIKKGRFYFFGFYCIAAGITALVVLLR
Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate EC: 3.6.1.27 Subcellular Location: Cell membrane Sequence Length: 266 Sequence Mass (Da): 27804 Location Topology: Multi-pass membrane protein
A0A931GH48
MSIARTSQAASGEPRLYRRMLVLAAAILLIDQASKAWAISALSDGRNITLIPDLLGLRLLYNPGAAFSIGAESTWVFTLATAVTVAGVLFVGRRLRSAAWTAALGGLLGGAASHLLDRLSREPGFGRGHVVDFIDYGVFVGNIADIALTVTCAAIFLLNLRGVPLGDAADRPEPEPPAAEDGGAPPARTERA
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage). Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins. Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains. EC: 3.4.23.36 Subcellular Location: Cell membrane Sequence Length: 192 Sequence Mass (Da): 20031 Location Topology: Multi-pass membrane protein
A0A532V5V8
MNNTGKLIVYEGIDGSGKTTQLQRSAEWLSSRKYLVRTYREPTSGPHGQKLRQSASTGRLSAEEEMNLFLRDREWNVTTRIRPALSERVTVLLDRYYYSSIAYQGARGLDTEMIRDKNRKIAQEPDLVLLFDLDPEMAIDRIRASRGDTPNLFEKIDYLKKVRAIFLSLTDPNMVRIDASEPIDTVWQQVEEALASLFPHP
Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis. EC: 2.7.4.9 Catalytic Activity: ATP + dTMP = ADP + dTDP Sequence Length: 201 Sequence Mass (Da): 23122
A0A9E7HK43
MESCRGVQVPPVILMCSVRQQLESANLQRSYFDNKLKNATRDTNMKFRNPKFLSMLNQLRFCLLEMYLKLHKIPFFTALWKIDKDGKVKGAVDTCFRLLHSHARSSSWLTSIPIPMKNPLELACKGRRY
Pathway: Glycan metabolism; pectin biosynthesis. EC: 2.4.1.- Subcellular Location: Golgi apparatus membrane Sequence Length: 129 Sequence Mass (Da): 15051 Location Topology: Single-pass type II membrane protein
A0A2H5YQA2
MLRRRSASAVIIVLVAVVPALLGGWVFIALLIAVGLLGLWELARAFQHAGHTIDFRLSGVLFLIILLSITTGRSSAVLLLSTGTAVLVPLVWALRSTRHEEALAHAALTSLAVLYLALPLGAASMLRELDGTSLGGWLQSTAERLSSGDTALGLAWFLWGLSVTWLTDTAAYLFGTRFGHTKLVPHLSPGKTRAGAIAGLAAGAVTGLLGAALFGLPLPLWLAPLAGLVVSLTAQIGDLAESLIKRAACIKDMGNLIPGHGGVIDRIDALLFTLPLTLALATLVAEVHWP
Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3. Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate EC: 2.7.7.41 Subcellular Location: Membrane Sequence Length: 290 Sequence Mass (Da): 30283 Location Topology: Multi-pass membrane protein
A0A924E3L0
MVFPADSRATWIASWHDRRVVVLGGARSGIAAATVLQTLGARTVLSDRGQLGAPTMDQLTTVGITCEGGGHSATLLDDAVMVVPSPGIPLDAPILTEAVRRGIPLIGEIELAYRLCPSPMVAITGSNGKTTTTSLIDAILQAQGRNVGCGGNIGLPLVSIAQQAWEVLVAEISTFQLETVHELAPETAVLLNLYDNHLDRHGSRDVYFGLKAKLFARQTASDRAVYNADQPEIVRRLSGIASRHFPFSRLQTLPNGTGLADGWVVVWEDGQVTPVMPVSEIPLPGDHNVENVLAAVAAAWPYCNDVAALRETIRTFTGVHHRLEAVRRLDGRDYVNDSKATNYEAARRALISFRRPLIWIGGGRDKGGDFRELTEAVAAGVRHAVLMGEAGPSFATRLAETGYTATTVVGTLEEAVSTARHLSEPEDVILFSPACTSFDQFNNYEERGDVYKAIVQAL
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis. Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate EC: 6.3.2.9 Subcellular Location: Cytoplasm Sequence Length: 458 Sequence Mass (Da): 49267
A0A6I8PCF8
RFTVPAFRRLPILAPSPHREPPPPVLTPSPHPPVWILGIPTVPGTVTLRKDPQNLIGISIGGGAQYCPCLYIVQVFDNTPAALDGTVAAGDEITGVNGKSVKGKTKVEVAKMIQVVKGEVTIHYNKLQADPKQGKSLDIVLKKVKHRLVENMSSGTADALGLSRAILCNDGLVKRLEELERTAELYKGMTEHTKSLLRAFFELSQTHRAFGDVFSVIGVREPQPAASEAFVKFADAHRNIEKFGIRLLKTIKPMLTDLNTYLNKAIPDTRLTIKKYLDVKFEYLSYCLKVKEMDDEEYSCIALGEPLYRVSTGNYEYRLILRCRQEARTRFAKMRKDVLEKIELLDQKHVQDIVFQLQRFVSTMSKYYDDCYAVLRDADVFPIEVDLARTTLSYGRKDTFTDGADEDEVEVEDEERRRAAAGEAAGGSGRPRDEDGQKLIDDA
Function: Probable adapter protein that bind to and organize the subcellular localization of a variety of membrane proteins containing some PDZ recognition sequence. Involved in the clustering of various receptors, possibly by acting at the receptor internalization level. Plays a role in synaptic plasticity by regulating the trafficking and internalization of AMPA receptors. May be regulated upon PRKCA activation. May regulate ASIC1/ASIC3 channel. Regulates actin polymerization by inhibiting the actin-nucleating activity of the Arp2/3 complex; the function is competitive with nucleation promoting factors and is linked to neuronal morphology regulation and AMPA receptor (AMPAR) endocytosis. Via interaction with the Arp2/3 complex involved in regulation of synaptic plasicity of excitatory synapses and required for spine shrinkage during long-term depression (LTD). Involved in regulation of astrocyte morphology, antagonistic to Arp2/3 complex activator WASL/N-WASP function. Subcellular Location: Cytoplasm Sequence Length: 443 Sequence Mass (Da): 49663 Location Topology: Lipid-anchor
A0A4R1ETK5
MGTLGDTLITKQLGLTDYESVWESMKNFTQSRDQDTPDEIWVVEHPPTFTLGRNGKEHHILQETSIPIVKVDRGGQVTYHGPGQIVIYLLLDLHRRGIGIRQLVTLIENCIVELLSAYEVTAYSDAKAPGVYVDKKKIAALGLRVSKGRTTHGLSLNVDMDLTPFGYINPCGYEGLEIIQCKDLGITDSMPVLSEKLTAIIHAEIMKAAETAKTTD
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2. Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein] EC: 2.3.1.181 Subcellular Location: Cytoplasm Sequence Length: 216 Sequence Mass (Da): 23865
A0A7C5W7R4
MDKRTLLGLLLIAVLTTLWALYTSIYFAPRVPSADTTRPSPAAIAPQPSSSAVLETAPAAPEQWLEVETDLLRIRLSSWGGTLTRWELRRYKDWRGEPVQLVPPGEAELSISYYDAQGRRIELRRFPFVFSLPPNSQYRVAGSDSLVVRARYAIDSLRFVERWYVFYGNRYDIKLGVRLVNLEELVAQRRYELSWSGGLKYQEYNSVDESNSAAALISLAGDVEKLDATKFDEPAETHVTGRIDWAGLKTKYFAIAFVPSPRPAELTVFARGQRFHAPNSGIVERYDLTFRLPYRRGEEQQVFQLYGGPIQYDVLKSYGLTQLVEFGLRWLVRPIGEYFMLPVFKAIHWLIPNYGIAIIVFAVLMKILLHPLILPQLRSAQRMQLLAPELQKIREKYKDDLQAQQRELFRLYQEYGINPMSGCLPMLLQLPILYALWAVLNYSIELRQTPFVLWITDLSVPDRLVQLPFRLPLFGFDYISGLALLMGIALFVQQRLSLTDPRQRWMVYVFPVLLTLLFSAFPAGLNLYYFTFNLLSIAHQLYLTRFRKKPLTLEDLKRQPKREGWLMRRLREAQALAEEQAERLPPSLARRLKLEQHKPTGQHKRKKKRK
Function: Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins. Subcellular Location: Cell membrane Sequence Length: 610 Sequence Mass (Da): 70730 Location Topology: Multi-pass membrane protein
A0A316ZD69
MSTRSRARGHAPRQASEPCISTSALGEGETERTPLLAASTSASHPGLTASSSATSTAANSANDLEARWSRWKSKVARFAQGKRRAREDEEQLEPRLLVSVFDGAGADEAQQEEQGEDGISEKELWHQVSQVRAAIAQGLYPKMITTGSSGSYFARARIAVPRHGSSSKTDAVVTTLAVFKPKDEEPYGNLNPKRLFLRRYFSWAMGRPCLIPNFSAYSEVGASYLDARLALHLVPRTELVSLASPSFHYDYKDRMAHERQGKELPEKLGSWQTFLPGYTNASDFLRAHPWPSRPRALLERDLVAEARAHRKSRKKQGKRVRTCLVGAKHLLLCRQGWQPDEEEEEEERQQQVLPTISEAPTTAPPMQQPGCVEVAGARDVVASFQWNSENMQSFRLELEKLVCLDYLQRNTDRGLDNFMLRPYIDEATGESRVALGAIDNSLAFPHKHPVGIRSYPMGWLYLPVDLIGHPFAPATRTRLIPLLADPKWWSETIEGLRAIFSRDEMFDVKLFERQMNVMRGQGWNLLQALRNPAEGPLELCARQKHVVKQEVLRLSEAELARRSGTLYQLRPDGRPIPMHPAATQPQQPGAGGAPTTAAKAVPLDVKPRPSASGSSSPAGAHPRSLPETMEGVTAAWHSALGQDGAFGSGKQTPAYEGTLGIDVVAQADKVARKARRPSLRKTLTGAVTPSFERTLSSSSIPEEGSVRALKRIPDNEPQSLDAVVLEAALEEDPMASSTPALPSTGGARAARRARSRGMSVSGWSITSERVGAAGAPAPPSEEAGAEEVKVKVVVERLEADDGIAWQAWLGLGA
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP + H(+) EC: 2.7.1.67 Subcellular Location: Cell membrane Sequence Length: 813 Sequence Mass (Da): 88907 Location Topology: Peripheral membrane protein
A0A933PXI8
MSKNVKLVIVLLLFGITLWFLWPTLQWYSFTPKAEKEKTEYSIDTMISKGYTSEQVTQVLKLKRLRSQAVNLGLDLQGGMRVVLEADFDDYAKRLEKSVKEITPEEKSDGMARLLERLRGRIDKFGVSEVGIRRMDDARIIIELPGAKDPDRIMDVIKAKGKLDFMFVDEEATKAISTNDVWLGSFTNYAKVPAGCTNLYFYGKKDEFHRRVRGAPLILKTNIVLAGDMLKEARVGSGEFMEVTVDFELNAQGAEIFGEVTAANIGKQLAIVLDGNVMSAPNIRSEIPGGRGQISGGFDAQEAQDLATILREGALPLSIKIGQQEIVGESIGSDAVKAGVKALIIAIILIVSFMVLRYRISGVIASIAMVINVIMTIAVLAQLQFTLTLPGIAGIILTIGMAVDSNIIMFERIREELRKQQPISEAIHLGFDRAFWAILDSNMTTLISAMVLWSLGSGPVQGFAVTLFFGVLINLFTAVFLMRVIFDVILSMNLIKEKHWLFI
Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA. Subcellular Location: Cell membrane Sequence Length: 503 Sequence Mass (Da): 55705 Location Topology: Multi-pass membrane protein
A0A316ZD86
MASAAPPPRRPSAAVLLLLSAVLLPLLSWLRPAAPGCVLRYGDFHLRFSLPLLALAAAAARPLLTPLDMARLVLLPAIAFVWTTPWDNEIVRQGAWSYPPPCVMARVGWVPVEEYAFFIIQSLLTTLQAVLLLRWLAPTPARAHRPLLFLLPLGVFFLGARFARPGEHSYYAGMIAWWAALPLALLWWGTQGAWMAMPRTHKAMWAAAWLAPSALLCALDRFAIHRGTWHITETTSFNIFPLPDLPIEEMCFFLVTNLILISASLAFDTCALQLRRTHASQTTPLSPSYMPLRASSLAALWTAFVAAPTGPSAADADAEVAERVLSRASASFAAAARLLPWDLRRDLASLYALCRAADDAIDEAPLSAAEQRARLELLHAVGAAAFCQDEAQSDEAARAAVRSATQAYAAAKGSLGAQGLEELRACACACIPLRRLVPLALWQELLRGYAIDVALGGAGGRVFTQPQELLDYAQCVAGVVGEMCVRVVLGRSGAPVPRSLAVSRDVDAAPPREALALLLWQARRMGVALQLVNVARDVVGDARTLRRCYLVFERPEDAWMAPALAAGQLGDGTPSSKGPTAAQLRPHVLALLQRAEGLFASAAPALDDVPSRPARAGLRAACAVYFDIAQVIRHQPREAWERGDRAVVPKWRRAVVALRAVYA
Pathway: Carotenoid biosynthesis; beta-carotene biosynthesis. Catalytic Activity: 2 (2E,6E,10E)-geranylgeranyl diphosphate = 15-cis-phytoene + 2 diphosphate EC: 2.5.1.32 Subcellular Location: Membrane Sequence Length: 663 Sequence Mass (Da): 71697 Location Topology: Multi-pass membrane protein
A0A269TII2
MLFSYLKLKELAGLDNSVTIEDVSKAINSIGFEVESISSFQNVEGIKFGHVLKTYKNPEGDNLTVCEVQFNDQVRIIQTAAKNVVDGAYLMAFVPGSKLKGTTIEARKMKGIVSEGMMVSFAELIPNDTLAREEHKNGILLIDKIDLNLDPIKYYKLDDQIIDIKILTNRSDANSYLVMAQELRAYFQVNQKLENSSNKYELNKNLKVTKNEVENFVLLKTKDKFGITIEEQILLAKNNIKSINDVVDLTNLSLIMTGMPTHVYYEKDLQNVNISNSNDKVEILGNKEVKLDNTLVIKNNNDVISLAGVMGIEKFSVKESKGHNYIFEFGIFDNKAIRKSMNTIKLESNAGRQSAKEISKGTMNLAIIFVANKFNNDVLISENLELKNKSLKFKIEDVYYYLSDNQKYDFKDAIKSLEILGFEFKNNEVIIPTYRHDIENTQDMVEEILRFYGYEKIVANAPKVAPFSIQEDIDNFLDVVPSLGYQEVKTYSLISKEKNIFNPFKFTKEMVLQTFVSKEREVVRNSLISSFLGVIDYNVKRKMDNVSIFEIGIVNNSKRVMALASNQSSFLKLKNDLIRIFRNYDLVFEHQKDVLDFANKIENLIIKSNNKVVGYIARLDASISEYDVVIAEILIDEITPKKYSKNSFDLSKQLKVYDVNFELELNQNSKVIETKITSLEKIFDYKIISEFEKEGKKIITVRIYSEEDYSSLLLKTN
Catalytic Activity: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe) EC: 6.1.1.20 Subcellular Location: Cytoplasm Sequence Length: 717 Sequence Mass (Da): 82097
A0A0E0B6B3
MLAELAGSPGVDAVVFTVFTPSLMFASLAKTVTLSDVISWWFMPVNIGITFIVGGTLGWIAFCDEDGNPFGKDRSLCRSRGLSYSSLSMALGGLFIWTHTYSLMQKAGKMYHKMQFKSIQCPADSDEEHHPAQGHDQVKLDGETAYADEEAALLVSAKLAPEHNEENQMEAPLLTCEREIANKGGFWTNLKETVHQVVEELMAPPTVSAILGFVVGLVPWLKSLVIGNGAPLRVIQESLQLMGNGTIPCITLILGGNLTQGLRKSVLKRTVIITIVCIRYVIQPLIGMAVVHAAYGVGFLPHDPLYRYVLMMQFALPPAMNIGTMAQFVDLPVCCHCAYDVVDDIHVHPVLRLRVTIKKNRICGNIQLTDC
Function: Involved in cellular auxin homeostasis by regulating auxin metabolism. Regulates intracellular auxin accumulation at the endoplasmic reticulum and thus auxin availability for nuclear auxin signaling. Subcellular Location: Membrane Sequence Length: 371 Sequence Mass (Da): 40670 Location Topology: Multi-pass membrane protein
A0A269TIL4
MLITLEGLDGSGKTTIANSIFNELVGLGLEKNFIFTREPGGAGIIEAEKIREVILDSHSRLSNISEALLYSASRRIHIDRVIEPNYENKIIICDRYIDSFYAYQGYGRELGIKWTKDLTELVIGKYKPDLTIFIDITYEETRNRREKRETTDRLETQSQDFYKRTYEGYWKLINEDRERFLVIDGKLSVEEIVKIIMDKIKTLDKFKKMGK
Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis. EC: 2.7.4.9 Catalytic Activity: ATP + dTMP = ADP + dTDP Sequence Length: 211 Sequence Mass (Da): 24663
A0A8U8BXK5
MEQRRSVGQEKSGGKSVGQEGSVGGSMGQEGSEGGEGSPLQLQVEVMVREGRALAVLGWWELLRGLLVFALCSHPRLQQDPEAFLRASRRVLGARLWRALLSVSLWGQFAVGRSPAAVQELGQRLRARGLRPLLALPIEGEGPDGEG
Function: Converts proline to delta-1-pyrroline-5-carboxylate. EC: 1.5.5.2 Catalytic Activity: a quinone + L-proline = (S)-1-pyrroline-5-carboxylate + a quinol + H(+) Sequence Length: 147 Sequence Mass (Da): 15780
A0A0Q5GAL6
MPIQETLETSHTFLARLASEAAAFLPNLIAAILILAVGLFLAGRLANLVTRAFGVSTKVDQTVREPLVAIVRYVVVILTLIIALGQVGVQMTSLLAVLGAAGLAVGLALQGTLTNIAAGIMLLWLRPFRVGDYIETQTFAGRVHQIGLFVSHLETFDGLFVFAPNSTLWNVWMRNHSRAASRLLAWAVTVPRDMPFEAARQALIEAWQQESADGRLSEPVAFLDQLTVDAQILVLRGRVTEGETATAQRRIAEAIRTRFLQRFGEGQEPRAIQRIVPADNDPSRYLGQDEAPAANPTLVNDRPETPSQGVVTTARG
Function: Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens conductance with a slight preference for anions. Subcellular Location: Cell inner membrane Sequence Length: 316 Sequence Mass (Da): 34365 Location Topology: Multi-pass membrane protein
A0A971GK46
MPSAVAEVKKTILLVEDEFLIAMMESRDLEAGGYYVIHAADGPEAVAVIHEKGEAIDLVLMDIDLGPGMDGTDAARQILEIRDLPVIFLSSHTEMEIVRKTEEITSYGYVVKNSGVTVLLASIRMAFRLFEANRKIFLKNNEILRASSRLMELNEELLRSRNSIAESEERYKRIFESFIDIYYRVDASGIITEVSPSVEELSGWSMGEVIGRSVRDVYLEPADRELFLSAIAREGRINGYEVAFKRRDGQVIPISIHAKLIFDKNGAPAGIEGTLRDISGRKRTEDMFYRTFEKYRMLVDNSVDMIWTMDTSGIITYVSPAWEKVLGYSPDYTTGKDFRVFLHPDDEPWCSGLILRGISSGERIKSPPYRLRNSDGTYRWHEAHGVAVYGRDGVSHLIVGISRDIHERKIDSDLLAAAKEASDSASLAKSEFIAKMSHEIRTPLNGVAGFTGLLCDSGLAGEQKGYAENAYLSAMCLLDLVDGIIDFSRIEAGMVEIEEAETDIPLLLENIREMTGYAAGVKGVEFRLEHDRGMPRYATVDAMRLRRVLINLAGNALRSACSGTVQLSAGFTPAGEESGLFRFSVSDAVQPVNCEAGSSIFSPFRQFEADGERACGGAGIGLDIAASLLESMGSSLNLVSDPERGRCFYFELRRPCRNVPVRSAESESPGFAAGEGGSRSFTPLEGNYTILIAEDNEINLELAKAFIKRLAPSAVIVEARDGAEALGAWKDRGADIIFMDVQMPVMDGYAVTAGIRELEKQSGIYTPVIALTAGAVSGEREKCLDSGMDDCIVKPADLRKLSALLVKYLVPGSGAAIPPENAAGSAPSFNYVELLNRLGGDDRLLSDMLAISGKYFGGYVSDLMDAVSAGDHKRISRQLHLLKGAALNACFSRLAELVCEFEKSMPSDDGIMKRFAQAIEDEYGHVKDEIAASGLAGGSYGFK
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. EC: 2.7.13.3 Subcellular Location: Cell inner membrane Sequence Length: 943 Sequence Mass (Da): 103131 Location Topology: Multi-pass membrane protein
A0A4R5TJH7
MNRLFPRFAITCVVAMALSACATQPRRPAGPADEAAARMHDQQRAAITGWQLSGRLAVSSGSQGGSGRIEWSQDGDRYVISLSAPVTRQSWRLTGDPTGARLEGVEGGPLEGDDSERMLLAATGWRIPVRAMVAWVRGIAASEDMAAPARVVHGADNLPASLEQLGWRIDYRDWHPAATDRPALPRRMDVVDAARGDARVRLIVDQWQVTQAQAVQPGIGIEMLDAAGELAAALARLDLEDPAADLRRQVAGGDLRPLVVCGFACLAPGDPEGVLPEGEVRILDGSGDVVLGDRHLRLKHKAEAYARAYNQALVAWHTEAEGAPVARPGRVD
Function: Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. Subcellular Location: Cell outer membrane Sequence Length: 332 Sequence Mass (Da): 35554 Location Topology: Lipid-anchor
A0A4P5US73
MFDIGGAEFLMIGLAILLLFGPKKIPEVMHSIGKGIRYFRKAQEDLKSQIRDISTEVEKQTNITNTVINESSSQIQIDTTIVESETQTISIRPAEGSLARNVHIDEIQEDSTHISDPNPQKTLEQGE
Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system. Subcellular Location: Cell membrane Sequence Length: 127 Sequence Mass (Da): 14165 Location Topology: Single-pass membrane protein
A0A9E7JYE9
MITCWQLGLRNLPLQKTRRRLGGGDVPLLPVPSLWSHALLIVDYIHFQYNGWLRPRLSPLFRLSVLEEGKDVAGGLILPGPICFFHHFFVHLLRHHCRRGPWEASRRFPTMGTAMSTVSSRRSVHSCSMSRFVLIVQFVHTRMPMVAHDDQEMDKVHNRYKKTEKQVHSCLFPFGRGYACRQVSAFWVPCIVLDKALAFVLAKLELDVPAPKASSRRAGFSRYLKIQSAPQGNQTECFKCFRCKTRIYQTIWNALPSGIVGGVLRSATAPIYSMGSGS
Pathway: Protein modification; protein glycosylation. EC: 2.4.1.- Subcellular Location: Endoplasmic reticulum membrane Sequence Length: 278 Sequence Mass (Da): 31540 Location Topology: Multi-pass membrane protein
A0A0B5I1P0
MKELFDDYKDKLPTVVLEEIEALAESRNLNKTQVKKVIELAYEEYRNSMIEPGESVGLISAQSVGEPGTQMTLNTFHFAGVAEFNVTVGLPRIIEILDGRKNISTPMMEIYLVEPYSKGKDIKTIAESIKQTQFKDIVKEINLDITEATLEIKIDFEKMKRLGLNEAKLGKVLEKSLKGFTLKLKDDTLTLKSKGKQDNIAELYKLKEKIKSVYVSGIKGILQVLPVKREDEFVIVTAGSNLKDVMKLEYVDKTRTTTNDIFEIQALFGIEAARQAVINEVYNVIENQGLNVDIRHIMLIADVMSFSGKVRGITRYGVVSDKSSVLARASFETPIKHMVEAALTGEVDPLTSVVENVMINQAIPVGTGLPELISKVK
Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Forms part of the jaw domain. Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1) EC: 2.7.7.6 Subcellular Location: Cytoplasm Sequence Length: 377 Sequence Mass (Da): 42059
A0A0A8UQ96
MAEIQIKVPDIGGSTDVDVIEVMVKPGDEISSNASLITLESDKASMEIPSPQAGKIKSLQVKVGDKVSEGDVILTLIVDEAESTKSAPESTEVTKQDESEKPKAQESKQTKATSASQRLEVRIPDIGGATDVDVIEIMVTVGQSIEKDQSLITLEGDKATMDIPSPAAGVVENVSVKVGDKVSQNSLVLILKTEQGDIAAEETPTAAEKIESDQEQPREKQASTEVVAVHTLPESTVGSNIPAGPAVRRMAREFGINLAEVKGSGRKARITKEDLQAYVKGRLSEKPATGGFALPTAPVIDFSKFGDIETKPLNKIKRLTGLNVHRSWITIPHVTQFDEADITDLEAFRKSSSEDASLTGYKLTMLAFVTKVVGKALAVYPQFNASLDASGENLIYKKYCNIGIAVETPNGLVVPVIRNVDRLSVAEIAIEMGKLSAKAREKGLMPADMSGGCFTISSLGGIGGTAFTPIVNSPEVAILGLSRSSIKPVYQNGEFKPRLMLPLSLSYDHRVIDGAEAARFTRFIAEALGDIRRILL
Cofactor: Binds 2 lipoyl cofactors covalently. Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3). EC: 2.3.1.12 Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + acetyl-CoA = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[protein] + CoA Sequence Length: 536 Sequence Mass (Da): 57353
A0A1D8TF41
MKKPFGLLMIITLFIGCSHYIPQSESLTTADDGNKDTFLDIAIKMGKEIGQDFQNVFRFGKNIIRNMLGEPTTIDSNDNRSKIKEHLSTMAKGLTNIKNELNNKASQEENTTKEANEVIDKIIAAINKIAEATDTNIGIGETKNDNKKKASIISNKQSVQSIINGIKEIVDIAKTSGVQIEKKDDDNTSISASSNTAATAALNGGGLYNAGAGQGSGAALAKVVSEADPWIMIDKIINASIASGSIHGNDNNNAGQLITGTTSEDKGAGSKSKADLAAAVALKAMSKGGQFAAYKTDNNNEEYVKKVKEAASEAVNKVLKVLNVIILQTLEAQLGKVAIKH
Function: The Vlp and Vsp proteins are antigenically distinct proteins, only one vlp or vsp gene is transcriptionally active at any one time. Switching between these genes is a mechanism of host immune response evasion. Subcellular Location: Cell outer membrane Sequence Length: 341 Sequence Mass (Da): 36166 Location Topology: Lipid-anchor
F6UT00
MEMMAGRGEVDHPVNMLPVDGKGDESRPDAAPSLPVPECAICLQTCVHPVSLPCKHVFCYLCVKGASWLGKRCALCRQEIPEDFLDRPTLLSPEELKAAGRGNGEYAWYYEGRNGWWQYDERTSRELEDAFSRGKKSTEMLIAGFLYVADLENMMQYRRNEHGRRRKIKRDVVDIPKKGVAGLRLDCEPNGVSPARESSADGADGTSARGGAPPPPPAPSPAPSRPPTALDGPPPGPAAPSPAAGAGLEDSLAHLQLGGDGPGGRGPRGEGEEGREAPLPAGLPPPDAAARDGESDGDDGAAAPARRPSARRRLANPSGTQAAERPAAGGGGGGAGGRARRPDGQCTVTEV
PTM: Ubiquitinated; autoubiquitinated. Pathway: Protein modification; protein ubiquitination. Function: E3 ubiquitin-protein ligase that specifically binds poly-ADP-ribosylated proteins and mediates their ubiquitination and subsequent degradation. EC: 2.3.2.27 Subcellular Location: Cytoplasm Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine. Sequence Length: 351 Domain: The WWE domain mediates non-covalent poly(ADP-ribose)-binding. Sequence Mass (Da): 36784
K8ZQJ0
MESIPITYDYYAREEWANLNHQKMAIPLSEEELQILISTQDQLNLQDIQEIYLPLLHYLTLIYEEYRSLQQKRASFLQKRNTSIPFIIGIAGSVAVGKSTLARVLQVLLERIYGLSVSLVTTDGFLYSKSELEQKGLLDRKGFPESYDMPKLLHFLEELKVGKKEVHAPIYSHEKYDIIPDEVITICEPDIVIVEGINVLQNPWNERIYISDFFDFSIYLDAEIFRIQQWYCDRFLLLRGNEFATKEEAIRIATKVWKSINEKNLLEYILPTKYRADLILHKTKSHFMDYILLKK
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5. Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+) EC: 2.7.1.33 Subcellular Location: Cytoplasm Sequence Length: 295 Sequence Mass (Da): 34693
A0A4R1ET05
MKPRHKRLAFVLLALISVGAASALISKAMKGNLAYLHSPEEVLNGVVPTGQVFRLGGLVKEGSLERSDSKLEARFIVRDNRDHEITVVTNKILPDLFKEGKSQVSRGKMGEDGLFYADEVLAKHDSEYMPQELKDTLEKEHTVNASEGTK
Function: Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH. Subcellular Location: Cell membrane Sequence Length: 150 Sequence Mass (Da): 16589 Location Topology: Single-pass type II membrane protein
A0A9E7EN21
METPFASPKIRLASEFTAFIRLGFFFKISRANPRFFLTLAKLQDGEPTNLMIVDVGEEKQAKLAGSETLTRSSSSDRVNSPPPEHEEEEESQQTQPLRQQGLPPHKVARVSSDEVTMAAPSSLMLGLGLGLGRGPGAAKPVFTFMQLQELEHQALIYKYMAAGLPVPVHLVLPIWKSVAASSFGPYVYPSCSTPPS
Function: Transcription activator. Subcellular Location: Nucleus Sequence Length: 196 Domain: The QLQ domain and WRC domain may be involved in protein-protein interaction and DNA-binding, respectively. Sequence Mass (Da): 21385
A0A1L5KGR0
MAVLQVLHIPDERLRKVAEPVKEVNAEIQRIVDDMFDTMYAEEGIGLAATQVDIHQRIIVIDVSENREERLVLINPELLEKDGETGIEEGCLSIPEQRALVPRAETVKIRALDREGKTFELESDGLVGYLYPA
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. EC: 3.5.1.88 Catalytic Activity: H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide] Sequence Length: 133 Sequence Mass (Da): 14995
A0A660TTK8
MKVAVFGASGYGGQILMRLLLDHPEVSKVLPVSSTSAGKPVDGRDSGLGPDLKGKLPEGRTFLSREEALEEKPDAVFSALPHGASAEFCEPFFGKSVVFDLSADFRLRDEKVHLQAYGAPAPYPELRSAAVYGLSEIYETQIRKSDLIAVPGCYPTCSMLPLIPLGREGLITSTITINSLSGISGAGRSAKEASLFVERSENSVAYNPGLKHRHLPEMIQEFNAAGGNSPIFFTPHLAPMRRGMLSTISTSVTGEPKAVFNKVEAALTAAYQGQPFINLTGNRIPSTRDVVGSNRCDIGWTVEGPINGSSMLYLFSTIDNLVKGASGQAVQDFNIRFGFPQETGLPLRGEV
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4. Function: Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde. Catalytic Activity: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH EC: 1.2.1.38 Subcellular Location: Cytoplasm Sequence Length: 351 Sequence Mass (Da): 37623
A0A345UHS8
MIPPGFENRLFTAAQSRDIDRRTIEELGIPGFTLMEVAAQRAADHIFEMQPGPVRVLSFCGKGNNAGDALAVSRLLLMKGFSVDVCLALGKTGMSADAAANLRILEKMLEADPELPLRFFEGVLPGRVYCTVIDGLFGTGLQRDVTGPLAEMIAEINRWQARVFAMDIPSGLHADSGAVMGTALQAHTTLMFGTAKAGCYLGRGAALSGKRVLCPLPFPAHLLREAEGAVLRSLSPGGKPQLENKLRKLREGREVRHKYQNGNVYVLGGSPGLTGAVILTAKAAWSTGCGSVQVFTTPEVSPAYDAHFVDITRKMIPGDGSGLFKADAVRAVAEVIAARPGVLVLGPGLGTHPETAAAVRQLLRLVKAPVVLDADGVRALSGHTEKLPDDLRLIVTPHPGEQEQLLGFSIAQPEQLAQALNHFPCRDNMVFLAKGSPALLATRNECRITTYDTRIFSRTGFGDVLAGLMAGMLSRLPDSTVTAESMLDVSALAMLESYARATCQHESAVSPSAPEAGGMF
Cofactor: Binds 1 potassium ion per subunit. Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalytic Activity: (6R)-NADHX = (6S)-NADHX Sequence Length: 520 Sequence Mass (Da): 55274
A0A159U821
FIFGMWAGMMGLSMSLIIRLELGNPGSLIGNDQIYNSIVTTHAFTMIFFFVMPVMMGGFGNYLIPLILGAPDMAFPRMNNMSFWLLPPSLMLLILSMFVGSGTGTGWTVYPPLSSNLSHSSSSVDLSIFSLHIAGISSIMGSINFISTVFNMKIHKIENIPLLAWAMLLTAILLLLSLPVLAGAITML
Pathway: Energy metabolism; oxidative phosphorylation. Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O EC: 7.1.1.9 Subcellular Location: Mitochondrion inner membrane Sequence Length: 188 Sequence Mass (Da): 20412 Location Topology: Multi-pass membrane protein
A0A660TDD6
MNREAGKFFPVSDASVRAGGTFVSYKNSDPDIVSISIDSRTVSSGGLFIALNGEITDGHKYISSAFESGASAAMISSKYYAKHYNNVSFFNGCLIVVEDTLSGFHKLAASWVADFGKLTRVAVTGSNGKSTTKEMIGSILAEDGSTVINKGNLNSETGLPLSVMGIKKEHKYGVFEMGINHPGEMKALVSVFSPQFALVTNIGTAHIGPMGSQEAIAAEKSEIFSLFDKDNTGFIPDNDSWADYMETHCPGKTIRYGLNSTEGVEKAFNLGLKGWNIQYKNLEINLKLVGQHNLNNAIASISLSSALGIIPDKIKKGLEKIEPLKGRSQIIEGLYTIIEDSYNANADSMKEIFQFISDLEWDGRVALVLGSMKELGDESVQMHRLVGTMAAELNPDVIFLFGLEMRDAYFAIQESDYSGQVVHILDYQKLENLVLDSLIEGDLVLLKGSRTMELNRLADEISKLMGVLGV
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis. Function: Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein. Catalytic Activity: ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine EC: 6.3.2.10 Subcellular Location: Cytoplasm Sequence Length: 470 Sequence Mass (Da): 51135
A0A9E7JKC3
MVFDQMQRFVAPDVYSYTILIDALCKRRNVEEAMALFSDMERSGISASIVTYNALIDGLCKRNMLKEAFALKEKMVRISINPSIVTFGILINGLVKLDRFGDVELVLTEMEEIGIPPNVVIYNTLIYGHCKMGRPTEALKLRDKMVAKGIEPNCVTYNIIVQGLCDAGDMKQAEYILDEILSNGMEVNAGLFGSIIFWLVTKEQRLDCAVRLLGEMLLRNLRPNDSLLTTLIVELCRMEEAIGLLNQLKDEDLVPDLFTCSMIIDGYCKVKEIDKAKSFLKEMRTWGLEANVVVYNSLVSGFCKNGNITGASNLVDEMKSNGILPNFVTYSSLMHGFCCTGYLEEAKRIFELMKENGMGLNVVTYTTLIAGYCRSGQMDEAIKVYKAMCVAGVTPNKFTYTVLIQGYAKMGNLEAASKLLDEMVNNGIVPDAVTYNVLMSEFCKEVCLVTTPIATDGWYCNYQFDCSPSTFTIFSFGVTRSRVIQGVISCVAIGLWADLVIGFVTEYYTRNAYGTIQDGADSCRAGAATNVIFGLALGYKSVIVPNFATAVSIFVRFSLGAMYGIAVAALGMLSSIATGPVIDAYGLTSDNIAGGIAQMDGTSHRIQERTDALDTAGNTTAALGRGGNLCLGDSDKNNLDSSFGKTATHKFQALQLIQLPWSLLQSSSYFHCGCSDTKGLQWVDCWCDASLLVLSHDHEECRQCSSEEGGGGALVMLTPLIIGILFVMETLSGVLAGSLVSGVQIVIRSSSNIGGAWDNAKKYIEAGALDHARSLGPKESVPHKAAVICGTIGDPLKDMSGSSPVKLMAVEFLVLAPFFATNEEVSSFSLLKLRIGGSLQDKVIFNTGNPQQPCLVSLKDAYPCPDGAHIIFGSNALDGKVPPSDDDGSLGPSNYTNACCGNGATIILAGSCSAAGSVGLISSSCCRICCTSGLAAGARSTQCRANFRVFSSSSPAAVPAASSSAPGRTPHWSTPLTIEATQCGKSMPFVTSAGDLPVRSSSMTTPRL
EC: 7.1.3.1 Subcellular Location: Membrane Sequence Length: 1008 Sequence Mass (Da): 108160 Location Topology: Multi-pass membrane protein
A0A923XTY8
MNDEQKSGEYYSFKVDNSQELMRIDFYLLNKIRYATRNKIQKAAKENKVLVNNVPVKQSYRVKPNDNITILINEPKRNKEILPENILLNIIYEDDFLIVIDKPAGMVVHPAFNNYSGTLLNALEYHFNQTNNSKERLVKSGLVHRLDKNTSGLMIIAKEKETLDNLLKQFFYHSIERIYQTLVWGNINLKKGKIITNLEKDSKNKNIKVSITGKQAITNYLVLEDFYNSSLIECKLETGRTHQIRSHLAYIGHPIIFDDLYNNVENNQIFQKINLQVSNTLDRQALHSSSIKFIHPKLKKELFFQSPLPNDIKNTIEYLKSISFDM
Function: Responsible for synthesis of pseudouridine from uracil. EC: 5.4.99.- Catalytic Activity: a uridine in RNA = a pseudouridine in RNA Sequence Length: 326 Sequence Mass (Da): 37998
A0A7V5SGP4
MNIAVTYVSGAGNTFTLVREGRRRFPVEVWQRLAPQLCRWTDGLLVLRKADARGVVPVLFFNPDGSTGMLCGNGARCAASIAMGERHRELTLLFADMPISAVAVEGGIRLRLPPPRIFPQERQLRLPTGDLRLWFADVGAPHVVIPIHELSSTGIHSSLEQLPVEQLGRLLRFHPAFAPTGVNVSFYTIAEDGSIQVRTYERGVEQETQACGTAAMAVALTAWSAERLHPPITILPPSRSPLRVDWEGEAPEQLQALFLEGSVEVLGTDTVEVSLEEDE
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1. Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan. Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate EC: 5.1.1.7 Subcellular Location: Cytoplasm Sequence Length: 279 Sequence Mass (Da): 30608
A0A1F4CYV6
MAEVRPVLAAASLARPKGERAAARREHWQKVAIAACEQCGRNRIPQVHALVPVEQYVLKENSSQKILLSPRAELRFSEACRTLGESLTLAAGPEAGFSAAEEAALLDCGFVPASLGPRVLRTETAALAALAALNALRGDF
Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit. Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine EC: 2.1.1.193 Subcellular Location: Cytoplasm Sequence Length: 140 Sequence Mass (Da): 14873
A0A7C5S5V5
MPVVSPYGRDNAAVLFGLAAIAALVGGSLGGIASWIGGVVAGALVGLTLWFFRDPDRAIPAEAQRDGVVLSPADGRVVQIVRLQEPEFLGEEAVQVSIFLSPLDVHVNRVPVSGIVRFLRYVPGRFFAAYRPEASRQNEQTLIGVETPCGKVLFKQIAGVLARRIVCTLQEGQRVQAGERFGMMKFGSRMDVLLPALRAELCVREGMRVWAGQTILGYLIPESAGLSQRDT
PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. Cofactor: Binds 1 pyruvoyl group covalently per subunit. Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2. Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). EC: 4.1.1.65 Subcellular Location: Cell membrane Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2 Sequence Length: 231 Sequence Mass (Da): 24960 Location Topology: Peripheral membrane protein
A0A7H8PWW5
MNNIDSNHYGDSFSSEEFVDLRKYFSILWSYKFPIVTVGLIAGILAAGFMWLQPKQYQATSTISFASGRANIVQIREIVETGNENRDYLQTQAEVIRSRQLASRVVERLQLTKASFDAPPNAITSLFELNGPTKPASELDSDAAMQQADQAAQESSETVPVSDARTSELTPEEVVSANSAPTSALLVNMLIKNLSVELVRGTQLITISVVTHSSELSAEIANTLAEEYLASQLEQKRDVASEATDWLGERLDVLRTNLEESEQTLLAFQRAENLVDVDGVRGLAAQELNEVTTQLLVAKRQLQQVSTSYQLVRRRGDDTEALASLPQIQEQPTILALRQQVSDIRRQISDLQLRYGAKHPRMIAAVNELDSANNALADEITGIVSVIVGQYEAAQANVNALEAELQRVKDDFQELSRKEIQFEELKRQVEINRELYDTFLTRASETSQGTGFDKGNARITDPAVPPLEPLDNKFNLIVFAVVIGSVLLSSVFVLIYEMVQDSIRNPDDVELVLKQKMFGLIPLHKQNNTESNFSARSYFDETYFQYAESIKTLRTSLVLSHLDTPAKIIALTSSVPSEGKTTVSTSLAFALAQNERVLLIDADLRRPSVGKTFGFATKVPGLTNLIAGTHKATECVHRDDASGLDVMPSGPIPPDAQQLLNSLRFSNTVKLLSKQYDRIVIDTAPVNAVSDALMISRISDATLFVVKSGSTRRKVILRGIERLTQVGINIDGIILNQVDVNSRFARSEEFYGYYGGQYGYGQSTDDRSESLAAPRSVKLETV
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein] Subcellular Location: Cell inner membrane Sequence Length: 782 Sequence Mass (Da): 86395 Location Topology: Multi-pass membrane protein
A0A1I7YFW1
MFILQTSIPQVSILQTSILCNVCSWQRPGALSLLRRQQIVNAFALELSEIRTSLQLISFLPFNGCFVFFLTAFCSHKYFSNFTLRQKRHSLSLSLKFAMIHFLHVSCLKRPFALRFLIGSVFSLRPPPSDMKRIKLTNRCVFVGIFLAVVSITIAILIFFSAPYRESSPDMEKTLYIMKTALNKANCLDHFWSRTGLXXXPLFSRTGPPLKCDEDVDLLVGVISLPSDFELRRTIRRTWADQSRYDTRRTRVLFFLGRQKNVSIEKEMDTYGDIIPITNDESYYNLTLKTYALLTYHQDYCGQAKCVLKVDTDVVANLAGLEELCRQNAETPLITGGSALIWARVDRNVSSKNYVPRFIYNAESFPPYAGGPAYLYSGAKVSSLVLDALRKTPFHQSENFRRLPEDVVFNGIARSLAEIPVAANNGFTIYKDQDLGYWCPSDRSPLPLIRHGAEPLEEHWRSFKGAIVDAKNSSWPGRVLRCRFR
EC: 2.4.1.- Subcellular Location: Golgi apparatus membrane Sequence Length: 485 Sequence Mass (Da): 55303 Location Topology: Single-pass type II membrane protein
A0A1C9EYM1
WSGMVGTSLSVIIRTELGHPGALIGNDQIYNVVVTAXAFIMIFFMVMPIMIGGFGNWLVPLMLGAXDMAFPRMNNMSFWLLPPXLTLLLSSSLVEAGAGTGWTVYPPLSSTIAHAGSSVDLAIFSLHLXGISSILGAINFITTIINMRAPGITFDRLPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNLNTSFFDP
Pathway: Energy metabolism; oxidative phosphorylation. Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O EC: 7.1.1.9 Subcellular Location: Mitochondrion inner membrane Sequence Length: 198 Sequence Mass (Da): 21256 Location Topology: Multi-pass membrane protein
K2A4M4
MHLTGYKFENTFWRKGLSVAGADEVGRGSFAGPVVASAVAFAPHSCYRASLLKQKIRIDDSKKLSVGQRECADSWIKASCIGYGIGVGSVGLINRAGIVKATNFAFRSAIKKFTISCMLSIDYLLIDGFYVPNVANIRKSKQIPIIRGDAKSMTIAAASIIAKVYRDSLMVALNEEHPEYFWYHNKGYGTVDHIKSLERFGPTKHHRKLFIRNYI
Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding. Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. EC: 3.1.26.4 Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester. Sequence Length: 215 Sequence Mass (Da): 23912
A0A496QR17
MGTNMINDYFDHVSGNDELNRNFVRPFSGGSRMIQLGLLTPPEALTASLVCFFLGSLVGIYLVWTRGPLILILGIVGVISGFFYSAPPFKFANRGIGELIIGLNFGLLMAVGSYYVQVQSFDAELVFVALPVMFLITAVVYINEFPDYEADRAVSETTMVVLLGRRRAVTGYVVIMTLAYLSIILSVTGGMISPHALLGLISLPLAVKAVDYLRHYYEKPFDLVPANVSTIMAHLITGTLLISAYIIERLGLKAVVALLPLAIVTVMVIVWLHRHIENQRRTFEGIRKAT
Pathway: Quinol/quinone metabolism; menaquinone biosynthesis. Subcellular Location: Membrane Sequence Length: 290 Sequence Mass (Da): 31930 Location Topology: Multi-pass membrane protein
A0A1L5KXW7
MNLFQAIVLGIVQALTEYLPVSSSAHIRIVGDLMLGSDPGAAFTAIIQIGTELAVILYFRHDIANILTHWFACLFGKNGKDWKARMGRGDNYATLGWNIIVGSIPIVILGFTLQNVIETTLRNLWITATVLLLFGILLWVVDARAKQTKTMDDMTYRDAFLFGLGQSMALIPGVSRSGGTITVGRALGYGP
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate EC: 3.6.1.27 Subcellular Location: Membrane Sequence Length: 191 Sequence Mass (Da): 20801 Location Topology: Multi-pass membrane protein
A0A2N9MNS5
MRRRVAVKLVKAGMNTREVIARFESERQALALMEHPAIARVFDAGATPEGAPYFVMEYVAGVPITTYCDSHRLSTRERLELFMQVCQGVQHAHQKAIIHRDLKPSNVLVMEVDGKPAPKIIDFGVAKALTQKLTADTMFTRLGALIGTPEYMSPEQARSSGEDIDTRTDVYSLGIILYELLAGVPPLDLRKIAFEEFLRRLREEEPPKPSTKIRTQDEATSTEVAHKRQTEPLALAKQIRGDLDSIALKALEKDRSRRYGSPSDFAADIARYLNNEPVTAVSPSFGYRAGKFVRRYRVALATICAFVLVLVAAAAISIRQSLRANSEAAVANAVTDFLQHDLLAQASAATQSGPNTKPDPDLKVRTVLDWAAARIAGKFDHQPEVEAVVRDTIGQTYIDLGQFPEARKQLERALEVERRALGAEHPKTLRTMSRLGCLMYLQGKNPEAEALLDRTLKVQRRVIGPEHPDTLKSMYYLAITYEEQSKFPQAESLESQTLEIQRRVLGPEHLDTTASMGELASIYHELGKYPQAEALDSQALEIQRRVLGPEHPRTLATMTSLGIDYQRENKYAQAEALDRQTLEIRRRVQGPEHPDTVSEMGNLASVYDEQGKYAQADPLHRQTLEIDRRVLGSEHPLTLAAANNLALVYHDEGKYAQAEALQNEVLEIRRRTLGSEHTRTLSSMGNLAETFASQGKYGQAEILFKQTLEIQRRVLGPEHPRTILTVSNLANMYQRQSKFVLAQAYASQALEARRHTLGSEHPDTSNSAGYLALAYQSQGKFAESERLAREAVEIDRKKRPDDWRRFRSESLLGASLAGQREYAEAEPLLLEGYEGMATRKEMIGVPDSYYLDLAREWTAELYQAWGKPQKAAEWRQKPQPKASPKQ
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] EC: 2.7.11.1 Subcellular Location: Cytoplasm Sequence Length: 886 Sequence Mass (Da): 99373