Datasets:
Synthyra
/
TremblNLP

Dataset card Data Studio Files Community
1
ids
stringlengths
6
10
seqs
stringlengths
16
1.02k
texts
stringlengths
117
4.4k
A0A076N8C4
MGQGMATRAEGAPDLVITGTVVLDHWGVVKADIGVRDGRIVGIGKAGNPDTMDGVDPALVIGPATEVLSGNGKILTAGGVDCHVHFICPQLVDTALASGLTTLVGGGTGPSEGTKATTVTPGPWNLARMLQAMDGQPVNVLLLGKGNTVRPEALREQLVAGAGGFKLHEDWGTTPAAIDACLSVADESGVQVAIHTDTLNEAGFLESTMDAVAGRSINAYHTEGAGGGHAPDIIKVAGLPNFLPSSTNPTRPHTVNTLDEHLDMLMVCHHLNPSVPEDLAFAESRITPEHHRGRGRAARPRRHLDDELGLAGDGPDRRGDHPHLADRARDETPPWSTARRRRRGQPAGPSLCRQVHDQPGHRARDGRRDRLGRGRQARRPGVVGAQVLRREAARGAEGRVRRVGRDGRRERVHPDPAAGARAAHVRRRAVRGRGEQPVRRAASARHRTSGDPAAGAGAQRAPRDEGRHGAQRRAAGHPGRCGQLRGARGRRADRAAAGAHGPAVLPVLMGISAILLADSRFPGGGHVHSGGLEEAVARGLIREVRDLPGFLHGRVWTAGYLAAAFAAASVVCRQWTRLDEELDARTPSPAQRAASRAQGRGTARAGRIAWPSPVIDELLTATPRPHHPIITGALTAVSGGTPRDAALAVAYLAVSGPASAAVRLPSPGITGARPARRSTPAPPAGRGASLCQLNTDTGTATCTRSTSTRRPPNPTATRRRRPAAGPSASASAGRSAAARSR
PTM: Carbamylation allows a single lysine to coordinate two nickel ions. Pathway: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1. EC: 3.5.1.5 Subcellular Location: Cytoplasm Sequence Length: 741 Sequence Mass (Da): 77391
A0A8J4YU60
MAKLPISIQAMEASCCVTVLPRKKRIVYSSWIWVLTFMIYCSYHLSRKPISVVKNVLHQNCSSLTPPENVNASVDPTWCDWKPFDGANAPTLLSTVDSSFLFAYAFGMFLSGIVAERVDLRLFLSFGMVLSGLFCAMFGLGYILKIHNIGYYIAAQVMCGLVQTTGWPGVVSCLGNWFGKGKRGLIMGIWNSHTSLGNILGTLIAASFVTYNWGLSFIVPGLIIAGLGVVVFFFMVPEPAMVGLPNPNKKMELEGTSSPHTRRRQMVGEFADTSDEERASLMANESPAIYDDKIKVVCVEAQESKEEKAIGFLEALKIPGVIEFSFCLFFAKLVSYTFLYWLPNYILYQTNYGPEESANLSTFFDMGAIIGGIMAGLVSDYTGMPAATCSIMLIAAIPMMYVYQTFCTVSLGINIFLLVVVGILVNGPYSLITTAVSADLGTHQSLNGNAKALATVSAVIDGTGSIGAALGPQIAGPISSYGWQYVFDMLMVSDVLALLLLTRLVLREIQRWRIRRREAAPARL
Catalytic Activity: D-glucose 6-phosphate(in) + phosphate(out) = D-glucose 6-phosphate(out) + phosphate(in) Subcellular Location: Membrane Sequence Length: 524 Sequence Mass (Da): 57304 Location Topology: Multi-pass membrane protein
A0A540NA00
MHGLMNFYNLEWEGDAGSIQINGTEYFLNECHWHTPSEHTINGIRYDLELHVVHRSADKNSVAVIAFLYQVGPPNSFLLKVNIVSREQLELLQQVVDDYAVMSARPLQPANGRGIKLYVPSLTLSDDKVPHTTIKAASSPQGSINAASPKSSQSPIQVVFKQTINLPCEL
Function: Reversible hydration of carbon dioxide. Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O EC: 4.2.1.1 Subcellular Location: Plastid Sequence Length: 170 Sequence Mass (Da): 18868
A0A4U0YAC9
MPACPIAPIDATPAGGGALLRDVLGGVELICAQSPADRERFLALGAGRVEDCGNLKFDLPVAAAIPAVPSGREHTWLAASTHPNEEAQVLAAHQAVRQRYPDARLILVPRHPERAGEVTRLVEGQGFSVETWSPGRPPREECTVEIVDRAGLLAGLFAEVPVVFMGGSLVPIGGHNPIEPAAVGRAVLHGPAVENFRQVFAALDERDASRQVADSEALGRAVIECFDRPESWAAVGARARDVIAEHRGAAQRLVDRLARWLD
Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis. Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A. Catalytic Activity: CMP-3-deoxy-beta-D-manno-octulosonate + lipid IVA (E. coli) = alpha-Kdo-(2->6)-lipid IVA (E. coli) + CMP + H(+) EC: 2.4.99.12 Subcellular Location: Cell membrane Sequence Length: 262 Sequence Mass (Da): 27931
A0A540KX62
MSSPSPIPVSSQQSSHQQTQPSGTNPLRFLRPFLTRISAVSHHALSNSRPWTELIDRTAFTRPTSLTDAASRIRKNAAYFRVNYLIVLAVVLAYSLISHPFSLLTLLTLAGAWIFLYARRSSEQPLVILGRTFSDTQALFGLGVATLIAILVTSVLSLLLTAGMVGVGIVCVHGAFRDPEDLFLDETQPLGSGIASIFGGGAPSFASAGASMMSRV
Function: May be involved in both secretory and endocytic intracellular trafficking in the endosomal/prevacuolar compartments. Subcellular Location: Membrane Sequence Length: 216 Sequence Mass (Da): 23104 Location Topology: Multi-pass membrane protein
A0A847QR70
LDAELTGENPLDFTGYEEKLNLSKEKTQLAEAVVTGYGKIHGLDTVVAVMDSNFLMGSMGSAVGEKITRAFEYATAKKLPIIVFTASGGARMQEGIFSLMQMAKTSAAVAKHDKAGGLYISVLTDPTTGGVTASFAMLGDIILAEPGALIGFAGKRVSEQTIGQKLPEGFQTAEFLLEHGFLDKIVARAQLKQTLSRILKMHLPSAN
Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA. Catalytic Activity: acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] EC: 2.1.3.15 Subcellular Location: Cytoplasm Sequence Length: 207 Sequence Mass (Da): 22010
E3VI81
RAELGTPGSLIGDDQIYNXIVTXHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLTLLVSSSIVESGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAINFITTIINMRLNNLSFDQMPLFIWAVGITALLLLLSLPVLAGAITXLLTDRNLN
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: 179 Sequence Mass (Da): 19205 Location Topology: Multi-pass membrane protein
A0A165JKX8
HDVVIIGAGPCGLAVAARLTEATPSALFTDAEHERFWGKRHNSSHRKTLNKSEDLTRQSPSTSRPVSRYSIAVLESHSNQWMSRWNNRFDALRISHLRSPMFFHVDPGDRNGLLAYAYAERRERELKEVRNVVGKELSKHHRKQRRSAGKKAAAPKIVPVNERDREDYFRPSQKLFCDHCQDVSRRYKVDNLIQQTEVTSVSYDHAEDDSGRSLFTIESTTGKFYSRTVIMAIGPGVPQCVPTSYEGDVFAACHTSYIMDGGELPAHLMKKIKSKAATNVVVIGGGLTSAQVTDLLIKKGVTKVWHLMRGPTKVRHFDLELPWVGKYKNNQLSTFWCCDDDDERLKMILESRNGGTLTPEHRKILETHCAHGRAKLFNYTEIASKTWDPATKTWLVKINGASDSATHPTRQGQIKSTEPPSDEDTLPSIDFIIYSTGNVADIDSMPLLEPLHRSHPIDTKGGLPCLTNDLMWRDDVPLFLTGRFAGLRLGPFAGNLEGARQGAERIAWKVEELLL
Pathway: Siderophore biosynthesis. EC: 1.14.13.196 Catalytic Activity: L-ornithine + NADH + O2 = H2O + N(5)-hydroxy-L-ornithine + NAD(+) Sequence Length: 515 Sequence Mass (Da): 57907
A0A8J4XNS5
MKWVAQIPTVLYEPVLYEEQCTKVSFSSLEDAIAFCEKNGWNWITQDPPVKPPRVKSYGANFSWNKRTRRSTK
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. Subcellular Location: Mitochondrion inner membrane Sequence Length: 73 Sequence Mass (Da): 8553 Location Topology: Peripheral membrane protein
A0A3P3Y9S4
MSGADGVPNPVLHVSGNPESAPRPDAVPSESPMSAVAMPTGLPPQAHVRQPSRAAANSGPSQPLPSDAFLLPVAVASSSSPDGQPQPGRGHVRAPSKQAAPDHGGGRRSIRTHARAPSRYVMDADQQVHPTATFQLPSGVQDDEEPSGGRPRKDPQDLARKDRALPSAKQAALEQHMARSADSQLVVASPVPESRHSSGTGSNGASVKAGPAEPRSMKGGEARHRNGSPVSPGGDHRLQERRQFARSSPVGVKPRLFVSLMIVTDVALCVYSMYLNGWQFESFSTNPLLGPSSSVLDGMGAKDTGRIRAGEWWRLVTAMCLHSGVLHLAVNMSMLWRLGGSLEQGFGFGRVAIVYVLAGISGDILSALFLPMQISVGASGALFGLLGALYGDLAHNYRLMEGSSFWYLVSLILNTALGLAAGLLPLVDNFAHVGGFVCGLLVGSCVLVDPHHARRSRSMPFYSAPLRIVSATLAVLWFIMLIWVFAWDVNPNRICGWCRALGCLPTPYWSCCVPHVDPATGRTVPC
Catalytic Activity: Cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains. EC: 3.4.21.- Subcellular Location: Membrane Sequence Length: 526 Sequence Mass (Da): 55803 Location Topology: Multi-pass membrane protein
A0A540KJK7
MWFAGNVASGSAAGATTSLFLYHLDYARAQLGTDGRGSGVNGQHQFRGILDVYSKTLSSDGIVGLYRGEFFGWSVTTVSGVCPHPFDTIRRRMMLTSGQPSKYRNALRAFREIVHLEGFKALFRGVTANMLLRVAGAGVLAGYDQLQRVAYRKGYFIEPHQRVLK
Function: Catalyzes the exchange of ADP and ATP across the membrane. Subcellular Location: Membrane Sequence Length: 165 Sequence Mass (Da): 18211 Location Topology: Multi-pass membrane protein
A0A7Y2E5D9
MPDSDQLYYGDYLDLDRLLGAQRLESTARGRTAHDEMLFIIVHQAYELWFKQILWELEAVIGVLESEIVEERELAEAVAKLERIVVIQRLLLQQIDVIETMTPLDFMEFRDLLVPASGFQSAQFRLIENRLGMRPGDRLRYSDAPYTSRLSDEDRDRVRSSEKRPSMFDVIERWLERTPFVHTEMFDFWDEYGEAVDRMLEGDRRLILENSTLNKEEKERQIEGLERTRAHFNTLLDAESYERDRREGKVRLSHDALQAALLIHLYRNEPILHQPFRLLETLVDIDENFTTWRYRHALMVMRMIGTKIGTGGSSGHHYLRRSAEHNRVFKELMNLSTFLIPRSEIPDIPKPVVRQLGFHWRPDDTGEG
Cofactor: Binds 1 heme group per subunit. Pathway: Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 1/2. Function: Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety. EC: 1.13.11.11 Catalytic Activity: L-tryptophan + O2 = N-formyl-L-kynurenine Sequence Length: 368 Sequence Mass (Da): 43416
A0A8J4Y2H8
MVGVAEMDSSSAWRKRCISCLTPAKALFKKSDGDFIRLLDCASCGQPVDRYVECERSIIFMDMLLQDIAVYRHILFNADNFTPQFYMKLGVALLLSEGYVRWSSLSHAFSPTTGIKDNEVYLYIMCLLTAIEIGIFGAIIVLYFWMRSHNRSPLSPLYNGLLLGQYGRLANVAAIIWYQAPSLVFQALVHVFIIISSIQSTRAALNAGKRESSVVVVMAAVISTSSSYILQTPLIKMYESYYL
Function: Mediator of sterol homeostasis involved in sterol uptake, trafficking and distribution into membranes. Subcellular Location: Endoplasmic reticulum membrane Sequence Length: 243 Sequence Mass (Da): 27276 Location Topology: Multi-pass membrane protein
A0A164EY88
LFGMWSGMVGTSMSWIIRIELSQPGSFIGNDQIYNVMVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSITLLLTSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAVNFITTIINMRPEGMTSERIPLFVWSVGITALLL
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: 175 Sequence Mass (Da): 18992 Location Topology: Multi-pass membrane protein
A0A1G9Y949
MKKVLVINSSARTGRSQSRKLTEVFVDHWRSIHSNPVIRFRELGNADVPHINENWIAAAFKPAEDRSEQEVEALKISDVYIAELKEADVIVLGTPMYNWSIPSALKAYIDQVVRVNETWKRNPDNMQNPYIGLLENKTVFLLLARGAQGYEKGGYNEHIDFQTDYLKTVFNIIGINNIHVIAINGESFDAEKYRNAIAASHQEVKALMETELV
Cofactor: Binds 1 FMN per subunit. Function: Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. EC: 1.6.5.- Catalytic Activity: 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) Sequence Length: 213 Sequence Mass (Da): 24229
A0A0V1PVU1
MVFRLTVWKSGSSYGSLLQNLKLTDFRKGKLIGYTKRSLLCAVLVGDYLYSKLQSYLYSIEESEASRNVSKFRLINSVKTFFITHKSKILSNLNDCFKLLNLINFTLFLVNGRYPSLSHRLFGVSLTPIVTDLLKFNGNKVNFEFQNRQLVWNVMTEFLVFILPLMQLGKLKRMTKKIMSPYKKGQRHETGNTPVFTPYTNLPVSQCAICHNNNDIAATSSNKNSSINSSCMVTNPYVTNCGHIYCYICIATKFNSLENSDSYYEGCLRCGMKLQWFKEHGESEGEIDEDAIIVPYEDREESDNDDDEETVEQETEKHSIAIEHETDYQADEKVRLYPKSATDEEEEEEAAENSDYSEGEDFDEDEDLEDADNDDFDDSDFDEGLDL
Pathway: Protein modification; protein ubiquitination. Subcellular Location: Membrane Sequence Length: 387 Sequence Mass (Da): 44427 Location Topology: Multi-pass membrane protein
A0A0V1Q6G8
MSGPTDSHPPNGNGPVLKKKSVKDYQFGTRIGEGSYSTVFSAVDIHSNKTFAIKVLSKKHIVKEDKIKYVNIEKTTLHRLGQQHPGIVQLYYTFQDESSLFFVLDFAEYGELLSIIRKFGSLSESVLKYYMSQILDAVSFIHLKGVIHRDLKPENILVGHDFNLKITDFGAAKLLGNTSDTSDESGEKIDYKGINQESSNGHHDHDRRGSFVGTAEYVSPELLKHNLCGFESDVWALGCILYQFFHGNPPFKGSTEYLTFEKIINVEYSYRNAIPPDIASIIDQLLVAEPLQRLTIPQIMASKWFRDVHWADQTYIWGRKVPRIEPYSMDNGTSSSLPTPSASPYIPAVKTGSNRNMNKSSSYHQLHSQIQQLDLNLIPSMGTKSYQPATKLKKNFMQPPTNTSSEVPLTPPLINNYKSSAQFNQRPIQKQRQNSAPMVPQVNNSANNMMRPNMSNAPKTPETEHGFPKPNPSPDSNKGQRANLRSNTAFASIPNSLQARNFHNRQYSTGSAQFYNKPVLQPGPSAQPVQQAQQVQQAQQVQQAQQVQQVQQFPQAQNQQQQISSQVNQPSYAAAAAANVSQKPNAPTGPHMNRNSPVERANFQRPSPPVSRPKSPQQDSTRFVRKTSGTRANQSAMNGNEPSVQQKSSPKPDDKSILFREIHGLLEPTEKILKMDIIMRLTLSNKEVKRDTSQLLDDSMIDDLITRFNSTLQNTSIPVVTVITNQARVFFIDGSLNVMMVDLKANQGGDYLMYDYEFEGISVEDEDGSIEEGQEIYGYLILELIREKGDLIFLKRVSDMNSPLIKNSVKVIDKDGHEIKLGKNYGWIECLLMAKEMVDCNKTSSNGKTKKATKQAPKGPSKKQKQKVPSSGSTRSETSSSAPKNANTLSKFAYAAAAAAHK
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] EC: 2.7.11.1 Subcellular Location: Chromosome Sequence Length: 902 Sequence Mass (Da): 100650
A0A0D9X485
MEAAAALSDDFRCPISLEVMTDPVILPSGHTFERRSIQRWLDGGHLTCPVTNLPLPPSPPLIPNHALRRLISAISPPAPPPPAPEEKRPAAPPAASEEVCAMLRLAKSGPEGRKVVMESGDVAALLRWCAAGDETAARAVLHLSLDGDDARVGLVADGAVDALSAASREGRLELARIPGIVAVLAAVAGGGNARAIEQALVVLNWICGESGELAREAIKIGAFHLCEALVNDDNCKIAKNAVELARTLEKLLLGLKLLRNAPGGKLS
Pathway: Protein modification; protein ubiquitination. Function: Functions as an E3 ubiquitin ligase. EC: 2.3.2.27 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: 267 Sequence Mass (Da): 27920
A0A0D9XJA1
MTIVYGERAVVIDDFPADVAAELVRRVAAAAAGAGKDDDVQRGGVVDQLPVARKASSQRFVEKRRGRLAATAPYQPRPPPPAAANAGKEDGDGGWLELGTPGTTHPTQ
Function: Repressor of jasmonate responses. Subcellular Location: Nucleus Sequence Length: 108 Domain: The jas domain is required for interaction with COI1. Sequence Mass (Da): 11274
A0A1H1GZ53
MSTKARTRLKVCCISTLGEAATAVACGADAVGLVAHMPSGPGVIEDDLILNIARQVPPAVATWLLTSRTTANDIVEHVLTCGANTVQIVKPIDPAEYQKLRLDLPASTRIVQVVHVEDEYSFEIAQEYGRVADAVLLDSGRPSHDELGGTGRTHNWDLSRHIVEKLDVPVFLAGGLTPKNIIEAIETVRPYGVDVCSGVRVDGRLNRAKLAEFAAAMACT
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5. EC: 5.3.1.24 Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate Sequence Length: 220 Sequence Mass (Da): 23549
A0A3P3Y5B4
MIAVGSVSNATMDRGKKFRMARSGDHTHFNMKYFGRSRRTIRLTGGGGYQQCVVSADSAEAHASGALISAVDEDCHTFYPDTAAFQGPPPPFDPSKISSSTIAAPLTYSSWGTPMFIRYLRRANARTYIHSTHGRPLCDASLHSKGHLQLELLVSVPRLVWSSSFIQTVRCEFAVSQFDFGMATSVLTSTLVVLLWALSLTVLVLSPSVGFIPKPSSLQGDEVDDDGTAAAASTANNVLATTPTDTVVAMAAMIAISVLCSVLVVVLHQRHVFVLDTARRAIGGLVVGTGFMWVVVVVLGAALLDNILSTLLLSCLLASLTLLMPSLLFGLRIKDWQRALVLFKFQTSLERMTAFTTYATLFAAWCSSLALTLDWDRAWQTYPVPIGIAAVLSFAVTSSTMQIVHSILEVTERTRTGPKRE
Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis. Subcellular Location: Endoplasmic reticulum membrane Sequence Length: 421 Sequence Mass (Da): 45583 Location Topology: Multi-pass membrane protein
A0A1E4T3T1
MTDELDLQPTATVVPTTKPDLPEFTLENVLADIKFGICSLFNNPEFAKPMAMVILFVESLALKVIIGLVPYTEIDYESYMQQLAQIEAGEFDYEKISGNTGGIVYPGGYVYFYSWMRWLTEDLDDMNSGQIAFRYLYMLTLIFTLAIYLSSGGHNGKFSVKPYILYLICASKRLHSIYVLRLFNDCFTTFFMVATILVLQQASLYKKSNGLLSYILTLLSADLFSVGISIKMNALLYIPAYLVVTYFLCDENLLKLVPILLFGIGVQIGMNWTFLSQGDEIRDHFIAGAFDFNRKFMFQWTVNWKFLTEDVFQSDLFHKGLLASHVTVLALFLFYRWLSPNVTGKSVGKFLKDSLKFWSSTIHPSNVILSESNGTLFVALTMMTCNLIGVLFARSLHYQFLAWYLYSLPLLLKFTNLPGYVNVILFGLHEYCWNKYPTDAISSGLLVSILSVVLLMNFKNDVFASGEANEVDELGEEKKNE
Pathway: Protein modification; protein glycosylation. Function: Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man(5)GlcNAc(2)-PP-Dol. Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+) EC: 2.4.1.258 Subcellular Location: Endoplasmic reticulum membrane Sequence Length: 481 Sequence Mass (Da): 54696 Location Topology: Multi-pass membrane protein
A0A8J7T8M9
MKEVFDCEGKPRVDLLKAHLTKEGRVEEAVALRIVNEGASILRQEKTMLDIEAPVTVCGDIHGQFFDLMKLFEVGGSPATTRYLFLGDYVDRGYFSIECVLYLWSLKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSEQVYDSCMDAFDCLPLAALMNQQFLCVHGGLSPEIHTLDDIKKLDRFKEPPAFGPMCDLLWSDPLEDFGNEKTQEYFSHNTVRGCSYFYSYPAVCEFLQNNNLLSVIRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNVLNICSDDELMNDGDEIFDANAAAARKEVIRNKIRAIGKMAKMFSVLREESENVLTLKGLTPTGMLPSGVLSGGKQTLQSATIEAIEAIETVEDGEAIRGFSPQHKISSFEEAKGLDRINERMPPRKDAVNNVGHSMGKMNMSELSRCEPALLALWRRVGKRRLEMTLGSLAALFTTTGSAEHGAGKRLGRQRDRRYLLDTECGEREGGFLPFTGMLDPQQPSGRRSVVPRPRGKLSVLTAAALCCVLLFCVVVWRGSLPLLRYAAVGCLALSTGSVLRGACLFVEELVNHSFSRYRGNLMKMLKVCFHWGHFLCLTVVCVFNQLAPEDWLSVCMGCICSLLFSAMGLCDPAAVEVSEIVEQRKMNVAHGLAWSFYTGYLRLILPRLEASIEEYHASRSAAVLQHRDTWKLHILIPLSCCIPDKLEEADDNISFLDNLPDITIDRAGIRRRVFKHSIYTVYDQAKRPHYCVVEYATPLVTLYQMSQEAMAGFDAEERLQQSTLFFRTLRDILESSRECRGRYRLILLDGEVLSCPGTPLALSQLQGLKGVEKSPAPRPAQATPYP
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate EC: 3.1.3.16 Subcellular Location: Cytoplasm Sequence Length: 902 Sequence Mass (Da): 101734 Location Topology: Multi-pass membrane protein
A0A7K2ZS95
PASGREAVERARSPQRPRAEAYLADYFTVRLPLHGDRCGGTDPGLLTGFGLRADGQPVAYVAQCGTPTRPAGYRAAART
Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. EC: 2.1.3.15 Catalytic Activity: acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Sequence Length: 79 Sequence Mass (Da): 8386
A0A2V3YAR3
MMKRASVVKGFGLWAAVSLMIMVMSLLCITSAAAESQPRVLRVAFCEAKGISEKDPDGSRHGLVVDYLNEIAKYTGWEYEYFDTTPDDMLKGVAAGEFDLMGGNYYLPGLEEYYDYPDYNIGYSKTVIFAREDDDSVQNYNLRSLNGKTIGVYDRAVENIRRLKQYLSMNDLDCTLKYYTFEQLVDGNLYPYLKDGEVDLLLGNSVEAKQGVRAVVSFDSQPYYIVTKAGNQEILDGLNMAMAKIADSNPDFAADRYATNFLNESTVDIRLSEEEKDYIRQKGSVTVAMPRNFHPLACETPDDMHDGLSYDILQEAAEFTGLEFHYVPAASYIEALDLVRRGDADMLGFYLGGESDSLEQKMVLTAPFASLNSIIVRNKASSYPGSELVGAVIEGRELPKTIRAAEVKRYHNINDALKAVNRGDADFVYGLATYMEYEIQKSHFANVLPVTLVNDRMDVSFAMARPTDPELLSIMNKAINSISADRREELLDQNMVSVGTGRLSMTELIYANPLMFVGILTAVLLIIVTVVLWINRVRVKAAVMQSDLKKAEAESRARGEFLSHMSHELRTPINAVVGLADLAGMTEGVPDNVRDMLVKLRASAHYLLDLINDILDMSRLDSEKLTIASEPFSLERMLDELQTMMEMDARRRGLTYRIEANISHGGVIGDVIRLRQVLTNLLSNAFKFTPEGGTVILRVTEMPDADEKTSFEAADYEFQVIDTGVGIDQKDQTRIFETFEQVGTNYSKSQGTGLGLPISHSIVRLMGGELRVKSESGHGSEFYFTLTLPAGAPSGAGENINQMPVGEELLKEIRILLAEDNDLNAEIAIQLLELKGAVVSRSENGRLAAERFAESAPGEFQVILMDIQMPEMNGLEATRAIRAMDRPDAASIPIIAMTANVFKEDVDAAMEAGMSAFEGKPLDVEHLYLKICRLLGLDTGCPREE
Function: May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with spo0H (a sigma factor) to control the expression of some genes that are critical to the sporulation process. EC: 2.7.13.3 Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. Sequence Length: 945 Sequence Mass (Da): 104835
A0A540KM31
MKRLKVPAAEHSPSPYNTSSAFIRESDPRCLLMPVIVSDRDTSVGQLGDLHLLQLATRSPGDVSGLISTSIRSALDCPLNYARSYLTELLPFCVCRVVYLNSNLILIDDIAKLSATPLGGGAVLAAPEYCKANFTSYFTFAFWSNPSLSLTFADHHTCYFNTNSKVKPSRWLVINLRNVDWNLYLNTLFWNLNYWDSISTLVGEVENPKKTLPKALFYALILVVLGYFFSLLMGTGAVPLDCELWTNGYFSDIAKIIGGFWLRWWIQGAAAVSNMGMVVAEMSSDSFQLLGMAEQGMLPKFFASKRL
EC: 2.4.1.- Subcellular Location: Membrane Sequence Length: 307 Sequence Mass (Da): 34190 Location Topology: Multi-pass membrane protein
A0A6M3YPK1
MQQPNADELEYVRAAFDNANHVAPRGPKLPGDPDFNIYFRSLLRTLDPKSSTGLGAFEAYATIGDALGWDGIRFTEVHRVAELQRLVESRLRDLARGVPDIAWFNDRAEEGADIAFQELKRALQGQEEQEAPPADNIKLFIKDEPHKISKVSEKRWRLISAQSLVDQMTDRVLFYSWVETEISDHFNVTSKGGWSPLPMGYQRLMAEFPEDTAVAVDKSLWDWTMPPWVVYEYLQAKARATPDMSDELMWLWARRFWFVLGPGARVRMPTGVVWRQDCWGLMKSGFYLTLSMNGAAQMLQHALAWRRMGKLTFPPRIWTMGDDTLTRLSPSDMEEYRVQLGTTGCIVKMVERAREFAGYKFEGNTIAAAVITPLYERKHQFILKHVDADNERSVALAFSLLYALARPGWHTQACVKAGVTVGPMQRLWARGQVKLDLLEVILIHMRW
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1) EC: 2.7.7.48 Subcellular Location: Membrane Sequence Length: 447 Sequence Mass (Da): 51169 Location Topology: Multi-pass membrane protein
A0A540KCQ4
MRGHQQNAIHLEEKEKREKELLVQIIEEADEFKLGFYQKRKITTENNKAANREREKLFLANQEKFHAEVDKNYWKAIADLIPNEVPAIEKKRGKKDTEKKPSILVVQGPKPGKPTELSRMRQILLKLKHNTPPHLKPSPPAPAPTKDAKPSTSAPPKAAVVAATPEAVVAAL
Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Subcellular Location: Cytoplasmic vesicle membrane Sequence Length: 172 Sequence Mass (Da): 19327 Location Topology: Peripheral membrane protein
A0A0V1PTM4
MFNTNHFHDRMGSEDLRNQFLSNANPPQPKDNLRPNGSYVTDDDDRSIIFGNDNSNLAPYPTSKGYSGISKNSDSSNANTHEYELDRLQSTYSINNSSAENPFNPLQGNHPYNGYGQKQKENPFRDQSVPEFPQQEYNPFEPHREQPPIPVDDEYEKMRKNEKARLKQLRRKPRFHYTKLPYFTILVTLIQVSVFIAELAKMSSLTGSAFQTKPYFNPMLGPSTYLMINMGARYAPCMQSIKGITNDTTINFPCPNSTTTDTNVCSLNELCGLSGVPVKDDVYKPHQWYRIITPIFLHAGFLHIIFNLLLQVTMGASIERSIGIIKYSIIYLMSGISGFLLGANFSPNGIASTGASGALFGVVATNIMMFVYCGKKNTNIYGTKKYGLFIFIMIMEIIISLVLGLLPGMDNFSHIGGFAMGILTAIILLPDPFFIYIDGIITYHARDGTMQQFRNNWNPMYNWEDKIPSRFYIWCGIRVICLVLAIVYIAMLVKNFFNSGENPIDNNCSWCKYINCIPVNGWCDIGEVTVETENTSNSKRSIDSEMLFSETKLKNIEVLETTSHLVQHNSNHISSGSSFFEYQNTSTGLVICLFLGAMTLKFYKSKKQI
EC: 3.4.21.- Subcellular Location: Membrane Sequence Length: 609 Sequence Mass (Da): 68833 Location Topology: Multi-pass membrane protein
A0A2U9I5S7
KDYKLTYYTPDYETKDTDILAAFRVSPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIESVVGEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPTSYTKTFQGPPHGIQVERDKLNKYVRPLLGCTIKPKLGLSAKNYGRAVYECIRGGLDFTKDDENVNSQPFMLWRDRFVF
Cofactor: Binds 1 Mg(2+) ion per subunit. Catalytic Activity: 2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O EC: 4.1.1.39 Subcellular Location: Plastid Sequence Length: 203 Sequence Mass (Da): 22950
A0A0D9W8U3
MGREERFPVWEAALGAGVAAAFATGLVGVYLSMPDSDYSFLKLPRNLEELQILTGHLENYTSDYTIQVLVGYCSVYIFMQTFMIPGTIFMSLLAGALFGQLRGLALVVFAASAGASSCFFLSKLIGKPLVFTLWPDKLMFFQKQVSKRREKLLNYMLFLRVTPTLPNTFINLASPIVDVPYHIFLLATLIGLIPAAYVTVRAGIALGELTSLSDLEDQEVSYSINWAIAGRGVVVRDKVFYNLETSELQKGGIVYTGNVTSGNPDVSRAQFAKLLKLVTFHLSSISSLYVQDGAVDSSMVCDAKVRVISDNPSAVMLLSNILWRTPDRAISHDTCPLTIYVASSISTNVRNSLGSGTQYANGFAAADIERSSLILCVDVIKSSGLQDVLVSTDSGVVVSSKGSSVLFPTKAREPNLLAKPTTAIIVSLDSTDALPKVSKLSPGQAAYHFLAGYHDGKEFMRLIEAILLNNLPDCNHEDTKDMSGLHMVSLRRNRSGGPLTVAYPMLLFLSSPSINKRSGGRLSGSSLLQQSRSTETKHCQEYWH
Pathway: Carbohydrate biosynthesis; gluconeogenesis. Catalytic Activity: ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate EC: 4.1.1.49 Subcellular Location: Membrane Sequence Length: 544 Sequence Mass (Da): 59231 Location Topology: Multi-pass membrane protein
A0A1H0Z2C5
MFSSTLVRFFRIATGLAFAVLIYAVLVQVLGRNVFNDSPVWTEELTRFALLYLAACGVGLSLRTGDLVNVDILINYFPTKIRRAFLIFASVATAALCATLMIPAWRFTAIGKWQTSPALSWRMDFIHASTIIFLGSILLFALLKIFEGIRDFNGPEDQIGEESE
Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system. Subcellular Location: Cell inner membrane Sequence Length: 164 Sequence Mass (Da): 18289 Location Topology: Multi-pass membrane protein
A0A540MUD4
MWLGEKGTIKGVKFRRKGSQEFTAHAPLTIVCDGCCSNLRRYLCNPKVEIPSCFVGLILEDCQLPYANHAHVILGDPSLVSFYPIDSREICCLVDVPGRQVPSISSGEWLTTWKQRWHPSRIIFQVPPELYTAFLVAIDKGNIKAMPTRSMPATAYHTPGALLMGDAVNMRHPITGGGMVVALSDVVALRNLPRPLRNLNDVPALFKYLESFYTLRKVSSLCWSFELLKSHIGELKGN
Pathway: Terpene metabolism; lanosterol biosynthesis; lanosterol from farnesyl diphosphate: step 2/3. Function: Catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, and is considered to be a rate-limiting enzyme in steroid biosynthesis. Catalytic Activity: O2 + reduced [NADPH--hemoprotein reductase] + squalene = (S)-2,3-epoxysqualene + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] EC: 1.14.14.17 Subcellular Location: Membrane Sequence Length: 238 Sequence Mass (Da): 26540 Location Topology: Multi-pass membrane protein
A0A7Y2GB53
DSKLLSREDRERLAARIRSRAVAVAVGVCSPEEIDELNILWASMEAMRRAIQKLVPQPTYLIVDGNHVIPDSAWPVEAVIRGDFKSQSIAAASIIAKVERDRLMHHLHEAHPEYNWISNVGYPTRAHYEALSSHGASPLHRRTFNLENPYPPFSEAATEPEQVDGHSSTR
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: 170 Sequence Mass (Da): 19095
A0A0G4IH25
MLLSEGAFPSVGPHNCCYLLAPADQLAGPNAFPNNYYIGFTVNPPRRIRQHNGEIKGGAKHTKSLAPWEMLCVVHGFPSQTAALQFEWAWQHCRRSLRLRPVWAEFTKWVTRQGRTIRKAFPDAQGVGITSLFAKFAVLHKMLAIAPWVHFQIHIRYIHPVCKEFLDRYCGDVLADLSNKSLTVSWGHFDSSTVTMFARDDVSPASSADNESCAGEKACHICFSAGRPDAYFGHCPSCRAAAHLVCLWRNNAEPGRILPRDVTCPTCGTLLPWSSVIANSGRGSERQATSISSLVDPMMAMSLSTIPDVIDLRSSDDEDSNGSETQRPRTSSPVTQPPAGPSQLLGNDGDDEQQVADPPPSIRQPVSPSRLLSTSLLDRLAAKRQ
Function: Catalytic subunit of a heterodimeric structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA. EC: 3.1.-.- Subcellular Location: Nucleus Sequence Length: 385 Sequence Mass (Da): 42275
A0A1C9D4Z8
WSGMVGTSLSMLIRTELGNPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLMSGVVESGAGTGWTVYPPLSSSIAHAGASVDLAIFSLHLAGISSILGAVNFITTIINMRPIGMTFDRMPLFVWSVGITAILLLLSLPVLAGAITM
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: 184 Sequence Mass (Da): 19586 Location Topology: Multi-pass membrane protein
A0A344ANV3
MVLSYVCLLVFVAVAASVQDFVNVGSYISLDFVGCALSFISILLMIFFFIFCGSVIGKLEAVLIGISSIFSVVCFLSNDTMVFWVSYELAIIPLVYSLLLGSPYSERFLAFWYLLGYVCLTSLPLLFSIQYVNFLAHTTNMGFKYGLEGPGGFILGVIMFILFSTKIPLPPFHAWLPIVHAEASTIVSVWLSGFIMKLGIIGMYRFVLPLIQDNSNMITVLIGYSVAILLSCLSELDTKRWLAYLSLGHIVIAVVGLLNSEGVNSEAPIYCLGHGFSASLLFICFLFIYESFGSRSWLAVSLAGRISVGFLLVISTSLLTAASFPPSLNFFAEIFILGLSFHSLNIILAYLFYLLVGGLIPVLILAYLVCSSGESHGNGVPSFGILFSLYIVALSTYVFFMML
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I. Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+) EC: 7.1.1.2 Subcellular Location: Mitochondrion membrane Sequence Length: 403 Sequence Mass (Da): 44170 Location Topology: Multi-pass membrane protein
A0A7L3PLJ7
MASLALELLGFSLTLLGLLGTLMTTVLPHWWRAAHVGTDILTAVGYAKGLWMECVWHSTGIFQCRAHLSQLALPPELRAARAMMVTSCCLSLLASGLAVLGMQCTLCAQGSPKKASLAVSAGATFVLAGLLCLVPVSWSTNDVVMDFYSPALPGGVRYEMGQALYLGFASALLTI
Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. Subcellular Location: Cell junction Sequence Length: 175 Sequence Mass (Da): 18462 Location Topology: Multi-pass membrane protein
A0A0G4J6T3
MHGIRRVDPSQVTEAQRAEKRKKIAKYVAMRDDVLAMRKDRRHDKEALALTRQVLEINPELYSLWNYRREILLGMMDKRSCDVAELLADELNVVGRAIQRNPKSYVSWHHRLWVVQRGGSDILKEIDLTSQFLMADARNFHCWDYRRSLVDLSNVSPSEELEFTRKKINDDFSNYSAWHYRSTLLTKIGIDQEVLDREFALVADCFFTEPDDQSAWLYHRWLCVQHPDIACLEKQLSIMDELLDLEPNCKWALLTSVRLLSELCRLDRTRSVPKRRIGDIFNRLPVLDPQRKTYYRDLCDRICVQLGPCIE
Function: Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to cysteines occuring in specific C-terminal amino acid sequences. EC: 2.5.1.60 Catalytic Activity: geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein] Sequence Length: 311 Sequence Mass (Da): 36728
A0A1E4IJB6
MRHGLFLRALETAACLALGAMMLLTVADVLGRHALGRPVPGTVELVQYALAIVVFAGLPVVTRDGRHISLSLLEGRLGAPARRLQRLVLGLASAVILAAQGWIVFGTAQLMRAQGDVIGFLNLPVHPAAYLMSILSFVTAAALLLDSTFANGREAPSGGAAH
Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system. Subcellular Location: Cell inner membrane Sequence Length: 162 Sequence Mass (Da): 16912 Location Topology: Multi-pass membrane protein
A0A8J7NKY8
MDLKGKGLTLNEVNPCARSIEVLDKEFIRMRAREIRKELLQGMKKPYKKLIDVSSGDAHMAGMKPISFLRQVLAVCLYPELLHSDRFPADVKQRAQRLLKNCEGGSLGSYSPPCGILSIRRNVSEFISQRDRGVPSDPDNIFITSGGQDAIRCILKILVHGEGHAQTGVLMPVPSYSYFKIAVLECGGAIVPYHLSEEQGWDLQVVELRRALQTARGHCSPRALYIINPGNPTGHVQSRKSIEEVIRFAAEEKLFLLVDEVYQQTVFGEGSAFVSYKKVLYEMGPSYSDMVELASLHSVSKGFTGECGLRSGYVEFVNLDPEVKKCAIRLLEMYLSSSITGQIALDIMTNPPGHKDLSYPIFKAECQAILETLAHNARRVQKTLDSLPGVSYQPVQGSLYIFPRLHLPPRAVEQARAEGMEPDRFYCSRLLEEAGVCLTPGCDLGQREGTYHIRYRPCSCCSHWAANPSSLRATSQP
Pathway: Amino-acid degradation; L-alanine degradation via transaminase pathway; pyruvate from L-alanine: step 1/1. EC: 2.6.1.2 Catalytic Activity: 2-oxoglutarate + L-alanine = L-glutamate + pyruvate Sequence Length: 477 Sequence Mass (Da): 53082
A0A8T2MI97
MAVQLVEGCLYYVDSEGNRVCGDQFAVGSGSMYAYGVLDSGLRPDLTVEEACDLGRRAIYQATYRDAYSGGTVNLYRVHSQGWERVSQDDVLSLHQQFASGSA
Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides. Catalytic Activity: Cleavage of peptide bonds with very broad specificity. EC: 3.4.25.1 Subcellular Location: Nucleus Sequence Length: 103 Sequence Mass (Da): 11252
A0A8T2MLT7
MYYLSLSQTPQPRELLAIEEESERLARELREVSRNRESLRNQLAQLCRYRGVLICTHSLTTSQATPPFLKSSSLLDNRQDVRLSFVAGVVHPWKVLAFERLLWRACRGYIIINFREMEEKLEEPDTVRDEGREGKREGKREGGRGSIGVGRNVGWQQHACVQVGWQQHVCVQVGWQQHVCVQVGWQQHACVQVGWQQHACVQVGWQQHACVQVGWQQHACVQVGWQQHACVQVGWQQHACVQGEMVQWTVFLISYWGEQIGQKVKKICDW
Function: Essential component of the vacuolar proton pump (V-ATPase), a multimeric enzyme that catalyzes the translocation of protons across the membranes. Required for assembly and activity of the V-ATPase. Subcellular Location: Membrane Sequence Length: 270 Sequence Mass (Da): 31250 Location Topology: Multi-pass membrane protein
A0A8J4Y8N9
MVEKRPKGTPLITVCNHYSCIDDPGLWGVLKWRHLWSATTMRWSPAAHDIAFTRRIYSWFFSSGKCVPIIRGGGVYQHAMDFLLERLGEGHWVHIFPEGKVNMTLETMRLKWGVGRLVYDSLVSPIVLPFYHIGMDRILPNHPPYIPRLGKWVTVVVGEPLDFRAEVQEMRKRNEDPATARRRITDRIQEELGHLRERAEELHGKLMAERGEAWKPMVHARNEGQVGR
Catalytic Activity: 1'-[1,2-diacyl-sn-glycero-3-phospho],3'-[1-acyl-sn-glycero-3-phospho]-glycerol + a 1,2-diacyl-sn-glycero-3-phosphocholine = a 1-acyl-sn-glycero-3-phosphocholine + a cardiolipin Subcellular Location: Mitochondrion inner membrane Sequence Length: 228 Sequence Mass (Da): 26454 Location Topology: Peripheral membrane protein
A0A0D9V3C9
MPVIPAQAPPTLPPPMGVTVIMPNSGTPASTSQSPPGPTAGTAISSPLAPPSGSWGGNAPSGLLVGVAVAGFLLALVSMGLFLCLKNRGKRRRPAYTTNLARRNTLVVPDRVVSPDVYQPSNGPAASPSGTNSYDFSGTTSWFTYDELAAVTGGFAEENVIGEGGFGKVYVGALGDGRRVAVKQLKVGSGQGEKEFRAEVDIISRVHHRHLVTLVGYSFTEHHRLLVYEFVSNKTLEHHLHARGLPVMDWPKRMKIAIGSARGLTYLHEDCHPRIIHRDIKSANILLDDAFEAKVADFGLAKFTNDSLTHISTRVMGTFGYMAPEYASSGKLTDRSDVFSFGVVLLELITGRKPVDSSAPLGEESLVEWARPLLVDALDTDDFRELADPALERKYSRFEMRRMVEAAASCIRHSVAKRPRMVQVWRSLDVDGSSTDLTNGVKLGQSTAYDSNQYSADIELFRRMAFANDLSSAEFGYSDEDDAHHASSSSRPGPNC
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] EC: 2.7.11.1 Subcellular Location: Cell membrane Sequence Length: 496 Sequence Mass (Da): 53692 Location Topology: Single-pass membrane protein
A0A7Y2E3Q3
PNKTWEGAAGGLVGALVVAWLYAEFRNPMFGLSNALVLGAIAGVLGPVGDLIESLLKRSAGVKDTSNLLPGHGGVLDRFDALIFTVPVHYLYLKYFTTLLQ
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: 101 Sequence Mass (Da): 10758 Location Topology: Multi-pass membrane protein
A0A2S0L2C1
MRGTSVKKNLDWRLEMKAWDNLRKSFKIAILTVLCITMVFSTGLLYMISYGASDKSSSKSSKQTESAKTSSVTNKVQAPEINAKSAVLYSENTNTVVFSKNKNERVAPFSTTKLMTALLVVKHIKNLDQKVTISKEAAALGGSSMELKEGEVVTVRQLLYGLMILSGNDAAYSLAEVVSNGNVDEFVKMMNDEAKALGCKDTNFVNPNGMKEENHYTTASDYMKIARAALKNKQVYKFASTKKYEMGATNLNEARVMKSHTDLINTKGSGVVAGKTGFWNGEASIVLAYDKKDLKMVLVLFGDDKENRPKDAKAIFEYAYKYLRVNKPVAKGKKVTKILVRGGKNTIVDAYASETAYAYTEKGDRAKITVKIKRDWSVKAPLRKGDQVAIAKVYVDGKYVSDAPLVVKQNVSKGWITSEAYISNLGAMILGPVLVVLIVIACLVKRRRKKAAVPIGKHDKGRDK
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis. Function: Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. EC: 3.4.16.4 Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine. Sequence Length: 464 Sequence Mass (Da): 51141
Q8HJB7
MTTNTRKTHPILKIINNSFIDLPTPSNISAWWNLGSLLGLCLTIQILTGLFLAMHYTADITSAFTSVIHICRDVQYGWLIRNIHANGASIFFICLYMHIARGLYYGSYMYIITWNIGTILLLLVMATAFVGYVLP
Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis. Subcellular Location: Membrane Sequence Length: 135 Sequence Mass (Da): 15233 Location Topology: Multi-pass membrane protein
A0A3G1XSW2
IFGIWAGMVGTSLSLLIRAELGNXGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTLLISSSVVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAINFITTIINMRINGLSFDQMPLFVWAVGITALLLLLSLPVLAGAITMLLT
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: 191 Sequence Mass (Da): 20337 Location Topology: Multi-pass membrane protein
A0A8J8WAG4
MRVHEMVVPARPVINSAPLPHATTPLLANNTRPTQGLAMLTGEVAPSGRGAGAEPRRGGRCVRVTPAVRYRPVRSLLLLGLLVLVSLFVLFTLSQMAVVQHTMMAHLGTGVAPGVAGGGSGAAPGGARGPKGPQRPWRSQFNQFKIEPLLVRNAPSVEVNLAMASNLRMANQIAAIIIRNSLLVSHSAHSTLAPQTPRTAQGKAQVASSPHNLPSHDQPNMNTNTHHFINTFYNSSTQAQQMRSGLHMSDTLHPGQQSSTAGQGQEASTPVGARGRAEQEGAKGIAEPSPLYEPIDSDVMELAARKNDSNRKRNPSSRLSEEQLRKLPVCPEIPPGLQGHLNVDLDFLEKLRLEDVLQQLSWVSPGGTWSPVHDPLHPCLPRHKVAVVLPYRDRLHHLIILLSWLHPILRRQQLEYTVYVAEQTGNATFNKGSIMNAGFMEAWQRSDAGCFVFHDVDLLPEDDRNMYSCPQHPRHLSVGVDTLGYKLPYFLLMGGVLSVRGDQFLRLNGYSNMYWGWGGEDDDMGYRQVKHITAHACHTLTLKLILSQPATQVRGKLLRTSGRRYRLDGLNTLKYTLHARHRHPLFTHLLLDVGTPPENLLRLDTPAHPPPRR
Pathway: Protein modification; protein glycosylation. Subcellular Location: Membrane Sequence Length: 613 Sequence Mass (Da): 67577 Location Topology: Single-pass type II membrane protein
A0A455TA43
MLNKKYPVLYLTAGLDEVGRGALVGNVVAGAVILDNSKLIQGLKDSKKLSYNKRTKLSVIIKLKALSWSIGIASSREIDFLNISNATKLAMKRAIFNLSIQPNFIFLDGKFKLNINMPCLSIIRGDNIISEIKAASIIAKDYRDREMLKLHNIFPKYKFNKNKGYPTSHHLKMIRNYGITKFHRSSFAPISKMQ
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: 194 Sequence Mass (Da): 21918
A0A1H1JFG7
MNLLHKLDRMLSNLFLLLGMVLLVVLFALTSLNVILRFFPIFSIGWFDEIVEVSFAWMVFTVAAYLWRDRAHPFIDFLLESLKGRRSQYVLLIFIESMNIFFLVAFTYYSFSLMMRASAWSPIFQIPKSFFYMSMPIAGAYMTIVSLFFWAGHLRNLCSSNPTPFTYSSCQK
Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system. Subcellular Location: Cell inner membrane Sequence Length: 172 Sequence Mass (Da): 20118 Location Topology: Multi-pass membrane protein
A0A223KUF8
MKKLLVLVSLILVLIIAGCGTSDNNEEQTGQGSNETTANNDTNNAAGDDQEEPVDLENLVFPQMSTEVAENERVVEIVTNKGTIVVKLFPEHAPKAVENFITHAENGYYDGVIFHRVIEEFMIQGGDPNGTGAGGESIWGEPFEDEFALELLNFRGALSMANPGQPHMNGSQFFIVQAGPLDDAYEEQLKKAGYPEKAVEFYMENGGTPWLDHRHTVFGHVLEGMDIVDEIAQVETGANDKPVEDIVIEKVNVTK
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. EC: 5.2.1.8 Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0) Sequence Length: 255 Sequence Mass (Da): 27934
A0A1H3JRA8
MLEGFIDIHCHILHGVDDGSKNLEMSEKMIQIALDDGIIGLVLTPHIRAPRFMLANEIVWEKFDELREDIRKKYPQIHLYLGGEFYYYSSILEDSPQMIRTINETDYVLVEFSPVIAYDDMLRAFQKLKANGYEVILAHLERYEVLRKNIDNVEHIKDMGIVLQMNANTIVTPFDREHKKFMKRIIKDELVDLVATDAHDLDTRKPCLSKAASYVTKKTSDEYANAIFVENQLKILKGKRII
Pathway: Capsule biogenesis; capsule polysaccharide biosynthesis. Function: Dephosphorylates CpsD. Involved in the regulation of capsular polysaccharide biosynthesis. EC: 3.1.3.48 Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate Sequence Length: 242 Sequence Mass (Da): 28132
A0A8J5CR89
MKPRWGPYHRGALELAGLYSRGKRTQEIVCVCMCITLMVVNLYFMAVHFRVEKVGSICLVALAGIFTADFASGLVHWAADTWGSVELPVLGKKLKDLTCAHEYAVAVSNRFDVLGALGDPVELWIPSNVKLYRLPRSVLGSAPGQGVVLSPTEMLEKIEESRAARLAGNRDQHRGSVTPD
Pathway: Lipid metabolism; fatty acid metabolism. Subcellular Location: Membrane Sequence Length: 180 Sequence Mass (Da): 19708 Location Topology: Multi-pass membrane protein
A0A165JV82
MTTDSQNAERTMGAAPVRLCKRCQEIEATTIMRTEPLCSNCFVEYIKKKVAKQLEAYRIKNASKNNRRRVLLPISFGVSSLSLLHVLDGHLQSQIRRTNRTGYELHVLHVNTSGVDADAPQIGRLEVLKEKYPRHTYSELTLEDVFDHANEYLETTLRDVNINIGDVAPPSSKHEKLVGLLSALPSPTSRADVVETLRNNLIIAFAKENDCQSITWGDSATRLAEKTISETAKGRGFSLPWQISGGESPYGLHVSHPLRDVLKKELVIFAENVDPPLTPLIHSRPAPTMTSAPAKSTTIDDLMGQYFASIEESFPSIVANVVRTTSKLRAPEVTEGQSRCDLCGLPLADSDASLGEGESSAQSLVQPEGNLCYGCARTTLGSRFTPHS
Pathway: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis. Function: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with NCS6 that ligates sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. May also be involved in protein urmylation. Subcellular Location: Cytoplasm Sequence Length: 388 Sequence Mass (Da): 42611
V5NFZ1
MPILQILTGLFLAMHYTSDTTTAFSSVTHICRDVNYGWIIRYMHANGASMFFICLYMHVGRGLYYGSYTFLETWNIGVILLLTVMATAFMGYVLPWGQMSFW
Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis. Subcellular Location: Membrane Sequence Length: 102 Sequence Mass (Da): 11742 Location Topology: Multi-pass membrane protein
A0A8J4XQM9
MVPQRLWLKKFALIALLLDEEEELNSKRHCFGYTQNGLLHMLDRNRRIKPDPERFQICKDKFDIIVTCEERVYDQVLECLEARIPEENTPVHVINIDIQDNHEEATIGAFMICELAALVSGNIYETIEHFLLPPARWQHPQRSYCLHLDTRHSRFTCTASVSPLTPTAPGAGTSLETIEHFLLPPARWQHAQRT
Function: Protein phosphatase that catalyzes the dephosphorylation of the C-terminal domain of RNA polymerase II. Plays a role in RNA processing and termination. Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate EC: 3.1.3.16 Subcellular Location: Nucleus Sequence Length: 194 Sequence Mass (Da): 22481
A0A3P3YA61
MLSSIAPMRSGLLGGVTVRGVAGSGPLPVALPRTCHFALGRAACTLPPAVMGARDDGDELALWDALQAGALLSTGRFTHAGRCASLQWTYKHRASNSTVAISSTHSVDGARQQTTAPADFEVTAPVSLSSYCHRGCCRAVIRKPSDDTGAFLEIYRQGRPPLTTSLKKVCGELPKGGSCLSGASFSANCDKFAFSADVKPDDRQSFWNDTPAHGNDAGSQPSRGTQYDYKQDWGEGLGLLRTIVVLVDIVDDRLLATVLDKAFNEKFSWGQVVFHPRQPYLLAVGYPQTGRRLGLLHFNTRRSSMFVASLERRDECATCITPADHSATLPRFNHDGSVLVYVTTDDVGFHISCSRLRSLSWADGPVPQSTRTIVDVVRANNTFPGLWPRGFPTRCWLADTSNIVVASQCQIRFALLVIDTRNGSVQELDIPGPFSSADVLDVHGFDILVKLETVGRPPEAFIGRMDPSNVQKVLWTAVSSPPLPFPSPVNHLSIPHCVIDVDGLFDAILVGTIKEDTRLIAFPHGGPHSAFTTTFATSVAFLALQGFALLEINYRGSTGYGQDMLESLPGRCGTQDVEDCMKAVDAVLSRFPSLSKDNVAVMGGSHGGFLTLWLIAKYPDRFRSAVARNPVANVAHMMSTTDIADWCAIECGLAFSPTGVPSAAHYEAMYKCSPISMIERVNTPLLLMLGANDKRVPMSQAVDYYHLLQARGVETRCIIYPGNGHSLTDRVDTESDHWINVLHWLRKL
Catalytic Activity: Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide. EC: 3.4.19.1 Subcellular Location: Cytoplasm Sequence Length: 748 Sequence Mass (Da): 81249
A0A5Q0U1C0
MKLISSLMFSMSSMAILMKHPISIGVALTTQTILMTMITGMMNMNFWFSYILFLVMIGGMLILFVYMTSVASNEKFKLNLMLVTAATTTFLTSMLFNKSEMNLSFKIKETLNFNSNNTKTMLTKYFNFPSMTIMMFMMIFLLLTLVVIVKLTKKSMGPIRKNI
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I. Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+) EC: 7.1.1.2 Subcellular Location: Mitochondrion membrane Sequence Length: 163 Sequence Mass (Da): 18654 Location Topology: Multi-pass membrane protein
A0A679ENZ2
MTFSYAIIVLYSLLLSCALFVVLTMNTVYAVFFLIFAFFTASAVLLYLGFEFLAMVFLIVYVGAIAVLFLFVVMMLNVRYIPWLKKDLRFAPLGFLILAFFLLLFLFAILHIESDIYWSLNIPYSFLSANLESAHSQISSAENTEMLGTLLFTHYGYPFLVAGYALFIAMVGAIVLTLRHIPLPSKKQDAYVQVTRLLSTVRLLAKDKA
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I. Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+) EC: 7.1.1.2 Subcellular Location: Mitochondrion membrane Sequence Length: 209 Sequence Mass (Da): 23651 Location Topology: Multi-pass membrane protein
A0A3B0N237
MTEERYVIWFDEPECDQVAVAGGKGASLSSMVRQGLPVPNGFVVPAGVLEACVDAEALKAYARAQDYAAAMKLVEDTAVVPQEVMTAYEELGGKVAVRSSASAEDSEAASYAGQQETYLNVVGAEDVRRRVIDCWTSFFSERALFYRGQKGSLDDLRMAVVVQQMVDCVFRRIRPPIPTTSGHLFRGIRPPVTRCREAAYFGYQS
Pathway: Carbohydrate biosynthesis; gluconeogenesis. Function: Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate. EC: 2.7.9.2 Catalytic Activity: ATP + H2O + pyruvate = AMP + 2 H(+) + phosphate + phosphoenolpyruvate Sequence Length: 205 Sequence Mass (Da): 22519
A0A8T2N9H9
MLGEGVEVANTGEELLIERSIRKGMINPGDDRQTIQHNGPVTSFNYTIRVKCDENYYGNKCNKQCRPRDDYFGHYVCDQFGNRGCMEGWMGPDCKTAICKQGCNLLHGSCSEPGGCTCKYGWQGPYCDQCIPYPGCVHGTCSKPWQCSCEKNWGGLLCDKAEHACVSNPCANGGTCHEILSGFECQCPPGWGGATCAKGKAAHPALEEKTPVSLTLSLPFSDWELFHRTEYMDECASNPCDKGGTCIDRENGFECLCPPQWAGKTCQIDANECMGNPCLNAYSCKNFIGGYLCYCIQGWVGQNCDISIYACHGQCLNGGTCKPDKLQDNMHLCLPGQDEHRGYHCSCPPGFVGIHCEIQRNKCTSNPCRNGGQCHNVVDSFVCECPEGFSGATCEVSERLGWVKVKSNPCSPNPCKNMAQCHDLMDDYYCACPDDYEGKDCSDLKDHCKTTPCEVIDSCTIAVATNTTEEGVRHISSNVCGPHGRCISLPAGNFTCTCEQGFTGIYCHENINDCISSPCKNGGTCIDGVNSFMCFCPDGWEGELCDLNVNECSRNPCKNNGYCVDLVNDFYCECIDNWKGKTCHSRK
Function: Putative Notch ligand involved in the mediation of Notch signaling. Subcellular Location: Membrane Sequence Length: 587 Sequence Mass (Da): 64343 Location Topology: Single-pass type I membrane protein
A0A8T2NE13
MNGATFPSPTAEMAEINRIHYEIEYTEGISQRMRIPEKLQVAPSASEDQDAGPQDALHSVLMQVPERIVVAGDSEVSQYPRPRDLDLIQSTPLESLSLKTPPRNGQVARNDST
Function: Plays a role in mitochondrial and peroxisomal fission. Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface. Subcellular Location: Membrane Sequence Length: 113 Sequence Mass (Da): 12487 Location Topology: Single-pass type IV membrane protein
A0A8J3XWY2
MQHARAGEGGPQRHEQLGDRLRSKRIVVLGQEVDDEIANRICSELLLLSAEDSQRDISLYINSPGGSVSAGMAIYDVMQYVPNDVVTVTMGLAASMGQFLLCAGTPGKRYALPHARIVMHQPLGGIGGTASDIRIQAEQMRYTKKLLAERIAFHTGQPLERIEADSDRDRWFTAEEAKEYGFVDHVVAGVRAL
Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs). EC: 3.4.21.92 Subcellular Location: Cytoplasm Sequence Length: 193 Sequence Mass (Da): 21191
A0A1E4SXZ1
MTEASDSLPPSFASDSNPPPASSTPFEVIFNPRLKRTSTTNYRTELEAQQQKAEDDARSQLTRRESEKNTFDKMSAQNFKRQLSFTKPDDDSKIEAPIETIYTRDSSAIDEGKEKHSLLGDIKNKLHIGSPHSLHSHHQKHETDQSEQTKLSKYEFGLNVSDQLNSSNSSSISISDVSPNESTSYTQPHAKRKNKKKNRLKDKQFLLPDDNSLTFKVLRYPFLIFIAMWLTVLSIVYLIVRLSIYISEQVMANTGQRRKMVNKLKNSKSYPEYIEHAKALNEYLKLDKWCEEDRFYCYDWKTLRRIVRDLRKLRRAGKNQELMIVLQNCVKSNFAGSENPLLYSHTYYGTKNLIVEYNNEVVTSLNSITESTSIPIETKKNFFKTISRSFGKTALALSGGASFCYNHYGVLKALLDNDLLPNIISGTSGGGVISALATTRTNKELASLITPKLAKKINAAGNEPFHVWFRRWWKTGARFDSLDWARKSQWWTLGSMTFKECYERTGKILNISTVPHDIHSPTILCNYITAPDCCIWSTLLASAAVPGILNPVVLMEKVHNGPDGKECIKPFSFGSKWKDGSLRTDIPIEALNTYFNVKFSIVSQVNPHVLLWFFNNKGDIGKPVNRSKGKGYRGGFLSSYLENLIKLESIKWLKLIKEFQLLPNFLESDWSNVFLQKFSGTITLFPKVKIWDYFRLLDDPSEERVAEYITNGQSVTYPKILFIKHRLNIERCIEQGRKSCQNDSYEVDDEDDEDDDDEDDDDEDVGLINSDGTLRHRSI
Function: Lipid hydrolase. EC: 3.1.1.- Subcellular Location: Membrane Sequence Length: 779 Sequence Mass (Da): 89092 Location Topology: Single-pass membrane protein
A0A1V1PKQ5
MRRGLPLAYPGMKIGLFGGTFDPAHEGHAHVAETALKRLRLDRIWWLVTPQNPLKPQSSPLATRMKSAGAMAHGSKHVVTDLESRLGRHYTFETLRALKAIYPGVRFTFVMGADNLANFRQWKNWREVAYAAPIAIVARPGVPARDKARMPRTWTWLSARHHTQSSTAIRARKRQAVANRKPG
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1. Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). EC: 2.7.7.18 Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate Sequence Length: 183 Sequence Mass (Da): 20608
A0A220EKL7
TLYFILGVWSGMVGXSLSILIRMELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWMLPPSLSLLLISSMVENGAGTGWTIYPPLANNIAHSGASVDLAIFSLHLAGISSILGAMNFITTIMNMRSNGM
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: 160 Sequence Mass (Da): 17295 Location Topology: Multi-pass membrane protein
A0A6U7DPM0
LMXSAPDMAFPRLNNMSFWLLPPSLSLLLSSSLVENGVGTGWTIYPPLSANIAHSGASVDLSIFSLHLAGVSSILGAVNFISTIINMRPPGMSFDSMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLF
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: 151 Sequence Mass (Da): 16115 Location Topology: Multi-pass membrane protein
A0A076MHF5
MTTTLARPGGGTSTEPAPRPALTRLGPGRTLAELVLGTVAAVVFSLVLQFGSNKLGVDPGTYVPDALVNLAVAVIVVVLFGSLAYSGAARWPLWVRLGGSWAALTALSTLLLAIPLQGTRFFLGGSSVDNTFRLQYLERLTETAGLGDVNYHGLAAYYPGGWFWLGGRFANLLGLEGWAAYKPYSITWAAVSGVVAFVLWSLVVRRRMALLASVATVLAGFVALAPEEPYAWPTTAWLPPVMLLAWHALRSRERVPAWTLLLIGIYLGFSAVTYTLHVAYGVAAVVVLALVALALDVRAGQQPWPVVRRLLLRLVVIGVVTAALALITWGPFILAGGLGKPNVAAHFLPEISAYFPMPFTSANAFGVLCLAGLVWLVLRARRDPVALVMLVLTALSYAWFALSNLALLVRTTLLSFRFIVTVDVVLAVAGVFALVELVRVLPRLIGRVRPVRTVAFALAVLGAVSVSQTIVGTTMKDSVDTAESDYYPDGWTASFGHDPEQDGYWTPELISTIAELTGRPPTGNIVFSAHDRLLSFEPYWGFQQTTPHYANPLAGYTQRNDEIRSWATARDSADLLARLRSNPHEAPNVFVLRRADDGKLLAPVVSDTFPRAVPIRVDEVEFAPELFSAPEFERRDVGPFTVIVDSSAPPIS
Pathway: Cell wall biogenesis; cell wall polysaccharide biosynthesis. Catalytic Activity: Adds an alpha-D-arabinofuranosyl group from trans,octacis-decaprenylphospho-beta-D-arabinofuranose at the 5-O-position of the eighth, tenth and twelfth galactofuranose unit of the galactofuranan chain of [beta-D-galactofuranosyl-(1->5)-beta-D-galactofuranosyl-(1->6)]14-beta-D-galactofuranosyl-(1->5)-beta-D-galactofuranosyl-(1->4)-alpha-L-rhamnopyranosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-diphospho-trans,octacis-decaprenol. EC: 2.4.2.46 Subcellular Location: Cell membrane Sequence Length: 652 Sequence Mass (Da): 70407 Location Topology: Multi-pass membrane protein
A0A158CT56
MTDQYAVIGNPIGHTKSPLIHGIFAEETRQDMAYTAIEGPLEPEQAFAETVRAFAAAGGRGMNVTAPFKLKAFAMADERSERAALAGAVNAMKFENARIIAENFDGIGLVRDIEVNLGLPMAGKRVLILGAGGAVRGALLPFLAARPAEVILVNRDIAKGRALAAQVSARGPISACGYGDLEAMGRFDLVVNATSASLTGDLARFAECLQP
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. EC: 1.1.1.25 Catalytic Activity: NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH Sequence Length: 211 Sequence Mass (Da): 22126
A0A1E3T5M4
MAKCVMVLYPDPLGGYPPKYARDSIPVIDSYPDGSSLPTPSKIDFTPGELLGCVSGALGLRKFFEENGHELVVTSDKDGPDSEFERELHDADIVISQPFWPAYITEERFAKAPNLKLALTAGIGSDHVDLDEARARGVTVAEETWSNSVSVAEHAVMQILALVRNFVPSHQWITDGGWNIADCAERAYDLEGMDVGVIAAGRIGRAVLERLQSWGVHLHYFDIHRLSPELEKQLGVTYHPDVESLARSVDVVSIHSPLISQTHGMFNEKLLKSMRRGSYIVNTARAEETDQKAIVAALESGQLAGYAGDVWFPQPPPKDHPWRTMPNNAMTPHVSGTTLSAQARYAAGTREILEDWFAGKPIRSEYLIVQGGKYAGTGAASYAQ
Function: Catalyzes the NAD(+)-dependent oxidation of formate to carbon dioxide. Formate oxidation is the final step in the methanol oxidation pathway in methylotrophic microorganisms. Has a role in the detoxification of exogenous formate in non-methylotrophic organisms. Catalytic Activity: formate + NAD(+) = CO2 + NADH EC: 1.17.1.9 Subcellular Location: Cytoplasm Sequence Length: 384 Sequence Mass (Da): 42084
A0A8J7NDC2
GIRKSFLRTPQTRGSVPDWSSPCKEGSSDSEMDKAPQAGKKKTKRVRKNRKTAKTEVKDNEEDEGPVEKKRKACECKTEQLKKEEGQSKAFDHRGFTAQVERWPSNPVDSIISYICNKPSSMVVSDFGCGDCKIARRVKNKVHSFDLLPINDLVTVCDMASVCLFSVRIFPDPSPRWLGGCLSLMGTNTGDFLVEANCVLVIR
Function: Probable methyltransferase required to silence rDNA. EC: 2.1.1.- Subcellular Location: Nucleus Sequence Length: 203 Sequence Mass (Da): 22645
A0A540LML4
MHLKNLEASRCSCWSVESDKMWKQNFQCINLQLLMSFEGFIRDKYTALPDTRERILATEITASWKYQYESIFSIPQKPLYFTERYLSVKKALADTFYGPPKEGVYSPSVQSTLYHMAKTVLNGFPDIEAVQLKMPNIHFLPVNLSNKDNTIVKFEDDVYLPTDEPHGSIEATLSRFWSKM
Pathway: Purine metabolism; urate degradation; (S)-allantoin from urate: step 1/3. EC: 1.7.3.3 Subcellular Location: Peroxisome Sequence Length: 180 Sequence Mass (Da): 20921
A0A482I474
TLYFLFGIWAGMIGTSLSMLIRLELSTISNMIGNDQIYNVIVTAHAFIMIFFMVMPILIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLXSSWVETGTGTGWTVYPPLSSIIAHTGTSVDFSIFSLHIAGVSSILGAINFISTMLNMKIK
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: 158 Sequence Mass (Da): 17339 Location Topology: Multi-pass membrane protein
K1ZBC6
MTVHTFGNIAGKKEIELYTHTYVREDTLALYGFGEISELEMFELLISISGIGPKAAMGILAIADPKTIGMAVINEDPSILTRVSGVGKKIAQRVILELKNKIKDMPMHEKTQLESDSDAFEALVAMGYSVSESREALKQISSDITDVGERVKLALKSLGRK
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA. Subcellular Location: Cytoplasm Sequence Length: 161 Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB. Sequence Mass (Da): 17613
A0A1V6F3D8
MNVLIIGSGGREHALAWKIARSPLVQKIYAAPGNPGIDRLDKGVCVNVAADDFEVLRTYIEAERIELVVVGPEDPLAKGIVDTLGTEDTLVFGPSARAARLEASKSFAKEFMARHKIPAAEYAVFDDARSAIDYIRAAEMPIVIKADGLASGKGVTVADSVEKAEAAIRAAMIENTFGLAGQRVVVEACLVGEEASILVFCDGKTFKPLASSQDHKREFDQDQGRNTGGMGAYSPAPIITDAMMDRINREILEPCLRGMEEEGMPYTGILYAGLMITKEGPKVIEFNVRFGDPETQAILPRMDTDIVPILKACCTGTLAEYDIEYKPQPCVTVVMASEGYPGPYEKGKPIRGIESAEALDNVQVFIAGVKQNGEELVTSGGRVLNVTAWAPTLPGAIEKAYAAVERIHFDGAKYRKDIGKKALRHL
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2. EC: 6.3.4.13 Catalytic Activity: 5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate Sequence Length: 426 Sequence Mass (Da): 46003
A0A660TR58
MMNMSLKLNSEIRYIKGVGPSTAEKLNRLGIEIVEDLIYYFPRDYEDRRNLKTLAETDEGEKATFHFKVIDQGYIRFNGRNHPKIKVTDKTGIAYLYCFNRNYLKDILVPGTSFYLIGKYSLKGRYPIFSSFNYELDDNNAKLGIIPVYRLTSGISQNLLRKIIKTVLDSLSDKLKEEIPEFIRKGYKIPPRGEIIKRIHFPPSQRELRRMREAYSYQEFFKYQLIVAMAKSKNKEIKKNRIKSSGELREKFLKKLPFKLTNAQNRVLSEIDRDLDSPAPMNRLIQGDVGSGKTIVSVFAALKALERNEQVAFMAPTEILARQHYNSLKEYLSDLNVKIEFLSSSVKGVKRKELVLKLLKGDVDIIVGTHALFSDDVEFRNLSLVIIDEQQKFGVLQRGKLRQKGKHTDCLVMSATPIPRTLSMTLYGDLDVSIIDEMPQGRIGTETHIVKQAEINKVYDFVKKEVSEGRQAYFIYPVIEESAVLDVKNATESFEYLNNEIFSEFNVALLHGRMSEEEKDKIMQEFKDRKYDILVSTTVVEVGVDIPNATVMVIEQAERFGLSNIHQLRGRIGRGKYKSYCFLIPDKSAGREAFNRLMILKHTNDGFKIAEWDLKLRGPGDIIGKKQAGLPSFIIDDIDINTKLIYRAQKDARKFVNGEIGIEKERELFLNSFIQSESYKRASLYFGG
Function: Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-DNA). EC: 3.6.4.12 Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate Sequence Length: 688 Sequence Mass (Da): 79112
A0A7V0SDR8
MGSGGSRGLQNRRPQSIAAAGSIPAPSALIKKMDTADEIFRKVPQVEKLLQSEGVRDYTPVLGRDVVVGIIRDETRHFRDLLKKNADTPVESLTDAIVQRCRAKKLEKLQRVINGTGIIIHTNLGRSPLAEDILENLKQIAGGYCNLELYLPLKKRGRRGGFAEELLCLLTSAEDALIVNNNAASVFLILREFGAGREVVVSRGELVQIGGGFRIPDIMNQTGACLVEVGTTNITTVEDYRRALTERTAMVFSAHRSNFRMEGFTASPELKELAALKEESLLFVRDLGSGNLVRDGRLPRDFEPTAGYELSQGADLVCFSGDKLLGACQAGIIVGRKDLIARLRKNPLMRMLRVDKISYYLLQETLLCYADGRVDSIKLWDMILQDSAAIRKRINRLLRRVHTPEKKSRFSPVPLKSTYGGGAMPAREIDSAGLRVRVPGYSADEIHTALAHGDVPIIGYVEDDDYFLNFMTVLDRDVNDLAAALNRLADNAPGGF
Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) (bacterial route): step 1/1. Function: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis. Catalytic Activity: H(+) + L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + phosphate EC: 2.9.1.1 Subcellular Location: Cytoplasm Sequence Length: 496 Sequence Mass (Da): 54677
A0A7V1EAG7
MRTFLAADIDNKVNEKIKDFMDRCRLMDRSVKWGKADTSHVTIYFFGEVEEKNIKVLEGTVSEALKQIVPFEASAARISAFPSMKGPRVFWIGIENRTHELEKIYESIKTDLPGKKIKVNIESKDYTPHLTIGRVKGRCDPETIRRMSACSETEFGSFVIDKIILYQSILRKEGPMYSPLKVFQL
Function: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester. EC: 3.1.4.58 Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 2'-phospho-ribonucleotide-RNA + H(+) Sequence Length: 185 Sequence Mass (Da): 21269
A0A918YSE4
MDETLSLGRIAGVRVGLHWSVLVIVALVTVALANGRFPAAHPGHSPFAYWALAVLTALVFLVSLLAHELAHAVVARRDGVQVEGITLGMLGGAVRLRGEAPSPAAECRIAGVGPLTSLLTGAALTGLAMGLAALRVSGLVVEAVAWVGAINVLLAVFNALPAAPLDGGRLLRAYLWHRTGDRLRATRGASAAGRVLGWCMVLSGFADVLFAGHLTGLWPALIGWFLITAASGEARQAQILGMLDGVPVRRVMTPHPAPCRRRRRSPTSWPKGPSAATGTLRSRSWRQTVRSPGCSPCGGWRRHHRRSARARRSAR
Cofactor: Binds 1 zinc ion per subunit. Subcellular Location: Cell membrane Sequence Length: 315 Sequence Mass (Da): 33300 Location Topology: Multi-pass membrane protein
A0A6L7U3N8
MTFSATGPIPRRVVITGLGALTPMGLSAVETWDNVLAGRSGIGPMTRFDPSEIKSKIAAEVKGFDPLNFMSRKESRSLDTYSRFGVAAVQEAIKDAGLEFSREDIQRVGVTISSCVGGIEDYTNSVKTLLKRGMQRVSPFLVPRMLVDSLASRIAVRYGLQGPTMGVTTACSTGLTALCQAFDQVRFGSVDIAICGSSEAAIVPPMVAGFDAMGVLSANNDMPEEAAKPFDNERDGFVIGEGCGIMIMETLEHARARGARIYAEVAGGGMSNDGNDMVAMEKNGIGIQNAMRVALYHAKQLLGIDASDVDYINPHGSGTKLNDKVETHAIKGVFGEHAYDVNISSTKSMMGHLMGAAGSVEAIMAVKSVDEDTVPPTINLHTPDPDCDLNYTPNVAQQRSVQAAMNNSIGLGGNNSSMIFSKPD
Pathway: Lipid metabolism; fatty acid biosynthesis. Function: Involved in the type II fatty acid elongation cycle. Catalyzes the elongation of a wide range of acyl-ACP by the addition of two carbons from malonyl-ACP to an acyl acceptor. Can efficiently catalyze the conversion of palmitoleoyl-ACP (cis-hexadec-9-enoyl-ACP) to cis-vaccenoyl-ACP (cis-octadec-11-enoyl-ACP), an essential step in the thermal regulation of fatty acid composition. EC: 2.3.1.179 Catalytic Activity: (9Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(11Z)-octadecenoyl-[ACP] + CO2 + holo-[ACP] Sequence Length: 424 Sequence Mass (Da): 44954
A0A0W0SMR6
MGKESTPKSSLHPQLQAFLLLSEDCIIVLDANYRILEFNEASTSLLGWKDKEMLGQPFASIYFQLGHKIPFPFYQYELILQNEHGEFEGMLYKNNTKRYFTWKFKRQSNQIILLGKDNTDTKRLALQNVTIFDQIKKISACVPGNFYWKNKDEEYLGCNKILLKTLGLNSMNDFVGKTDLDLWPEHAEELRKNDQRVIKGKKPVLFEETVTLNGKKMYFTVIKMPLIDDEGNIIGILGNSSDITELKRTQADLKIAKEAAEKASQAKTEFLANMSHDIRTPLTGIIGMTKMLEETARSEEERQYASWVNESGEQLLKLLNGVLDVVSADDMNEDDLYLESFYLRDCLEDLNQLEQPAMMQKDISFQLKIDSNIPEYIRTDRFKLSRVLLNLLGNAIKFTDQGMIQLIVDLISSDDQQKSLMFKVIDTGKGIPKEAQEKVFERFYRISPSYKNNHHGHGVGLHIVEKYVELLGGKIGISSEEGKGTTFYFAIPLVPGVAPEIDEKEKIVSSPAVITPSHSPYLLLVEDSIVALKVLERMVMKAGCRYLSASSGEKGLSLAKTEPFDLIITDVGLPGISGNEMTRQIRDWEKQMGSTSQLLIYGLTGHAGQIAEAESLQVGMNGLFTKPMKAINLRTLLESFQSRENGGGKTILSLGIDLPNTEEELFALNNFSLLDIEKGIATLGNLTVFSDLLLTLVSDDLPHEELGIRQAYIQGDWIKIESLAHKLKSGAVYCCTTKLQYACQYLERYCKAGHSKLLEKLYYQLIQVIGETKQAINSWLEERVVSKEVESQIELTSL
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. EC: 2.7.13.3 Subcellular Location: Cell inner membrane Sequence Length: 798 Sequence Mass (Da): 90084 Location Topology: Multi-pass membrane protein
A0A1B1YU95
METVRLVLVTLLLVITFFIYQAWQAQRPQPVQPPSIEQGTLPTPAVSQSAPVPGAPAAAAGPVAPPAARPSGTPVAVSTDVMNVQIDTAGGDITRLDLTAYRAHAGPDAPPYSILDVAPPRLFESQTGLLSAEAGRAPDHQATFTAAANSYQLAPGADTLEVPLSWTDAGSGIEVRKVYRFARGRYDIGLRYEVRNTGSQPWQAQPYTQLMRRKGADAQGSIFMPASFQGAVYYSAADKYRKIGYDDMLKAPLATTLSDGWVGLSEHYFLAAFLLTQGQAQNCYTKALADERFLAGCIAGPLSVEPGQTASWETRLYAGPKAQDSLEDVAPGLALTVDYGKLTVLAQPVFWLMRTIHNFVGNWGVAIILVTLLIKLAFYQLSAASYRSMAHMRKVQPKIMALRERYKEDRQQLNEKMMELYRTEKINPLGGCLPIVVQIPVFIALYWVLLESVELRHAPFALWIRDLSGADPYYVLPVLMGVSMFLQQRMTPMIGMEPMQRRIMLAMPLVFTVFFALFPAGLVLYWFVNNVLSISQQWFINRQLERKAAA
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: 550 Sequence Mass (Da): 60741 Location Topology: Multi-pass membrane protein
W4ERQ8
MTLNPVTTIVLVSPKGNAEDIFARIKIPYEVEYHHVAIDYPSTTSPLDFTVYCSFVTLWRQFMVEHNKAYISTKRTVSINGEIMSPPTTRQAAYRYLAKLSNRQHIVTTAIAVRYLGQLTMVVVESKVTMKKLSQKIIEHYVETGEPFEHDIGYNIQGLGANLSESIEGDFDNVAGLPIDSLQEHLINKKILDVKEGEIVDVY
Function: Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'-deoxyribonucleoside 5'-phosphate + diphosphate + H(+) EC: 3.6.1.9 Subcellular Location: Cytoplasm Sequence Length: 203 Sequence Mass (Da): 22935
A0A3B9UHJ9
MRARGHRAGAARPRHLEFTGTPKLVKKLPYALRGQLVLGSASPRRRELLAVLGIPYSVRTSDADESAPEVLNDVETVRYVARLKAEALVPELSHGEVLLTADTEVWFEGRRFGKPRDLDHAVEMLQTLRGQTHKVITAVCATDGHQWSQAESIAEVTFHRVDDAFIRYYVETFQPLDKAGAYGAQEWFGQLAIERIHGTFDNVKGLPLDTVVEVLGPWLENA
Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. Catalytic Activity: H2O + UTP = diphosphate + H(+) + UMP EC: 3.6.1.9 Subcellular Location: Cytoplasm Sequence Length: 222 Sequence Mass (Da): 24780
A0A972R4H9
MMKIPFTKAQAALNDFVIVDDREGSIPVEARKAFAREACLRRKGIGGDGVIFIEKNNLVEFTMAFYNPDGTDGSMCGNGGRCAALFAYRKGIAGSEMGFEVMNQYYKALILDDGVRLFFPPPKTIRLNFKLRLRDKTVTAHYVHNGAPHVVVFIDDFESASYLSLDDIPVRSLGQEIRLHGDFRPVGVNANFVSIDTDQHVHIRTFEKGVEAETASCGTGAIAAAIVSHAVRNIEPPVTLHTFGGDCLTVGFRPLSEADRVEIIPFIESDIRSAGIGNDLYLEGPAHLVFEGVTCFDEEHLLLVWPEEDRGQVRSR
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: 316 Sequence Mass (Da): 34877
A0A9E7E7M5
MPEPADPLRISDQQQVLQTMETMDEGCRGVGVEECLMRRTLAAHTDYIYTQGNKH
PTM: PSK-alpha is produced by endopeptidase digestion. PSK-beta is produced from PSK-alpha by exopeptidase digestion. Function: Promotes plant cell differentiation, organogenesis and somatic embryogenesis as well as cell proliferation. Subcellular Location: Secreted Sequence Length: 55 Sequence Mass (Da): 6265
A0A7V1EAU7
MRYQVTDLSPADLVIRAALSEDLCVNFGKGLDAFLRGETPDFIDVTTDAVFSAEEKEAHLMAKSSGIISGAVVFKKVYGLIDPGLAVTFYKKDGEGFKKQEKIASLKGRMRSILAGERTALNFLGHLSGIATETGRLTGLLSGTGIRILDTRKTLPGLRELEKTAVVHGGGVNHRMGLYDMVLIKDNHIDGAGSIAGAVNRVRTRHSDKYKIEVECRSLEEVREALSLGVDRIMLDNMTRSTVKKAVKIVNRKTEIEVSGNMNRRRIKKLRKVHVDYISAGCITYAAGNSDFSMKIKPDP
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from quinolinate: step 1/1. Function: Involved in the catabolism of quinolinic acid (QA). EC: 2.4.2.19 Sequence Length: 300 Sequence Mass (Da): 32910
A0A9E5XS57
MKWLAVDYGRKRTGLAETDDLRLVASPLTTVETAGLWSFLDDYLRHNRVERLIVGEPLREDGTHNPLEADIRGFIKKFRKRYPGIAVEREDERYTSKMAFDAMIAGGLGRKKRRDKALVDKISAALILQAYMDRAGR
Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. EC: 3.1.-.- Subcellular Location: Cytoplasm Sequence Length: 137 Sequence Mass (Da): 15681
A0A1I7YCZ6
MSGKEKSQSTSCDNSHQSQRSKRGKWNSNVQFILTCVGYSVGLGNVWRFPLKAYENGGGAFLIPYLFCSMVIGFPVLFLEMSLGQFTSSGPGTIFRKLCPLMQGIGWGQAAMSFVVSIYYNVIVAWTLLYMGYIVIGKWKTFATCDNDHNTECEWPSSYNDPDTKFLLYRVRANLLVVDGRMLFRNCYSNLQKESIWPDDPVDYQFYYNRQNYSYADTKNVTLSLAVLRKALNHTEPTATAAEEFFNYNILRQSPGMEYVGDFNYKLLIALAIAWLITALCLIKGVKWIGRIALVTATVPYIIICILFFRSVTLEGARKGIDFYLLKPNMDYIFKFETWKQAATHVCFSLGIGFGGLLSLSSFNSRDHNCYRDAAIVTFADGFMSIFGGTAVFSVLGFMATETNREIKDVVAGGIGLAFIAYPEAMSRMLGTPYWAFLFFAMLFTLGISSQFGYAEVACTAICDQFPKVRKHRAVIVSCVCFMAFTIGIIMCWGSGIYYFYLFNEHSSSFSLMLLIAAELILVNHVYGYRNYKKDLQSMFGIREKGTTTWSMIKWVIGQAFGRKGFYAAYMMIAICPSVYLAMGIYSFYGLTIDYDEYNGRKFPAWSKPISFFIAGIGVIVLIILAIVNTVVYRRNGKSWKKLVCVQKDWPKRKPAEKKQSETPLLAPENEGTSDGSTAADTIMEVEQVATEGEVLLPQKKFYRQRAHANPMSDHDIVYPRTPKEMDWSPYYGEVPPSSKVEFVDVGCGYGGLLMKLSPMFPDKLMVGMEIRVKVADFVSDKIRALRAKVPGQYQNVCCLRTNAMKYLPNYFEKGQLSKMFFLYPDPHFKKAKHKWRIITPALIAEYAYLLRPGGIIYTITDVEDLHIWMKKHLSEHPLFQELTPAEMESDPVVPLLFESTEEGQKVTRNEGSKFPAVFRRLDL
Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis. Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine EC: 2.1.1.33 Subcellular Location: Membrane Sequence Length: 924 Sequence Mass (Da): 104843 Location Topology: Multi-pass membrane protein
A0A9E7JLS8
MGVRVALHLKGVVDYDFLQERLGEKSQLLLESNPVYKKIPVLIHNHNPVCESMIIVEYADEAWAASGRAIRTADPYDRALHRFWAACIDDEVRVAPRRPTFFCLGWSQCPRHHAAAVGSHR
Function: Is involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+) EC: 2.5.1.18 Subcellular Location: Cytoplasm Sequence Length: 121 Sequence Mass (Da): 13763
A0A5C9CXE0
MIFEAGEIGGMIGAVCKGNLQAKVSSVSLDSRDCGPGALFVALKGERADGHDFALKALENGATCVLAEKDKAHLLLASIPPAMLKDACLVFLDKSLEGLQRLAKEHVRRIKGLLRIGVTGSSGKTTTKECIGAVLRAAYPSDTVAVGKGNLNSDSGLPLALFSLEPFHKAAVFEMGMNRRGEMDELARLFEPDIGVITNIGTAHIGLIGSRMGIAEEKKKIFSRFTGTQKGFVWEDDDFKAFLSLGVKGSVQEFGPRSTQGFEGARSQGLAGWIISWKGLEIAFPLPGKHNLLDALAALSVAHELGLDPAKCALGLSSVKPLFGRSELFGGKISLFRDCYNANPDSMRAVLDLCDEVDWLGRKIYVLGGMRELGDKLSTEHVIMGERAARSDADALFFFGEEAGIAAQAAQKALSAIPLDGNSSGKRPMIFHTSDIDALISRVAAFLREKDLVLVKASRGLALERLTETLFDAGWADREKNSQTSQGARVC
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: 491 Sequence Mass (Da): 52570
A0A7C2KJ69
MFFSIIRRLKSVWFKVFFLRELKIILASSSPRRIELLQEMGIPFDAVHPNVNESIINMDSKQKDVQQVAIDLSMLKALAVARDYPRRLVLGADTLVSVDGEILGKPKDIEDGRRFLKLLSGRKHQVITGISWVYQLKNYSFSEYALTHVYVHRLSDREIEDYLESEAVLDAAGAYKIQGAFFKYIKKLDGFYHNVVGLPMSLVYQSYYRLCGESDKNV
Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. Catalytic Activity: H2O + UTP = diphosphate + H(+) + UMP EC: 3.6.1.9 Subcellular Location: Cytoplasm Sequence Length: 218 Sequence Mass (Da): 25105
K2DVM9
MFLNLLLQYLLPQHILSRLIAKIANCRIRLIKNLFISQYCKFYRIDMTDMLEPNPLNYQTFNDFFSRALKPGARPVTDDKNVIISPVDGRVLQIGKVSANLLIGAKGKNFTLEQLLADNEDAVRFHNANFAVLYLSPSDYHRIHMPVRGKLCSMRYVPGRLFSVNPNVINQIHDVFARNERVIITFETVLGPMIMVLVGAIIVGSVETTWGGVVMPNSQNSVINWDYTKQEIIFERGAEIGGFKLGSTVILLFPEKTMEWNKLSQDAAIKMGQDLGTAL
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 autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, 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. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase. Cofactor: Binds 1 pyruvoyl group covalently per subunit. Pathway: Lipid metabolism. 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: 279 Sequence Mass (Da): 31519 Location Topology: Peripheral membrane protein
A0A7C5MXD4
MYTFLLVIFIIVILLLIPIILMQSGSGAQSGMLGSDFAFGVFGAKTNEVLVKITKWLIGIFMFLAFILGYIKVKEFNAYKARHVKETEEVNKVESQAASSVSETTSESQTNINLPLQGK
Function: Involved in protein export. Participates in an early event of protein translocation. Subcellular Location: Cell membrane Sequence Length: 119 Sequence Mass (Da): 13138 Location Topology: Multi-pass membrane protein
A0A9E0ECT3
MKSANIFKYFILLILSIIFLPALPIFFLIDLSVNLTRKDLCKFLKERYGWLSWIKTYKSFLKSFNNKKDNKLILCLATSAGEIATLEALFEKYSKANFFILTTSITGRNRCCNFASNSKIQYMPIPNFLFTMTIFSLLKPDLFLVVESEFWISYFITSKILNIPIVAVQIRHTMFQKKITELYYYTFIRLCAWIILPEERDAYPDNFPFEKVKFFNTDLKLLKVRVKKANCRKVFCIFASTHKEEEVVFFECINKMIDSFEGIFVIAPRHPQRAKEISDFALKKDLCPIFLSEILDFLTKKVDNIEDTKNNIDNQEFILSLKKKMPLHFKNTDIMKKINNEKLSQFQNANFKNLQNPINRRFIIIVDLFGKLDWLYDHSKVTIMGGTFYDYKGGHNIYEPLLSASFCIAGKYLLNLLSFFKEAEKAGLTSLVSDFNKLDFEILKFWEISKSLENKNGILQFEGSQFEKLYIETQNVKQQILHEFSQF
Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis. Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A. Catalytic Activity: CMP-3-deoxy-beta-D-manno-octulosonate + lipid IVA (E. coli) = alpha-Kdo-(2->6)-lipid IVA (E. coli) + CMP + H(+) EC: 2.4.99.12 Subcellular Location: Cell membrane Sequence Length: 487 Sequence Mass (Da): 57227
A0A9E5XWB7
MENHLFDFDKILLLGTRSPRRRELIERMDIPYRTIEIPFDESRAGAGTPLEMARAKMDAYKGELSSHEILLTADTMVFAGNRRLEKPRDTRQAMEMLESLSGRSHRVVTGVCMKDVLRQTCFDDTAYVYFRELSREEMCYYIHQYMPLDKAGAYGIQEWIGLTGITRLEGNFYTVMGLPAAKVWEEWLRFNGY
Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. Catalytic Activity: H2O + UTP = diphosphate + H(+) + UMP EC: 3.6.1.9 Subcellular Location: Cytoplasm Sequence Length: 193 Sequence Mass (Da): 22498
A0A6S4QPW5
MNESNLSVTTSLTFAKRQGPLRPVKINAALLTGNASSSSELSVIRDALDIPALAVLGSKYVANRLIVLGLLSAGTSTFTGIPVNEDIEIALAGIKGLGAKFSYEEQGTILNITGTGGRINSSASALFLGDNGTFSRLVTPIAALSEKPIVLDASSQMKRRPMSPLFESLTTLGATIVRAHKSSLPSFPVTLSGPLQNNDLTLAGSISSQFISALLLVAPYLNALDKTSAARKPFTLKLTSPLVSRGYVHLTRRLMKEFGVIVDHEEHKGLDHFTVKAGQSYLARPYVVEGDVVAASYFWGLSLIKGESLAITNYPQDSFMGEAAFTSVLEEMGAKFEKITDSNLLSSWGSKQGLRIIPPKSRLRGVTVSMKNMPDVVPTLAVIALSAATPTHLTGIGHLRYKESNRIDDLAVELRKLGARMDIEADAMTIFPLSEKIRTENRNRNLIFDTHHDHRLAMALSLCALMCKTVTLLSAESVAKSFPTYYKVLQELGFTGFTENK
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. Function: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. Catalytic Activity: 3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate EC: 2.5.1.19 Subcellular Location: Cytoplasm Sequence Length: 501 Sequence Mass (Da): 54102
A0A1A3GRT9
MRRLSGEDNSFLAWESAVQPQHTIKAVVLDPAQGHEPITFEAVRAALPGLVDRVEPLQWQLMSPRFGAGRPWWITRARGDLNYHMKRATAAAPGTDRELGAEIAKLFEEPLDRNRPAWQMWYIDGLADGRVALVLKIHHAVADGMASLNLLEQFYSQDPADRLPEPSARPAPDEHRPPTAEWLPMVARQQVKSLTKFPKVLARTAKVTRTIQNRQKSGKPGYAEAFIPPALPFNEPLTARRGFAFVNVEMDQIKRVSKAFGVSVNDVFLAMCSTVLREYQASRGPVGDDTMTAVVPVSMRPQDGDRWGNKVARWNVELATNIADPVARLKAISANTATAREVQSERDAWLQHDWMEYWPLFKVYSRVLPTIGAKVKKRPMFSMIASNMRGPQKTLYFGGAPVEKLISTGPLVFPMGMNITGWSYEGGMQICVLTCTDQVKDPHAIADRLPAALAELVARCETATDSVTS
Pathway: Glycerolipid metabolism; triacylglycerol biosynthesis. EC: 2.3.1.20 Catalytic Activity: a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA Sequence Length: 469 Sequence Mass (Da): 52163