ids
stringlengths 6
10
| seqs
stringlengths 16
1.02k
| texts
stringlengths 117
4.4k
|
|---|---|---|
A0A358DTG4 | VMVGVIITGGFHEDGLSDSADALGGGYDRAAVLRILKDSRIGAFGALALILVLMLKLSLLVDLGTMAPAGFLLGQSLSRAVPVMQLGVQPYARRDDAESKSRDVARSGGVQAMIAAAWVVAIVLGAAYAGLSSAVLVGSLVAMLVVGVVVGVYVQRRVGGLTGDFLGAIQQLAEVGILLALVSP | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)
EC: 2.7.8.26
Subcellular Location: Membrane
Sequence Length: 184
Sequence Mass (Da): 18713
Location Topology: Multi-pass membrane protein
|
A0A498DTD1 | MRNVAPHPVTPPKGIPVPAQNAPLTAPATADAPPLGPVPVLSVSPVELPTPDRAVDLRLRVSAPVTGDRLPVLLLSHGQGMSHHLSSLHGYAPLVDHWAAHGFAVIQPTHLSSRTLDLGPDVPGGPLHWRSRAEDMTRVLDRLDEIEDAVPQLRGRLDRDRVAVAGHSMGGHTAALLLGARLTDPDDGTEVDLTEPRIKAGVLLAAPGRGGDALSEFTATEWPFFRTTDFSRMAAPTLVVAGDADDSAHLSVAGPEWHADPYALAPGPKTLLTLYGAEHGLGGISGYDVAETTDENPARVAAVRRLTAAWLRSTLHAGDPAWREACDELTAGPGAFGRVESK | Catalytic Activity: (ethylene terephthalate)(n) + H2O = (ethylene terephthalate)(n-1) + 4-[(2-hydroxyethoxy)carbonyl]benzoate + H(+)
EC: 3.1.1.101
Subcellular Location: Periplasm
Sequence Length: 342
Sequence Mass (Da): 36061
|
A0A5K1UM11 | MTSLFISPIQLPQVGTIQFRALQKEDYDKGVCSVLEQLTSCSTDKNKFNDVFDLMKKENNYYIVVGEDLSTSQIILTGTLFIESKIIHNGSSVGHIEDIAVSNSYRKMNLGRILIDTLVKLGQVNSCYKIILDCSSSVLPFYEKCGLSKKGHFMAIYF | Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 1/2.
EC: 2.3.1.4
Catalytic Activity: acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N-acetyl-D-glucosamine 6-phosphate
Sequence Length: 158
Sequence Mass (Da): 17750
|
A0A094D9I8 | MRGLQTTLPLLLPALILLHLLAAPYTKVEESFNLQATHDILVHGTPLSDLPTHIRSTYDHIAFPGAVPRTFIGSLILAWLTRAFLHADIFGHARAFGNAVLGTPLHFAHSQLIFHSLVKASAQTTARFILGSLTALSLIRYSKGLSRAYGKSVGGWYVLLQATQFHIPFYASRTLPNTFALLLTTEAARAFLPVPNQNAVGQRSQVRRGIYLLVAAGVIFRAEIALLLTTQVVFLLASRRTDLRTVILAGLPAAFLSIAASVLVDSTFWLRPVWPELASFIFNILHGSSSEWGVSPWHTYFTSSLPKLLLNPLAIPLICASLYLPATKRAAAALVLPQLAYVALYSAQPHKEARFVIYAIPPLTAAAALGASYVWTRRARTVVYRIGALALVGGVG | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 396
Sequence Mass (Da): 43056
Location Topology: Multi-pass membrane protein
|
A0A814RQM6 | MDLFATIPQNGDIRVKDWPLMQSVIPTVLIIVAYIFFIIFGRKWMKNKNAFELRDFMLVYNIVQVILCTYITYEATYVWIKERYSFTCQPIDFSKSETAMKACKACWWFYIMKLVDLTDTILFVLRKKDEQITFLHVYHHITMTFCGWSGSKYVGGGQSLFVIIINSFIHVIMYGYYGLSACGPKIQKYLWWKRYITQAQMLQFVAVIIHSIVNLRQQCIYSVIERTEMRSILCYGDSNTWGFVPGSFGIRERFDRNTRWTGRLQQLLDPAYFYVIEEGLNSRTTNLDYGDRPNGFRGTEFLSVILYTHAPLDLVIIMLGLNDLKKQFNNRTSQQIAEGIKELIDIIRSTTYGSNMQESPAILIVSTPIPVETSSENPSDMFEGAKERIQDLADELKTLVNKYDKNVYFVDAAPSVQMSPVDGIHFDATAHEQFALLMNKTIRKIFNLPA | Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
EC: 2.3.1.199
Subcellular Location: Membrane
Sequence Length: 450
Sequence Mass (Da): 52119
Location Topology: Multi-pass membrane protein
|
A0A220EMF5 | SLYFLFGTWSGMVGTSLSVLIRIELGFPDPFIGNDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGSPDMMFPRMNNMSFWMLPPSIMLMLFSSFLESGVGTGWTVYPPLSTSNFHSGSSVDLSIFSLHLAGISSILGAVNFITTIMNMHSLVLFDKLPLFVWSVLITA | 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): 19379
Location Topology: Multi-pass membrane protein
|
A0A2K3DKX5 | MEFDFASLAFGGEQHISFWDSKRIATLKPDDQELLTKLLDVFGKKSAVAQGLGAPVTDIYRLRSTDQRLYLYMYRESRKTVVLGGLKVGSKRLFVRTGTADLREIEPVCVLDFYVHESCQRQGVGKALFEHFLMAEGHDPATLAYDRPSPKLLAFLRKHYGLEQYVPQSNNYVVFDRYWELCPPGSRQPHRGPGSMPPGASGQLQGRNASRGSVASISTPSGHGGHGPRATPLMGMMPPGSGAGGYPPHWTPSALGSPSGGHPGGPPAPIGNSPSFGRRWASNNFGQGPPQAAPPYPAPGTAGGPAFSIPPAGGDAQGGIVDALDAFARQQQQQGSGASSPQRGGAGAPWEGGAAGPAGTGASGFGGGAGTWPPQGAPELPPAGAPSGMQPPGSRGAYSYRPPWATDEAAGPSGGSASGGVDAGPGAGPGAAGYAGFNSPPPPMRTPSKDRFGMGPGNGGPAPVQRSPMHSILGGGGGYDAVAGGRSGAAQTRALQQQLLSMQAGDGAVAAAAAGGPVLGGGYGGGGGHPGSYQQQQQHAPPSLYSGAPPAHGAGQGGDEDGGRLPGMMGHGSLALGMLGAAPSGRHGAGSGGHAGGPGGGPPGGTSAGTPPAAGGHSAAKLMAVKQRSGAGAADCLVW | Function: Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. Promotes microtubule destabilization and accelerates microtubule dynamics; this activity may be independent of acetylation activity. Acetylates alpha-tubulin with a slow enzymatic rate, due to a catalytic site that is not optimized for acetyl transfer. Enters the microtubule through each end and diffuses quickly throughout the lumen of microtubules. Acetylates only long/old microtubules because of its slow acetylation rate since it does not have time to act on dynamically unstable microtubules before the enzyme is released.
EC: 2.3.1.108
Catalytic Activity: acetyl-CoA + L-lysyl-[alpha-tubulin] = CoA + H(+) + N(6)-acetyl-L-lysyl-[alpha-tubulin]
Sequence Length: 639
Sequence Mass (Da): 63687
|
A0A5E4PH54 | MIKKLLSALLLLCLGFALAGCGFHLQGETRLAPPLHRMYLQTSDPYGQLARNLQQYLKLSKVQLVSSPQEATAILNILHDNTSQELLSVSGTQQTRQYTLKVTVTFEISDAKGRTIISPQTLSESRTMTVQSNQVLGSSNEASLFYQQMRRTLAYAIMKRIASKEITQAIENAFHPDSDQIKP | Function: Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane.
Subcellular Location: Cell outer membrane
Sequence Length: 183
Sequence Mass (Da): 20399
Location Topology: Lipid-anchor
|
A0A060BTW7 | MGGIYPMFGWGLHFCPFIIMGRVTYVHHYLPALYFAMIVLVFLLEHFTRPLREGKTTKKTIIYWSIYIVWYIAVIGT | Pathway: Protein modification; protein glycosylation.
Function: Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+)
EC: 2.4.1.109
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 77
Sequence Mass (Da): 9103
Location Topology: Multi-pass membrane protein
|
A0A4R1LZL4 | MATTCVLERMKFSLSDLAAVDSAIEALRAGALIAYPTEAVFGLGCDPSNDQAVSAVVRLKRRDSSKGLIVIGATLEHIKPYVDWDRLDRGAQTAILASWPGAQTWILPRSPGAGAVLSGSHPGIAVRVTAHKPTADLCTVFGGALVSTSANPSGAPPARTADAVQQYFGTRVDLLLDEPVGSRTRPTPIRDALTGRLLRS | Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate.
Catalytic Activity: ATP + hydrogencarbonate + L-threonine = diphosphate + H2O + L-threonylcarbamoyladenylate
EC: 2.7.7.87
Subcellular Location: Cytoplasm
Sequence Length: 200
Sequence Mass (Da): 20999
|
D9J9Q1 | GSLYLMFSLIMFLIGGAMAMVIRAELFQPGLQLVEPDFFNQMTTVHGLMMVFGAVMPAFTGXLANWMVPMMIGAPDMALPSMNNWSFWILPFAFSILLMSLFMEGGGPNFGWTFYAPLSTTYSNDSTXAFFVFAVHIMGISSMMGAINVIVTIVNLSAPGMTWMKLPLFVWTWLMTAFLLMAVMPVLAGVVTMVLTDKYFGTSFFNAMGGGDPVMFQHIF | 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: 220
Sequence Mass (Da): 24295
Location Topology: Multi-pass membrane protein
|
A0A3S6Z2W4 | MPWAGNSIQPLNYMAVTCTVPAEAVEETVQIFLSWTGAGVEWDDGSPAQAPYTDIPLAPGEPFVRAYFPLDASWPSNQARIAAEARSKGWEVSYREILTEDWENSWKQYYQPISLPEGYQIVPAWSDAVTDDSRHQIVLDPAMAFGTGDHPTTLMCLEQIIRVAPVGQRVLDLGAGSGILAILAARMGAKRVVAVEPDPVAFRALKENVDRNAVAATLILGTLADVPHREVFDLALLNLIADIIIPEWPHLVPYLAQGAQSILSGILSERTDEVAQVVRQSGFQVQSVQHRQGWAMMVVRR | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 301
Sequence Mass (Da): 33079
|
A0A3Q0EZW3 | MVFSSNPLALSVPEPAFESWLRDTGYLEILDHRTSSSAAASPAPSSAAGSLFSRLFTFFSLFTLNPFAKLTADDFAADTPSWSRSFFAFSDSYSFPSSSSQARLRVQENIKRYARNYAYLFILFFACTLYKMPVALVGLILCLALWDFFKFCSQRWGLEHYPLTRQCLIRAAQCGEQSFPTGEIFFFLVF | Function: May be involved in both secretory and endocytic intracellular trafficking in the endosomal/prevacuolar compartments.
Subcellular Location: Membrane
Sequence Length: 190
Sequence Mass (Da): 21522
Location Topology: Multi-pass membrane protein
|
A0A956AD32 | MIETRRFTYFAHHRLYDPNLSEAENDELFGICARGHGHSYTIAVSLDLAVASWGAADDRVRRVLEAILDYTDLNQTVGGIPTGERLVVFLWDRLRPVLAPGALVGLRVEETGRNYFEFAGDA | Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 4.1.2.50
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) + triphosphate
Sequence Length: 122
Sequence Mass (Da): 13666
|
A0A5P9NTK2 | MLYFILGIWSSMLGSSMSLIIRMELGTPGSLLKNDQVYNSIVTSHAFVMIFFFIMPVMIGGFGNWLIPLMLGILDMSFPRLNNLSFWFLPPSLILLIFSNFIGKGIGTGWTIYPPLSNNMFHGDMAVDLLIFSLHLSGISSIL | 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: 143
Sequence Mass (Da): 15957
Location Topology: Multi-pass membrane protein
|
A0A7Y3GXR4 | RRVGRIAGAFAMIVAGERPEKRPLSGRRILVTRGADRAGPWCDALARAGARPVARPLLRTEGVRAPELAAQVARADWIVFTSAEAVRRFGQPTGTAKIACVGELTAEQARRAGWVVEPGPEEASASGLARSLVARGIDGANVLFPCAEGARDVLPRALRGAGAVVERIHLYRTVAEAVDVHALERDMVEGSFDALTFASPSAVEVLFAQLSEAGRAAVRRVPCAALGESTAEALRKWQGSADIVPERPDIESLVAALETYFCREGR | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
EC: 4.2.1.75
Catalytic Activity: hydroxymethylbilane = H2O + uroporphyrinogen III
Sequence Length: 266
Sequence Mass (Da): 28297
|
A0A0T6AZY6 | IDSLYLLIRPKRGMGSEQRLKELFKNPVFNKIRETNPNALTKVRIIEGDVSQPNLGMSEIDREKLAEKINVVFHSAATVRFDENIRNAVILNTLGTKRVLDFASELKNLKSLVHVSTAYSNADRREVEEQVYDPPFDPKSLLNCIDILPDEALDILITKVMGKHPNTYTLTKSMAEYIVFEYSGKLPVAIVRPSIVTAAWKEPFPGWVDNISGITGIMMEIGRGSIKSILCKDNMIMDLIPVDIVANMLVTAAWHTTAYRSNSMRVYNCTSGQINKVSWKDFGSLTQNYARQYPTKYLSWYPGFSYRTNRVAHWIHSLVCQTLPACMFDLILYCTKRKPMMYKISRKFDKALEIGSFFSLNEWDFHTTTVKELHEAVDSAEDGENFNIDISSERGFDWNPYVKDFMLGIRQYVLKDDLSSLPKARVKMNWFYWA | Function: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
EC: 1.2.1.84
Catalytic Activity: a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain primary fatty alcohol + CoA + 2 NADP(+)
Sequence Length: 434
Sequence Mass (Da): 49858
|
A0A1I6K8F2 | MTDRSPAAGVVLAGGYSTRFGERDKALAPVDGTPMLRRVVDRVGRVTDAVVVNCRAGQREEFATVLADCDVPVAFAVDAVPDEGPLVGLAGALAVHDAPETVLVACDMPFVDPAFLSFLREERAARDADAAVPSQGEDIQPAQAVLGTRRARRAVRAAIAAGQTSLQSLYDRLETVSIDEEAITSRGFERSLVDVNTRDVLAARCRRRKTPGRDRR | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
EC: 2.7.7.77
Subcellular Location: Cytoplasm
Sequence Length: 216
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Sequence Mass (Da): 23170
|
A0A1E5P717 | MPRRVPGAAAVPPTAPPVTARPRTAVPAVRRPCGGARDRPLTSLRRAAPALAGYVAVRLAGVLLLAHWAHLKGHGLWPALATSWDSRWYLEIADSGYDTALGTARNSNNLAFFPLYPALIKAVAAVTPGSRAGVGVLLAVVCSLVAAWGIFAVGDRLYGRRAGTLLTVLWGCAPVAAVQWMGYTESLFTALTAWALHCVLTGRWLWAGSLAALAGLTRPTGVAVAAAVSVTAVVALWQARRSGGGPRAAVLAAGLIAPLGWTGYVAWVGVRLGRWDGYLAVQKLWLNDWDGGADTLREVRRLLLYQSRPHLYLVVVTLVLFFSVAMFALCAAERQPLPLLVFTGVMLLVVLGSGGVYFPRARFLLPAFPLLLPVALAVARARRLTAVMVLAATALSSLWFGAYMQLVWPGPP | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 412
Sequence Mass (Da): 43787
Location Topology: Multi-pass membrane protein
|
A0A8B9RLD2 | MMLKQYTALVKKKKRETTSQNLSEQADISLPYFDRLDTPLPDRPYQDSLSAAEKSLKQKEKGPWTSLSNEEKLALYRIMFKETYAEMKRPTGEWKTVVAGILFFMGATGLVVLWQRYYVYPPHPPSFDEEWQAKQVKRMLDMRINPVEGFSSKWDYEKGQWK | 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.
Subcellular Location: Membrane
Sequence Length: 162
Sequence Mass (Da): 19112
Location Topology: Single-pass membrane protein
|
A0A815ISD8 | MIRFPRIVQNILTSTTPEELLLTCVDNHVISSRLTQAVPGNLVSPYEYYKDNSLVGGECAALELAYSKNNMPMIVVFGHSDCKVMNLLYRIRNEISTPSNIPLSQWLKIHD | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 111
Sequence Mass (Da): 12552
|
A0A077ZA34 | MKSSDIQAFSDIPLSKKTLNGLSRSGYATPTEIQREGILLALRGFDVLGAAKTGSGKTLAFAIPVIEYLWRQRWTAGFGLAAVVISPTRELALQTYETIRKVGCFHEFSAALIIGGTVGFPRLYFMILGCRFGETPYKSLQHDLAHSNCLVLDEADRILDLGFAEQLNAIFANLPTDRQTLLYSATQTKSVTDLARLSLNEPVYISVHEYSKFSTPDRLDQKYAVVAEEDKLNFLWSFLRNHTKLKILIFLNSCRQVRFVYNAFCKLQPGLSLLSLYGTMPLKKRVAVFEDFARKQHAALFATDIAARGLDFPAVDWVLHLDCPSDVNEYIHRSGRTARYVNKGRALLVVTPNQTSLVTALQNAKVPITETKINPDKLFSIQKKLQVMCAQDSVLKGFAQRAIVAYVKSIFFMGNKEIFDAEKINLQAVALSAGLVCAPRIRFMERRQSKPASSESASNDVQSSTSFFGQEEAVDDDDSDDFLKVKCRDVFGQLAVLSRLGVQTEETDNESSDDVDISWLPDPDKLQAVTNEQDNVSEAK | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 540
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 60190
|
A0A972I9R0 | RLVVIEMNPRVSRSSALASKATGYPIAKIAAKLAVGYRLDELRNDITGTSAAFEPTIDYVVTKVPRFAFEKFPGADPRLTTQMKSVGEAMAVGRTFKESIQKACRSLETGKDGLSSLLDRVDYRDFVQQVRQLVSDGPGQSLTYNAPKEDLPPATEEELRAAILEVVRTPLGERLFYLGDGLRVGLTVDELHAATGIDRWFLVQMKEIIDEERALAASKGRPLTAEEFRRAKEMGFSDSQIARLRGEDPVKVRAARKAASVTPIYARVDTCAAEFQALTPYLYSTWGRDCEADPTDRKKVMILGGGPNRIGQGIEFDYCCVHASFALREMGFETIMVNCNPETVSTDYDISDRLYFEPLTYEDVMNIVEVEKPDGVIVQYGGQTPLKLAVPLARAGVKILGTSADAIDRAEDRERFDAILEALGLRRPRGGIARGVKEAFDVADSIGYPVVVRPSYVLGGRAMEIVHSRSDLARYMKTALEALEGAESQTILIDEFLKDAIEVDVDCVSDGTQVVIGGVMQHIEEAGVHSGDSALVLPAHALPAGVLAAIRSSTRALALELGVVGLMNVQYAVRGSAVYVIEVNPRASRTVPFVSKAIGKPLARIGAQVMAGKKLAELGFTEEIVPTHVAVKESVFPFAKFPGVDTILGPEMRSTGEVMGVAETFPEAFHKAMLSVNAILPDAGKVFVSVRDDDKQAACELGLRLSQLGYTIVATSGTRRALARVGVDAELVYKVGEGRPHVVDRIRDGEIVMVVNTTEGAETIRDSRSLRRQTILAGVPYFTTIAAAIAAVEAIVVKRKKPLTVKPLQEYHRSS | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
EC: 6.3.5.5
Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
Sequence Length: 815
Sequence Mass (Da): 88588
|
A0A2S7UYH2 | MTGKIAGAFFGFLLLRNIIGALIGLYIGHLFDTAIKRLTNKQNVQEWLTSDDSKQAIFFYTTFSVMGHVAKASGNVTAEDIQTANEFMTQMHLSGEQVNEAKEAFNEGKSLGFPIKKKINLFKQYFGKRQDLCQFFIEIQIQTAYSDSILEPAEYELLLNIANQLGFTKRHLGQLIVIWEAELRFQNYKRDQQQKNRRYERRRTGSNNNQSQQQGRQQNHHHSASESPSILDAYALLGITDKESVQEIKRAYKRLMSKNHPDKLVSKGLPPEMMEVAKQKTQDIQSAYELIKKERGF | Function: Regulatory DnaK co-chaperone. Direct interaction between DnaK and DjlA is needed for the induction of the wcaABCDE operon, involved in the synthesis of a colanic acid polysaccharide capsule, possibly through activation of the RcsB/RcsC phosphotransfer signaling pathway. The colanic acid capsule may help the bacterium survive conditions outside the host.
Subcellular Location: Cell inner membrane
Sequence Length: 297
Domain: The transmembrane domain is a dimerization domain.
Sequence Mass (Da): 34146
Location Topology: Single-pass type III membrane protein
|
A0A8S2Q7X4 | MEKFNSRITIFQIDKQHLKLLRHIARGIPLFHSPRFIHLPTCYADLLQSNLGRQCFYCRKSIIQPILCLICGIVHSKEDTEKKCCHQHILSIKEHLISCNDGLNLSINIHSTETLIQRKQRYNYWSSLYLDKYGEEDIHLRRGRILYLNEDRLKLLYSAWISSNLDQLSNTSSIDEFDF | Pathway: Protein modification; protein ubiquitination.
Function: Ubiquitin ligase protein which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation.
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: 179
Sequence Mass (Da): 21166
|
V8NGI0 | MDWKTLQGLLSGVNKYSTAFGRIWLSVVFVFRVLVYVVAAERVWGDEQKDFDCNHRQPGCTNVCYDFFFPISHIRLWALQLIFVTCPSLLVIMHVAYREDRERKNREKNGENCPKLYSNTGRKHGGLWWTYLLTLFFKLGIEIVFLYLLHRIWDSFDLPRLVKCDLKPCPNTIDCYIARPTEKKIFTYFMVGASALCIVLTVCEIFYLIFKRVIRSMNKWKKNKKSLTYSKASTCTGFQEHLQDSNDHRMGDWGFLEKLLDQVQEHSTVIGKIWLTVLFIFRILILGLAGESVWGDEQSDFVCNTKQPGCTNVCYDNAFPISHIRYWVLQFLFVSTPTLVYLGHVIYLSRQEEKLKERESELRALQAKDYKVATMLMAVEKKMAKICVAEDGRIKIRGPLMFTYIISVIFKTIFEAGFLLGQWYLYGFVMHANYVCQGSPCPHHVDCFMSRPTEKTIFILFMLVMGLISLVLNILELLHLFCKHLVKKVKESDCCSPSSAPPLPFDANSIGKMPTGPYPPDKPYFYLPMSDRQAPPYQGYNKLSSEQNWANYNTEETLALQNQINPPDLFATGAPKTHLSPERQSSRPSSSASKKQYV | Function: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
Subcellular Location: Cell junction
Sequence Length: 598
Sequence Mass (Da): 69041
Location Topology: Multi-pass membrane protein
|
V8NJE5 | MDCTTNISQYVHRMEESEPLRKYFNSTEDYLLFLYGPKHSHLSLPVTWIYALIFIVGVSGNLLVCLVILKHRNMKTPTNCYLFSLAISDLLVLLFGMPLEVYEMWSNYPFLFGLVGCYLKTAFFETVCFASILIITMVSIERYMAVLHPFRARLKNTQQRALRIILILWFLSVLFSLPNTSVHGIVLQYFPNHTEVPGSAICAVVKSMWIYNWIIQLTSLLFYVLPMSVISVLYCLMGLKLRRDRSLEIKEMQMNIKLSSRKSITKMLAHPGFDELGIYQIQKLYTLLCSPSLSDSCPSNRFWGMLGPIPHRSSFLQLCYNLDRTSCKYIQPNSCGFSANTGTLNIPQAIPHLS | Function: Receptor for the neuromedin-U and neuromedin-S neuropeptides.
Subcellular Location: Cell membrane
Sequence Length: 354
Sequence Mass (Da): 40624
Location Topology: Multi-pass membrane protein
|
A0A7C8DGC4 | MVRDCVESSRSDRDILVLAVLDSKNSLTTKRTSPFDLDRPVLCLVIDRSCSVRPVLEAIEAAVAAGVDWLQIRERGCESGELLSFAQDVHAAAERGANGRNVRVLVNRRVDIALATQAAGVHLGFDAMSPTDARTMLGGEAWIGTSAHSTKDVEAAAQAGVDYVHLAPILRPLSKAATRPALGYAVLAEAARLGVKVLAQGGLEAQHCGDALAAGATGIAVTGSILMSPDPGKAAAMLRSALDTAAGG | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
EC: 2.5.1.3
Catalytic Activity: 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Length: 248
Sequence Mass (Da): 25658
|
A0A956DW67 | IDFWGVALKPGKPTASGRLGTTRVLGLPGNPGSATLTFCLFGMAILRTLQGDRAPRPRPTRMPVRGGLRRRPGREEYLRATLELEAEGWVARLHRGQSSGAVTSFARADALVRVPADQAEVVDGASLDVFRLADF | 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: 135
Sequence Mass (Da): 14568
|
A0A4D7QDF9 | MPQRFRDSLLLEALGTLCSEAGARIMSHYGASATMKADGSPVTAADNEAEEIILAGLATLLPGVPVLAEESAAAGRLPASTDLLIAVDPMDGTREFLAGNGEFTVNIGLISAGVPIAGLVYAPARERLWIGMGDKAEAMQIVPGAPIASASQRSAIRTRSLPPEGALALVSRSHPDAGGEAYLAKHHVTHRLAMGSSLKFAVIAEGGADVTVRFASITEWDIAAGHAVLAGAGGRVTSPEGAPLVYGRADKAFRTDAYVAASAAFGAT | Function: Converts adenosine-3',5'-bisphosphate (PAP) to AMP.
Catalytic Activity: adenosine 3',5'-bisphosphate + H2O = AMP + phosphate
EC: 3.1.3.7
Subcellular Location: Cell inner membrane
Sequence Length: 268
Sequence Mass (Da): 27370
Location Topology: Peripheral membrane protein
|
A0A3A4JBC5 | MNVVAILCKRGTAGTPDILNGLIRYLDGKIKTLRIAEGVCCGEGQAEVVPEEKLGDGADLLIVLGGDGTLLHAVKLLRGRDAPILGVNLGRLGFLTEIQLSELYPTLDKILAGECPTQIRRMLHATLTREGKEILSQDVLNDVVINNGALARILRLHVGTAQGFMTSYRGDGLIISTPTGSTAYNMAAGGPVLYPTLATFALTPICPHTFANRPVVLPDDEEVIVELTEATSDVHLSLDGQAGAVMRQGDIVRVRRATTTARLVRSPTRGYFDILREKLGWGQD | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
EC: 2.7.1.23
Subcellular Location: Cytoplasm
Sequence Length: 284
Sequence Mass (Da): 30503
|
A0A0T6B7Z4 | TKSPILRVTQMNAIYFDNQIYKMLLGHVQDCLKHFHPQYTQLLSNEVELCMKFAILWFSIGRCDSTFGQKLLCTKYENITPAKKLVLGISLFVEYAVDKLQLLTDNMLLNNTAMKLKNLIHFCQFLNISIFLRNGLKPRLLERILRLNLSHDELKIAQRQYNSHYMMRELLWDSFIEILIYVLPLVNYHKMKRSINHLNPFRQKLVLSKPIVAQLTINTKCPHCNESPIIPHSMGCAHVFCYICLKLMTSRYEKSYALLCIWKRNFYFSDMSSIYPRGTRSQVRISLSNIIHHSII | Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Membrane
Sequence Length: 296
Sequence Mass (Da): 34822
Location Topology: Multi-pass membrane protein
|
A0A143FRK5 | TPQPGVPPEEAGAAIAAESSTGTWTTVWTDGLTSLDRYKGRCYDIEAVAGEKNQFIAYVAYPLDLFEEGSVTNLFTSIVGNVFGFKALRALRLEDLRIPPAYSKTFIGPPHGIQVERDKSNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFVAEALYKAQAETGEIKGHYLNVTAGTYEELLKRAHCARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGERDVTLGFVDLLRDDYIEKDRSRGIYFTQDWVSMPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGT | 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: 364
Sequence Mass (Da): 40306
|
A0A1D2QX67 | MNIKKFKDSEKILLAYMQLIRLKNCAIVFFAIFITAAMVSGEISISEKIFFAAAAAFIITAAGNIFNDYYDYVIDKINRPDRPIPSGKVKRSDAMMLSLTLFLVGIALAYNINLICFAIAGVNVIILMIYARYSKKMLLVSNFIVSYLVASVFIFGGLAAAGEIVEAKPIFVLSVCAFLMTFSREIVKDIEDIKGDEESGAETLPIQIGADKAKNVAVIFLVFAVLLGFVPYIFKLINNLLYYLIVIIIADIVFLYSLTKQPKESQKMMVAGIVIALLAFFAGSVF | Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Function: Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.
Catalytic Activity: (2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate
EC: 2.5.1.42
Subcellular Location: Cell membrane
Sequence Length: 286
Sequence Mass (Da): 31580
Location Topology: Multi-pass membrane protein
|
A0A0T6BDL4 | MDAGGDRILHSTHVAVIREVYDGEFAPQGFAMELERALDACCSVIVIEPTQLGDETARWISVGNCLHKTAVLSGLGSIVSGLLWPNNVYIYAPLGTFSTLCI | Function: Plays a role in mitochondrial morphogenesis.
Subcellular Location: Membrane
Sequence Length: 102
Sequence Mass (Da): 10967
Location Topology: Multi-pass membrane protein
|
A0A956AA30 | YHRTIDRLREERLGDGKVGTTGRGIGPTYEDYVARRGVRLHDMVDEESLSAALDRVLDERNAVIEWLGGEPCAKDAIVEEHLRYAERLRPFLCDVTPLLVQASKSNEEVIFEGAQGTLLDVTHGTYPYVTSSSTIAGGVCTSLGIGPQEIDLIIGVAKAYTTRVGAGPFPTEQDNELGELLQQRGNEFGSTTGRRRRCGWLDGPALRYAVRVNGITSLAITKLDVLSGLDTIKVCVGYEYKGDILSELPTNPRILAQSRPIYEKFGGWQEDISQATSYDDLPDAAKDYLHWIEVLANRRIVMISCGPGRGQTLLRDIGLYKEISKEVVGESGSVG | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Function: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
EC: 6.3.4.4
Subcellular Location: Cytoplasm
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Length: 335
Sequence Mass (Da): 36790
|
A0A5C3EU07 | MASQQPTQQKVSSEDIISQKTDLCISNAIVKTGIGFSAGVVLSVLLFKRRAFPVWLATGFGMGSAYTDCERSFNPVAVPGIRVVPSGPSSVSASSNAPQTTFEKLQQKAGEAFGAAKDKAAAGVEKAQDKSADLAERAQDKGREAVEKAKAEGQKLEEKAYRIHSPSEGAAPAGASVRLPGSDCLGCRLTGFAAMTGMGAYSLAEAYKMGAFRRGPLPSGAKARPVWGASLVVFGIGCIGAGVIRLGM | Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 248
Sequence Mass (Da): 25659
Location Topology: Single-pass membrane protein
|
A0A0S1HRH7 | MVMPIXIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLMSSLVESGAGTGWTVYPPLSSGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTIINMRSVGMTFDRMPLFVWSVGITALLLLLSLPVLXGAITMLLTDRNLN | 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: 148
Sequence Mass (Da): 15754
Location Topology: Multi-pass membrane protein
|
A0A0T6B3U1 | MLILGAWHKTKSLRLICLGILVHVSLFFGVLDVYFSSPVEFGLSSFKTNFSLADRVVVFIADGLRYEALGDVNFDGHTPFLNKIRRQYGVWGVSYTRVPTESRPGHVALFGGMYEDPSAVLSGWKHNPVNVDNVFNQSVESLLWGSPDIVPMFNRDNLKKINTHCYDTSFEDFSGRKSTIELDKWVFEHVKDYLNRTSVQRLQGGGKIFFLHLLGMDTVGHVFKPNSREYIDNLKYVDKQIGNMFNLFQAFFEDNKTSYIFTSDHGMTDWGSHGSGSEHETESPFIAWGSGLKRYEEPCYLHQADVAPLISALLGINFPTNSVGLIPYMYLNATMYEEVLLLYTNMRQLGERFNKRHERIQCATVYGFFKPFPWLNEKIFAKKINQIEGTIEKRSYEVAVGSTTSENNHLNINLYFIEGRYFRVNRINSRG | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Function: Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor.
EC: 2.-.-.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 431
Sequence Mass (Da): 49448
Location Topology: Multi-pass membrane protein
|
A0A1E8D1W4 | MPSGRDLAPVPDRLRWGLHLLVAALLVLVALRGITSPSGMDGTAAPWPWVVAGCALVGAIYAAGPLSGVVADSSGASAVWLGLLLVAWVGLLALAPEAVYLAFPWFFLLLHLLPRRVALTAVFLTTVAAIVGFAWHQNVFTVAMVIGPVVGAGVVIATVFGYQALQAESEQRRRLIVELDRARAELAVAHHRSGVVDERARLAREIHDTLAQGLSSIQLLLQAATRSLDPAREVDAERAANLVEQARQAAKDNLAEARRFVQALTPVDLDQSTLAAALRRLCETTTARSEIAVTFHEVGAPTALPTPVDVALLRIAQGALANTVQHSGATRADVTLTTADAVVSLDVVDDGAGFEPGQGDATDAAARARGDDGVSASDGTGFGLRSMRERAALLGGRLSVESRPGAGTAISVHLDRPIESAEQAMTVERVP | Function: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and transfers its phosphate group probably to a conserved aspartate residue of NreC. NreB/NreC activates the expression of the nitrate (narGHJI) and nitrite (nir) reductase operons, as well as the putative nitrate transporter gene narT.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cytoplasm
Sequence Length: 431
Sequence Mass (Da): 45157
|
A0A1S3TD48 | MVGVILFCIGEDDLLLWLAKVVLSATLTRDPGRLVQLNLRHPLFLSAGKMRYRLPENLESFKLICERKVKPLYLVALLKSLGEEKCIVFTRFVDSTHRLCKLLNCFGDLQIDIKEYSGRQHQRVRSKTLNEFRKRQFQVLVSSDAMTRGMDVEGVRNVINYDVPKYIKTYVHRAGRIARAGQTGRWFTLMSNDEEMAPAASSNMVPASPPPSFKRNDPRKPNKKTLDQEQDVNDNPSSVSMDCKVRLQAPLDHQVQFDDHVVIQGSAKELGSWNKNVPLN | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 280
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 31940
|
A0A5E4PER0 | MLKQRIITAVILIPVMLGILFYLSAPWFLIVTGLISLGAAWEWSNLMQVRSFAGRLLYVLIAAAAFVSAMFIPVTLIFAAAFVWWLLALFLVLCYPLCSQWWGGSVFARGLMGILTLLPCWAAVNYIRSQAQGLYSLLFLFVLIWGADSAAYFSGKKWGKTKLAPLVSPGKSWQGVWAAQVCSVLIALLTLWICQIRYAVWPWALLLSLVTVMFSIVGDLFESMMKRQAGLKDSGRLLPGHGGLLDRIDSLTAAAPVFVLGGILLGSYLN | 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: 270
Sequence Mass (Da): 29700
Location Topology: Multi-pass membrane protein
|
A0A5E4PL71 | MITRETMDFDVVIVGAGPAGLSAGIRLAQLGEQHHHPLNICIIDKGETIGAHILSGAVLEPRALDELIPGWRDKNPPLHTPVSHDQFLFLTKNRTWRLPTPPQMQNHGNSIISLGLLCRWLAEHAENLGVNVFPGFAATEVIYDGNRVCGVVTGDKGLDRQGQPKPTYQPGIELRARQVIFAEGCRGSLTQTLFNRYDLRKNSDPQTYGLGIKELWEIPEGLHQSGQVIHSVGWPLDTRTYGGSFAYHFGKNLLAVGFVIGLDYENPYLNPYEEFQRFKTHPCMRPLLEAGNRIAYGARTLIEGGLQSIPKLTFPGGLIVGDAAGFLNVAKIKGIHNAMKSAMVAAESLYPMLLNTTEQECTAYPDNLKKSWLWDDLYKVRNIRPSFRWGLLPALTYSALDTYLFRGRAPWTFRHKIPDNQSLKKASLCKKPDYPKHDNKVTFDLPASVFLANVSYDENQPYHLKLKDRHGIPVTVNLREYASPETRYCPAGVYEILYNDKNEPRLQINGGNCIHCKACDIKDPTQNIVWTPSEGGSGPNYEMM | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Accepts electrons from ETF and reduces ubiquinone.
EC: 1.5.5.1
Catalytic Activity: a ubiquinone + reduced [electron-transfer flavoprotein] = a ubiquinol + H(+) + oxidized [electron-transfer flavoprotein]
Sequence Length: 544
Sequence Mass (Da): 60891
|
A0A059EHT6 | RNWADFDPKELFDMPIETKIIDSSIKRNLLSLSQGVDKIIIWTDCDREGEFIANEIKELVGHRSVKRARFFAISRGEITNALNNLVEINLKEAEAVEARIELDLRIGAAFTRIQTLALKGSVKSYGSCQVPTLGFIVERNEAIKDFISEDFSSLNVSIKKEKENLFSWQRGNFFDKNFVNLFYDILNKENLQVVSIESKAVKKFKPYPLRTVELQKKCASALKISPDRAMKIAEDLYNKGYISYPRTETDSFPPNFNYNQILTKLSSEELYKYFKDFEYP | Function: Introduces a single-strand break via transesterification at a target site in duplex DNA. Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand.
EC: 5.6.2.1
Catalytic Activity: ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.
Sequence Length: 280
Sequence Mass (Da): 32374
|
A0A7Y5LQ86 | MVCQWTALTGEFVYDDLPAAVENPNARLPLRLRQILTEPYWGLRPGTEQISLIRPVVTFSFAVNEAVTGFVPTGYRAVNLFLHSVASCLVMLIASVVGVPLLWSFFAGVLFAVHPIHCEAIAATANRTEPMCAVFYLGSLLCYFLARSATKRETAIGMIIGSLALFSLSLGSKEVAITLPVVILAIELMMRYVRVPSPWGRGFLNPAATVGDEIGHLPTARTLRVPSPILPPLFGLGLVLILLLYFLYRSMVLTSPFSANVSPGDNPLIGSAGLERWATPFSQIALATELLLYPARLSVDYTAAVVPVVQTMADWSFLAGVGCLGIVVVGLIVAVRRKNIPIIVGLCLLGGSYALISNTVILATIFFAERVMYLPSAGFSIVSGALLASVRWNRSKLTTTLVGVVVVVALGVLAVRSWERNKDWQNDERLFSSSLFARPNSSRLHTNLGRLSMLNQNWELSVLHLDTALRIYPENAQALMLRGQLARRMSNSEAAIEYFDRANASLGGKHGRALAELCSIYSERKQTEQAGDVCRRAIRLRPDHPDTWTAFGDFANLQGDTGLADNSYRRALDLEPTNLHALNRLGRLLAETHKYGELLDIMFRILEQNQGNAALIHDIEGLTMKVAAEAVRTKDIGLARTILSRARDKLGNPERWNNMIGELP | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.109
Subcellular Location: Endoplasmic reticulum
Sequence Length: 664
Sequence Mass (Da): 72776
Location Topology: Multi-pass membrane protein
|
V4YES3 | MGGQLPSVAHPEFVPNPELTRDEMRTLQREIADMAVYTDSGDASGGRRSDRRLTPPEPAAVSLDEAADLSDGVPEPSNTVSDTDHQEPVVVGIDQAFLAERVISAAVALCGNEVVERASAVTPLKIPYIPGLLAFREGGPVLAALDQLQISPDVLILDGSGRIHYRQAGLATHIGVTTETPAVGVAKSLLCGVPDDSVDGRPAEWSTPIRADSQVESADETVIGHAYQSRQYQNSPRINPLYISPGHGLGAVRARDLVAALCGGYKLPEPTRLADAFADELKREFDSQ | Function: DNA repair enzyme involved in the repair of deaminated bases. Selectively cleaves double-stranded DNA at the second phosphodiester bond 3' to a deoxyinosine leaving behind the intact lesion on the nicked DNA.
Catalytic Activity: Endonucleolytic cleavage at apurinic or apyrimidinic sites to products with a 5'-phosphate.
EC: 3.1.21.7
Subcellular Location: Cytoplasm
Sequence Length: 288
Sequence Mass (Da): 30634
|
V8NMY0 | MSFFAERFFALFDSDASGTISLDELLKTLKLLVHGNETDKLRFLFQVYDVDGGGSIEPDELRMVLKACLKESSISLPEEKLDDLTRALFESADSDKSGSITFEELRGELQCFPEIMENLTISAASWLKPPTAPRKSQTPHILSPVYWHNNKNKLLLLGSYACVNIILFILAALKQAGSGIWIVVARGCGQCLNFNCAFILVLMLRRSLTWLRTTWVAKVLPLDLNVILHQLMGYMVGALTILHMGAHVINFVRLSQAKGGYHLWEYLFTTRPGIGWIRGTASLTGLVLQLLISLMLVCSTTLVRRSGHFEKVTILLFLSHQQVFYWTHLFYIPIWALLIVHGANFWKWFVIPGSLFLGEKAFAAALSRVGGLYIVEVNLLPSKVTHLVIQRSPFFHYKPGDYVYLNVPVIARYEWHPFTISSAPEQPETIWLHVRSLGQWTYQLHEYFWNFQEPFDDNPESSVARKSRNKNRLSSFVQKCLFCSSDLDLPVATTKDEMIQMVSYTPIQDSSITVTDKPEEVSGRPIKNHRLCNIKCYIDGPYGTSTRRIFSSEHAVHHMRKQASCSHRNSLDENMKLQKSSPMQAQGWNTLLSPLGKPSLFELYEEYQTRGMRDSWQAAFLVHVIILLILGFKH | Function: May be involved in the cellular control mechanism of the secretion of toxins from the gland into the venom.
Subcellular Location: Cytoplasm
Sequence Length: 634
Sequence Mass (Da): 72244
Location Topology: Multi-pass membrane protein
|
V8NBW1 | MAMAPGPAWMPRRTGAHRSLEKTLQGLTKLQQLACQPQVALRNSAPHLPSLLPLIYQHLKLIREHYGAGLAEVWESDFFRIFLLNLLEKIKQATQLFKRGKDKEEILLEGSAASHMLAELQAVFPNGEDQGSTYQLSKQEAQVFWRGTWRERFFLAKSCWLCNVNLMAFSTICFASPSNSFPVFSSQPWPTLLKNWTYLAVTHPGYMAFLTYDEVKARLQAYVNKPGSYIFRLSCTRLGQWAIGYVTADRNILQTIPQKKSLFQALVDGHKEGLNSLSSTARWNPPSSFAKSAPRTTRMFKSVRAGIFSAGNALSHGSFQNLPPAPFVARRSGAMKMWRSAHTAPRRAAPPPRTRATRGTWRMWTWCCNS | Pathway: Protein modification; protein ubiquitination.
Function: E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome.
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: 370
Domain: The N-terminus is composed of the phosphotyrosine binding (PTB) domain, a short linker region and the RING-type zinc finger. The PTB domain, which is also called TKB (tyrosine kinase binding) domain, is composed of three different subdomains: a four-helix bundle (4H), a calcium-binding EF hand and a divergent SH2 domain.
Sequence Mass (Da): 41811
|
A0A0N9GVB2 | TLYFIFGAWAGMIGTSLSILIRTELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWMLPPSLTLLLASSMVEAGAGTGWTVYPPLSASIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVVITAILLLLSLPVLAGAITM | 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: 192
Sequence Mass (Da): 20465
Location Topology: Multi-pass membrane protein
|
A0A363TX36 | MIDETFWVAVAFLIFIGILVYVGAPQMVLKSLDDRSQRIKAELDEARRLKEEAQKLLAEYQRKQREAEREAEAIIESARDEAERIAEEAKGKMEEFVARRTQLAETKIAQAEQQALADVRAAAAEAAVRAAERILTDTVKGKVADDLIAEGIRDVKSKLN | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria.
Subcellular Location: Cell inner membrane
Sequence Length: 160
Sequence Mass (Da): 17940
Location Topology: Single-pass membrane protein
|
A0A0L0V7U7 | MAHMRLVPLHSRLRSIRPCPSLSKPSTASQSLFSNGFTPRSYSRTVGRPSHQRSSRPTNRPFSTDLCRARPTPGYALLAAALGLGALVSGATVYALESPDSFADPLEALSPDTLRLKTAHVTQKPCQDLLRSYLTLLLCEMPGVATYGPILLNHCISLRDNVPVIGPAAWTVVEWFVYHTFFSHYTGGESAEDCQPVMEALYAGKVGSLLNYSVEALERSGGGGKESGLSLESVAAISRAVDSLAGYELGAKGYAPGSARMKPSSVAIKVSGLVEDPYLFKRASENLQANGLSPFRARGSPFPKTSPSSPDPLSPSDHLALDGLMDSLRSICQKAKSADIVLMIDAEYSWFQPALDRIATFLSAEFNKAQPKGSKGESYSPTVFNTFQALLRSTPARLAEFVDEGHQQGFSVGVKLVRGAYLVSETAKWREARAAGQPDVPEHPPVWGSKAETDGCFDDIASSLVQRLANNARRAEGLTSHPRQSTTSSPIEVAMMIAGHNPLSAAKVLKQLRDEEGLAKNMDSQCISLSDSLRGRLMFAQLYGMADNLTSTLTDILAPSDAGQRQPQPFVFKYLPFGPVDKVLPYLARRAEENSSILEVKDGESVLSLERKLIGKEIRKRIGSLFFFS | 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: 629
Sequence Mass (Da): 68146
|
A0A0L0W2F9 | MARPTSPCSSEFDTKLDLWTQLQASEESEPSASTSAITLETANQPVDTHERIKRSSSTEETSTLTNRVKPTKSLEKRAREPEEDEEKLDKKIKPGFSKSPRPHDDPSTNSPDNNPPVPAPKSKAPGIQSLGNLTCAICLSSPSPAAVTKCGHVVCGECLASSIVSQHNSSFGSFPPFMQPAGTQINNGQCPVCRAALVGGWGTAMRGAIFKIGNPS | Pathway: Protein modification; protein ubiquitination.
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.
EC: 2.3.2.27
Subcellular Location: Nucleus
Sequence Length: 216
Sequence Mass (Da): 22961
|
A0A7S3HH73 | MWSPANILLNRLRRMLFRLGAFAAVMGSLLAINVYGDYNFFIVTCVVGAVYIIFGASIEKWCEKNILYSKSVNVPSRDLHDQRRYKTYPSANANSWYHFVDSDALKNEGVIEFRALGRVFVLWRDSNGKPVCQDAFCIHQGANLGVGGVVEDNCIVCPFHKWKFDSEGTVTEIPYLKDPTGCSGLKNRKQKTYPCMDWNGLLLVYFHVDNKDPEFYPPEYVTEEFKKDNWQPHMKWDVGFFTFSPVDWVDQAGDHAHFQTLHADFMIPWTNLRFPDWFYRLIPVGICHTCITYRGDDKEWAEEVKNTGWGAVGKHLLFFTDLAGLTWKRKPMLTTLSPTKEMFVGPGMILFHIPFTIGTIKVFVTTTPVDGGSILRVRTWVDGRVVRNPLIKALAVVLTGISASQLNADVSILENKIRLRKPLIQPFDGPYNRVNTWLKQFYSESSSTNGYSCDAYKNDW | Pathway: Steroid hormone biosynthesis; dafachronic acid biosynthesis.
EC: 1.14.19.21
Catalytic Activity: cholesterol + H(+) + NADH + O2 = 7-dehydrocholesterol + 2 H2O + NAD(+)
Sequence Length: 460
Sequence Mass (Da): 52673
|
A0A060C0F2 | KSVPKPLLRRVLDKLSRNDAIFAPRIVSDGRSLLLDSRTAGDEPFMLANNLRGVVVLVDRDRVKSGLFAIRKFGADVLLLDDGFQYVRLDHRLEVTLVDSQAPFGNGHMLPRGMLREPPANLRRATHILLTKCVPGADYSALVARI | Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
EC: 2.7.1.130
Sequence Length: 146
Sequence Mass (Da): 16225
|
A0A317TMU0 | MYIIGSINTRFISKSEQNKKEIFNKIDNIVKGGGNIIRMNLSHGKHRDVECCIDYIRSNHKDVKVLLDLQGNKIRVANNIYGTFKVNTGDLVYFCSEDTYDVYLKHVDRNKLIPLNIKNKFIYNNNFKKIYMKDATMEFIVISNNNGLIKTKVKLGGVVRREKGCNLPNLDRKNWGISEKDLEDIKFAIEKNVDIIDYSYCSYMEECREFKNIVFKNLKSNQVIPKLWGKIETNEGINNIKEVAKELDGIVIARGDLTAEVGILNVPIVQEKILYALKNENKAIIVATNLLSSIRNK | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
EC: 2.7.1.40
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Length: 297
Sequence Mass (Da): 34116
|
D9Q0W6 | MGTCEVKARKGLIRVSSEVVGGVIARVSITGDFMVIPEDKVFELEESLVNTRFDRGEVSGVVRRVLQGSSLVGCSEEDFVDAIMCSGEGDAA | Pathway: Protein modification; protein lipoylation via exogenous pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2.
EC: 6.3.1.20
Catalytic Activity: (R)-lipoate + ATP + L-lysyl-[lipoyl-carrier protein] = (R)-N(6)-lipoyl-L-lysyl-[lipoyl-carrier protein] + AMP + diphosphate + H(+)
Sequence Length: 92
Sequence Mass (Da): 9797
|
A0A0D8JW76 | MARTAGRGERKEPSRAVAVSKALSYVLRHAAEREGVKIDSQGYANVGELLLWRKLKSLKVTFPDIIEAVSSSDKQRFGLLYVPSTSSSHSHDSLTQDAALQSAEENASKDPGANEDATAQALAASADDTDPSHYLIRARQGHSIKSIEASSLLKMLSLEDDNLPATVVHGTYHTAWPKILETGGLKCMGRNQMHFATGPALSEVLPNGDGGDVIIPSKLKGRSAGGGGGGDGSVISGMRSDSQILIYIDLKKALAAGCPFWISENGVILSEGLETGDSHGKVVGTEFFDVAVELRRGLGVLWEKGSLVQRTPDWMLQAKGPPGKGDKRHRGPKAAQKRALPRVHVGNDADGADVADQP | Function: Catalyzes the last step of tRNA splicing, the transfer of the splice junction 2'-phosphate from ligated tRNA to NAD to produce ADP-ribose 1''-2'' cyclic phosphate.
EC: 2.7.1.160
Catalytic Activity: 2'-phospho-[ligated tRNA] + NAD(+) = ADP-alpha-D-ribose 1'',2''-cyclic phosphate + mature tRNA + nicotinamide
Sequence Length: 358
Sequence Mass (Da): 38001
|
A0A7S3H1A7 | QKVLNFGSCTNPQFRGNGLGKIGTTGFFIGLVGGVHFGVGVTLYLVKSAIAADQKSHVLSALVMWCTYMSLLCGFHFMEFFTTAVHQPKVLSYESYIVNHSKSYTVAALASWTEFWLEYYWFGGSKLRTYVSILGVLMVLMGQIVRSVGMWHCGEHFSHIIMDEKKQEHQLVTTGIYRYFRHPSYFGWFYWSVGTQLVLCNPICTVAYAAAAWYFFHDRIPYEERLLVKFYGEKYVKYAESTVIGIPGIKGYAS | Catalytic Activity: [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine + S-adenosyl-L-methionine = [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine methyl ester + S-adenosyl-L-homocysteine
EC: 2.1.1.100
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 254
Sequence Mass (Da): 28923
Location Topology: Multi-pass membrane protein
|
A0A8S2KY79 | MTIPDDDSTKRKRWTHLRRVLERTGPFKDPNFEPSTELLSGIESVRILIIGAGGLGCELLKDMALMGFCRIDIIDMDTIDLANLNRQFLFTKADIGKSKAEIAAKFIMNRIPNCNVTPHMNKIQDFDASFYSQFRIIVCGLDSIVARRWINSMLVSMLQYDENNQVVPTSIIPLIDGGTEGFKGNARVIMHGYTSCIECTLDLFPPQVNFPQCTIANNPRLPEHCVEWVTSILWPKEKPFGPGVNIDGDSVEHIQWIVEHATKRANEHNITGINFRFTQGVVKRIIPAVASTNAVIASICATEVFKLATSYVHVNGMTTVIDTFLYLQRDIEQSFQRVQTIFSSSHYDRRELDRIFNHISCTLDDLEKVNQLINSSSSVENESVNITSNQNASLLLNLSENDLGDEVSNSRISIKNSTKNNFTVGYSKENEERLLVTNSNATVDLQPSFDEREDFIRRMKLQHDYYKNKIQSINNETQMEIIQLDQTPDDHKNEDHIIRKQDEQLEQIHHSIVSLKNLTQNINFEINDHIRVLDNLETGMIDSQGHVERLTNQTKTFIRSSADDVGGHTCLFALAVGLFFILSIGFTFVFGGSGVIANISVQLNKSEKHDAKFCLSRVLLNDINLVKSSMTDKSNKSTLEQITDKMEELDVEKEPINEELDEETLAMRAMGLPTSFTSSLIERGTPRQRTHSRSLSNEPMTGKKTNY | Pathway: Protein modification; protein neddylation.
Function: Catalytic subunit of the dimeric E1 enzyme, which activates NEDD8.
EC: 6.2.1.64
Catalytic Activity: ATP + [NEDD8 protein] + [E1 NEDD8-activating enzyme]-L-cysteine = AMP + diphosphate + [E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine.
Sequence Length: 707
Sequence Mass (Da): 80034
|
Q32YU0 | MTNIRKMHPLAKIINNSLIDLPAPSNISAWWNFGSLLAVCLALQILTGLFLAMHYTSDTTTAFSSVTHICRDVNYGWIIRYMHANGASMFFICLYMHVGRGLYYGSYTLMETWNIGIILLFTVMATAFMGYVLPWGQM | 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: 138
Sequence Mass (Da): 15629
Location Topology: Multi-pass membrane protein
|
A0A0T6B0Z7 | MAQAPVQLEQQKLQLLQELEIEMMADMYNRLTSTCHKKCIPPSYGDSEIAKAVCKQYASNIEISAHLSITLGSYILHGYPIYLLNYASNIIFHFILASKYCFTRYALCLLDRRRPEFQTD | Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 120
Domain: The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space.
Sequence Mass (Da): 13857
Location Topology: Peripheral membrane protein
|
A0A7X9HP30 | MTEIRKDRHLQLRLRAPLACAEEVCERLLGVGASGVEWVDETCLDRPADLLSGEVELRFSFGPGAGGQADLQDCERLVALDERVRLVRQVELDPADWATAWRAHHRAVRAGRFFVHPEWVSAAGEACPVLIDPGMAFGTGLHPTTRMCLLGLDRALPARRVLDLGCGSGVLALAAARAGVPEVWAVDNDPEACRVTAENAERNGLERVLTIRQGDIETAEGTFDLVLANILSGPLVAMAPGVARRIVPDGRVLLSGLLQEEAPEVTSAYRAVGFQLEHEQHEDEWVALAMLRGKT | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 295
Sequence Mass (Da): 32029
|
E2CDM9 | MLSGYGRYMAKGYVRHKETHEHLAVYGQTPEVMVISCCDSRVTPEGIFNVGPGELFVFRNVANLVPPCETDSGHHGTSAAIEYAVTALKVKHIVVMGHAKCGGIQAFRENAGTSNLEGAFIGRWIKLLEPAAISLACMPVDKIDDPQLAMEYAGVRQSLVNLGTFPFVEEAIQNGSLSLHGAWFDIGSGELRVMDPDTERFAPAEPASIQAAE | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 213
Sequence Mass (Da): 23004
|
A0A964JR13 | MSAHEIDGHKRLPVDVRPLRYALTLELDPTSDRFRGEVNITVRFEASVDRIRLHADQLRIEEATFERDGHVSAVPFHEGENGGLEYLIPTAEGPTAEGPGEASLRLVYSGPLTEVPEGVYRVREGDAWYIFTQFEPISARRCFPCFDEPGFKAEYEIKVRTPKGLIALSNSPIARVEHLLEHDVHAFYATPPLASYLVAFAVGPFDVVDAGNTEDGVPLRIITTIGRSHLARFAVEETPAILAELTRWFGMPYPYAKLDLVGVPNFAAGAMENVGLVTFRERLLLLDVDHAPAHDRLWAKVVIAHELAHMWFGNLVTMPWWDDLWLNEAFATWMETACVHAIDPSLDIAYEAVLDSLRVMDHDALKEARAIRQPIRDGGDVLNAFDGITYSKGAAVVRMTEAWLGSDVFRLGVQRYLTAFEHGNAVTQDLIDALETASGKDVDVTLRTFLDQPGVPIISVTPIDGGGHARVQQWRYLPNTRPAEPDGRWRIPLTIRYGDSSGETGRVSHLLTSADEVISLPGGAAATWLHPNASEAAYCHWQLPKASLAMLAGPARIHLDLSEKIALVEHVWALLESGEIPAVDAFEATLSLAAEPHRMVLGAVAGVLRRMARLVVGPLETPALALRLNTAFAPHLSRLGHFPKTGESPADRLLRPVLIGLLADVGACPSVNAELSTWARVALRSIKDADVEVLQYALPIAAWDGDEALLDELVKALDDVPTPAHATAFLTALGSFPGPILGVRALDVFLTDRVRAQDVFTLLRPSQRRPATFQTMWTWLDRHFEVIAEKIGDEMTAHLPGLASGFSDVAGRLEAERLFADASRHKPGLDRNLRQALEDIDRRARLRACIEGPLRAHLGCDPRL | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.11.-
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.
Sequence Length: 864
Sequence Mass (Da): 95120
|
A0A0L0V0S7 | MMGISIKTNAIFLLTATLSTLHNAQLGLCHGYIKAWSADDGHTWTLGQKQDLATSSIRGFSENTGWIGSKFLTKPAIVCSSGLTPSLKVVAPSGDLFSQADQSAGKTLSVASGATVRLLINDEPHKIYPHENGHIQIYLGYCGPSETACEKFDAASISYFKILSLKHGLGSKEEFPYNKHKDGNEVKVPIPKNLPMGSYIMRIELIVFGQSSEAEGKQDQYYITCGQMALPKPEINPPISIESLESVRFPGAYKNGNIDPEDPLPGPNVVDFSGEAQGSAKASSTVRQSTPSPTPSPNDSGEDEGSRLSGSVPECARACLAKKISENAEGKLGVICATPSPQPGQTQALCQCKDEKFTEAFANCARDHCQPGCEVEDAINSFSNLCGLKTKPSRCQNNNKRERPVLLI | Function: Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds. Involved in the degradation of complex natural cellulosic substrates.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
EC: 3.2.1.4
Subcellular Location: Secreted
Sequence Length: 408
Domain: Has a modular structure: an endo-beta-1,4-glucanase catalytic module at the N-terminus, a linker rich in serines and threonines, and a C-terminal carbohydrate-binding module (CBM). The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion.
Sequence Mass (Da): 43812
|
A0A0L0VTJ2 | MAPRPSLHQFLNQALQLVPTNEANPRTFELLTLATKPFRTFTLFPHALNPTVSIMRTDYLITLAEKFEDYRPKDDTISTPTPEVTVPVFALEASLYTISTTAVQLLYISKIDTTGLAPLPAPSGQLTIAFLSYFLQHMPKSIQSLRIHIFARASREGQYLFPASAENAPNGTGDGAKFASKIITSAGGDWGATFPYKTPTGKRILDDQQLVKWWHKVLSQLALGYHQASKTIKNPLECFYILPGLDHEESLEVLPLTPELKALWNYGHPYHKIRSPCTSAHQDQSQQPSKIGSSDRSQSCLLSELIPAFDDDPKARFLHSIGNCSTNASGEPGDWDDAIGQRSSSSLESDRNRERIKINNVSSDEFWDRMGGRQECCDGRWWACSSRVVE | Catalytic Activity: acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-lysyl-[histone]
EC: 2.3.1.48
Subcellular Location: Nucleus
Sequence Length: 390
Sequence Mass (Da): 43515
|
A0A6B2M109 | MQKVSDSRPLVELETNKGRIVIELFDQEAPVSVANFLEYVNNGFYEGTIFHRVEPGMVIQGGGFTEDMERKETLPTIINEAGNGLRNNRGTIGAARTRDMNSANSQFYVNLVNNSGFNGDGVTSGYAVFGRVYEGMSVVDAIALEDTGTVSGLKNVPLEPVIILSARQVR | 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: 170
Sequence Mass (Da): 18520
|
A0A094EVX1 | MINSPPALVEMLDRNKKHAETYKAPPHLMEVLPKIRDAGNGVLILTCSDPRVNVFEIFGLDSALGAAVIRNAGGRAADALRSVAVLQHIARPGAIVVMHHTDCGGTHIEPNDVKKDLVELSPSDKTTIENTQFGKKMTSIKESVREDIALLKTSPLVDHSTQFVGLTYDTFTGLVSEVTLD | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 181
Sequence Mass (Da): 19594
|
A0A059EQM1 | MWDFVGGRFSLWSAAGITIALYLGFKNFLRLLTGASVMDKHFKNNPLESACAMHSLVEIYYTLLNYDTKCIVPYDYYLRDFYLHLQQLDMESNGKSAKKNGKLTTHSGMIIWGGVGTNSQHSFFQLLHQGTHKILTEFIYTLVPEREYSTDGSHHTKLLSNCVAQSEALMKGDENSDINKLFQGNKPSISIRLSKITPETIGALIAHYEHKVMASGVFFEINSFDQFGVQLGKVIAQRINDIIDGKIDMPDKEKCGCSASSRHAVEEIIKSKMQN | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4.
Function: In the cytoplasm, catalyzes the conversion of glucose-6-phosphate to fructose-6-phosphate, the second step in glycolysis, and the reverse reaction during gluconeogenesis.
EC: 5.3.1.9
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
Sequence Length: 275
Sequence Mass (Da): 30958
|
A0A8S3F398 | ALYNNSYRLFKIDNDQQLTSDRLLWNALQAYLNQTLPSLNDLTFSFLFDLLHSITNNHTHTKTFVKEKTTPGIYTLFTASQYSANTELPVRSIEPAYKQCFDEVVRTYMEEVNKISRNMGRFLEYKKTLYGYYKYEPRHGISYILDLYLIYRKYMGRKMSVSYFEYNCFLSDSS | EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 174
Sequence Mass (Da): 20725
Location Topology: Single-pass type II membrane protein
|
A0A820A6W5 | MLSYFIFFRIHQKEERRDERTVKLNASTLFNYLVRLIILISLLLITFIIPYSSTIINLFFGTNLLKNYNLILYVHLYLIKMLLNGINGITETFIQSVMSIQQTTQKILFVLTSHDIFPNGHPTGWCLPEAAHPYCVLENHFTIEWASPKGGHAPLDPSSVENFKDDVECKQFLSDNKAKQGYENTKKLTDINVNDYVALVYVGGHGPCFDLSEDKTSIKLAEEFWKQGKLVSAVCHGPAALG | Function: May be involved in N-linked oligosaccharide assembly.
Subcellular Location: Membrane
Sequence Length: 242
Sequence Mass (Da): 27491
Location Topology: Multi-pass membrane protein
|
A0A1S3VGL4 | MASATSSTLIFMALNGCSIWDCCKALQPANSTLSVNSKHDLGKSSKWRRCCSSVVNGAKSSFEYSDRVQVQITELDDGFHKDVNLLLKSLTANDFFSRDGTKLCVAYKGLAGAYTEEAALKAYPKCETVPCDDFETSLQAVESGLADKAVLPIESSEAGSIHHNYDLLLHHKLHIVGEVQLLINHCLLGLTGATKENLKFVLSHPQALVQCEMMLTDLAVTNIGVDDTAAAAKAVALDGRRDIGAIASSRAAKLYGLHILAEGIQDDDNISRCLILARDPILPEPNGSYKTSIVFGLQEGPGVILKALEVFGMRNINLSKIERRPVKHYPIRLRDDSKYEIVKYFDNLFFIDFEASMTNPNAQHALESLQEYTTFIRVLGCYPVDKTDISC | Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; L-phenylalanine from L-arogenate: step 1/1.
EC: 4.2.1.91
Subcellular Location: Plastid
Sequence Length: 391
Sequence Mass (Da): 42911
|
A0A2N7XB47 | GKFRPGHFRGVATVVNRLFHLVDPTRAYFGQKDIQQCLVLKRMVKDFGTPVELVICPTIREMDGLAMSSRNRFLTSAEREKSLVIY | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
EC: 6.3.2.1
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Length: 86
Sequence Mass (Da): 9857
|
A0A2N9MF66 | MMLLACAVLAARFAAPQTRTNTDPPDTARIQSALNLCGPGRAVVLKSDGRRAAFESAPLILPRGVTLFVGHGVTLYASRNPRDYDLPPDGKAAAHKAFLFAYQAAFSGVSGGGTIDGQGTAPELVSSYESQGFQIAGVTLRNAARIPAAIYKTPGLKVSAIRIDSPSASTGLLLSNAQDASVTGAWIRVPGEAIVLQASILGATSQIAIRDVHVIGGRGIRIGDDTYGAVRGVTFDGIAMEGARTGFSFNLKGAEGGEARDIRASKVCLHGVAEPLRVDPVGATLPAGRDLDLGGLSTPCGIPTFTPAPFTADVTLARGIGSARSTVVAPGSSIQKAVDALPPNGGEIRVKPGTYREVVTIRKPHVHLRGEDSDPSKTVIVYGNGPAQGGTFATATVFVEASDVTIDGLSIVNDLGVGRGQGVALAVTADRAIFRNLRILGAQDTLFAASRYCYGDYGPCVAARQYFADSYIEGNTDFIFGDSAAVFERCELHGISSGSVMYTAQSRHTAEQRSSGYVFDHCRLTGDPRQGAISLGRPWRPYATVVFLHAQIDAPVIPAGWTEWVRFGQPSLPTAYYAEYESSGLGANPQAREPYSHQLTAVEAEQWSPRRVLAGADNWNPR | 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: 622
Sequence Mass (Da): 65487
|
A0A5B8LWK3 | MSSIPAPGTVKTEILTTSPVAVVTIDFPPLNVGSHAMRSALLAALDALAERTDLSGIVLVGGGANFVAGSDIREFDAPPLAPHLPEIIERLESLPMPVVAAIKGAALGGGCELALGCDWRVASPDAVMGLPEVTLGLIPGAGGTVRLPRLVGAELALDMVATGQRLTAGRALETGLVDQVADGDVIAACLAWLETHKQKRRCLDLPVPAYGQQNLAAAGRALVAKARGADAVPVAIEAVQRGLTLPPADALALERAYSLRLRVSPQSRALRYLFQSERRAGRLPARVTGRPIHRVGVIGAGRMGSDIAFALARGGLSVLVVEANADVLAQSMGRITQSAERLVKRGELPAVVDLLDRIHSVTLEQLGDCELVVEAIPEDMAAKSALFAQLQTIVGPEAILATNTSYLDIDAMAEVVSRKDRVVGLHFFNPASILKLVEVVQAEQTGQDVLASALQLARRIGKLPILTRVGEGFVGNRIFAAYRRQCEYLLEEGCLPEEIDRAMREFGMAMGPFEVFDLAGLDIAWAMRKRLAATRKAEERYVTIPDTLCELGRFGRKTDRGWYDYEAGKPVPSAEVTQLIEDASRARDIARKVFTDGKIVSLLLTAMVNEAGWVVAEGVSAQPEDIDVAFCNGFGFPRHLAGPLYWAALQSPEILHAELTQVRAMSGRPTAPGLDAMLRRIADQDRRSA | Pathway: Lipid metabolism; fatty acid beta-oxidation.
EC: 1.1.1.35
Catalytic Activity: a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH
Sequence Length: 689
Sequence Mass (Da): 73632
|
A0A5C5FVH4 | MDFDTYAPASPRQSGFLRSIKDAPRPPTPTGMPTAFESSYDLFLNPAVPIAFGIVYFAVAKTLSHYQNGKNRIPGKRWQAAVFSHNVFLAVYSAWTFLGTAPQVLGHFWSAFAEYGVAGLTHAFCDSSFAIWSSESFSKFAYLFYLSKFYEIVDTAILLLKGKKVGMLQSYHHTGAIWTMYSAYVTQAMPIWLFVVFNSFIHSIMYTYYAFSTVSLPFPRFLKKSLTRLQITQFLVGGSLAASYLFIKLPELPSWPTSTDEARAQLTQAASSFEAGVNALRTEGARCLPNPGQRAATIINCVYLVPLTYLFVSFFIKTYQKSQKAAKAKAAAAKKQA | Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
EC: 2.3.1.199
Subcellular Location: Membrane
Sequence Length: 337
Sequence Mass (Da): 37527
Location Topology: Multi-pass membrane protein
|
A0A7X9HNF0 | MHPIITTVFGQPIYSYGAALGIAFITGWSLATRFTNREGIPYKFATTAYTLAIIFALIGARVFELLANPEMWRFKGFLVALFASKCEGLVAYGGFVGAWIACFVYARMKSQDFWSLADCTTPSMMLGLGITRIGCFFAGCCHGQPTEVPWGIVFPPGSPAARAFPDLAHRVGETVSSLPVHPTQLYESLLGFALFPIAYLAYKKRRFTGQAFLITIPLYAIGRFLLEIIRGDTDRGEVASLSTSQFIGMVVVLCAIGIYLYRRTRAPAPPPPLSDEEIERRQVEAGAKKSKKKSR | Pathway: Protein modification; lipoprotein biosynthesis (diacylglyceryl transfer).
Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+) + S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[prolipoprotein] + sn-glycerol 1-phosphate
EC: 2.5.1.145
Subcellular Location: Cell membrane
Sequence Length: 295
Sequence Mass (Da): 32461
Location Topology: Multi-pass membrane protein
|
A0A838SW82 | LMADTCLDEYTDHGHCGPLRADGSVDNDAAVAAYARAAVAQAEAGADLVAPSGMMDGQVAAIRAALDSAGHAERVGIMAYCTKYASAFYGPFRDAAECAPRFGDRAGYQLDPGNADEGVREALADAAEGADLLLVKPAMVYLDMVWRVKEATGLPLAAYQVSGEYAMLHAAAQQGWLDGDRAMAEALLGIRRAGADLVITYAAAWLARRLQQA | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
EC: 4.2.1.24
Catalytic Activity: 2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen
Sequence Length: 213
Sequence Mass (Da): 22354
|
A0A9D9H0Y4 | MLTGDFRYPYFLGIGGIGMSALAWYYLQNGAKPSGYDRVPSSLTRQLERAGIGIHYDEAPEKIPVETDAVIYTPAIPGDHAEWAEIRHRGLPVFKRAEVLGWICRRYRTLAVAGTHGKTTTSSMLAYLLRQSIGCNAILGGISLDLGGNYHYDASSPFMVTEADEYDRSFWQLHPWFSVVTAWDADHLDIYGTLENMRDAYRQFMRQSEHFIAYEGLRGELDAPEADGFYGIAESAGKRVPAVDAGAGTGCCPFSAQALHLEVGNGAYRFDYAGPRATIQGLELHCPGRHNVLNAVAAITLALEAGVAPESIKRLLPAFKGVARRLELKAEAGNVRYYDDYAHHPAEIEASIVALREFYPKARLCVVFQPHLYTRTRDLAPGFARSLSMADEVFLADIYPAREMPLPGVDTRLIGREMLDKDVYYGSREEALEWLSRKIAQAKEEGTRPVAEKEGLLLVTMGAGDIDRIVDKVVDSMREGGAL | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
EC: 6.3.2.8
Subcellular Location: Cytoplasm
Sequence Length: 483
Sequence Mass (Da): 53448
|
A0A3S5ERI4 | MEKSKIILNSIFYVILTAIFIYIFVKEKALTDTIKIYRDKFADKVIMVLNIKGKVLSKGIRTTINLVETIGTALILVLIIQKFYLGNFLVPTGSMIPTIMPKDRLFGNMLIYKFRKPQREEIIVFKEPIQNKVLYTKRVMGLPGEVVNIKIIIFM | 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: 155
Sequence Mass (Da): 17903
Location Topology: Single-pass type II membrane protein
|
R7BU27 | MRALIQRTFKSALSVDGKLISEIPSGLTIFLGIEKGDTEEQADYFARKVAKLRVFRDENDKMNLDIKQAGGEILLVSQFSLAGTLGKGTGNRPDFGHAELPDRARYLYERVTEKIREEGIVVKNGVFGAHMFIEQQQDGPLSFVFEC | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality.
Catalytic Activity: a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)
EC: 3.1.1.96
Subcellular Location: Cytoplasm
Sequence Length: 147
Domain: A Gly-cisPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of L-amino acids.
Sequence Mass (Da): 16441
|
A0A5C8PQ80 | MDFIGFFTNNIILTLLVITVLVFVHEWGHYWIGVRNGVHAEVFSIGFGPELWGWTSRKTGTRWRISALPLGGYVKFLGDSNPASVGGDDGLTGEQRKRAFHTQSLGVRAAVVVAGPAANLIFAIVLMAGLLMTYGQPYTPPTVVVTEPQGAAAKAGLRSGDTVVSIGGRSVESFEDILSIVQLNPGITIPVTLTRDGQTQTTMVTPAPIDFKDRFGNIHRLGDLGVSNVNALPVIGRVVPGSAAERAGLKAGDRILEIESAPIDNFGQIQRFIRERPNQPTAIKVERGGAVIDVTATPAPEEVRGADGKPRFEGRLGFASGSVSVVRKMGPLDATVEATAQVWHMSGTIYTVIRQIVLGLRPANEIGGPIRIAKTAGEVSQIGWSAVLYFVIGLSVTLGIFNLLPIPMLDGGHLLFYAIEWIRGRPLSARAQDIGFRIGLAAMGGLMVFATFNDISLLIGRILPL | EC: 3.4.24.-
Subcellular Location: Membrane
Sequence Length: 465
Sequence Mass (Da): 49704
Location Topology: Multi-pass membrane protein
|
H0WBJ7 | ETLETLIRQAENYTSRLFCNTYRNMALEAAASVQEFFTDVGLYLFGADVSPEEFVNRFFDSLFPLVYNHLINPGVTDSSLEYAECIRMARRDISPFGSIPKRVMGQMGRSLLPSRTFLQALNLAIEVINTTDHLHFSKECSRALLKMQYCPHCQGLTLSKPCMGYCLNVVRGCLAHMAELNPHWHTYIRSLEELSNAMHGTYDVEHVLLNFHLLVNDALLQAHVNGHKLLEQVNKICGHPVRTPTQSPPCSFDPNKEKQGILKTSVRNGEDTLANRRKDFINSLRLYRSFYGGLADQLCVNELAAASRLPCWNGEDLVQRYSVSPNL | Function: Cell surface proteoglycan.
Subcellular Location: Cell membrane
Sequence Length: 327
Sequence Mass (Da): 37044
Location Topology: Lipid-anchor
|
A0A834G4K6 | MACQRGRDFQHQSVIITANVIGVSPQMLGYISDCICSLCLFLRESFTCMFTLHNDITVIVVRVSDQQFVGTWKPDKYSFPNIVCSEVVHAVGRMDELKLEKVSSIACWWAGYFAVDAMDREKETGKADLKGNESTSVEIKVLFFARARDLTGLTELPLEVSSGSTACDCLNKLIAKFPGLEDIRACMVLALNEEYTPESTIVKDRDELAIIPPISGG | PTM: C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-adenylated (-COAMP) via the hesA/moeB/thiF part of MOCS3, then thiocarboxylated (-COSH) via the rhodanese domain of MOCS3.
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Acts as a sulfur carrier required for molybdopterin biosynthesis. Component of the molybdopterin synthase complex that catalyzes the conversion of precursor Z into molybdopterin by mediating the incorporation of 2 sulfur atoms into precursor Z to generate a dithiolene group. In the complex, serves as sulfur donor by being thiocarboxylated (-COSH) at its C-terminus by MOCS3. After interaction with MOCS2B, the sulfur is then transferred to precursor Z to form molybdopterin.
Subcellular Location: Cytoplasm
Sequence Length: 217
Sequence Mass (Da): 24027
|
F3L0U4 | MHVGPASDTDTICAIATPPGRGGVGGIRISGPRALAIAKQLSSITNIAPRTAHFSSFKTPDGELVDTGLLLFFATPRSFTGEDVVELQTHGSPIVLNRLLAEICGLGGRLAEPGEFSKRAFLNNKLDLVQAEAISDLINANTETAAKNAQNSLQGAFSSHVNGLLAKIIGLRVLVEAAIDFPEEEVDFISELDVQTQLNTIITETELTLNQANQGQIIQEGLTVALVGAPNAGKSSLLNQLCGLDKAIVTDIPGTTRDTLETVVNIKGVPVTFIDTAGLRLTDDVIEQAGIQRAVNTLERAQLVLFLMDASATSEQSVSLFTLLPSNLAEACLAHPFIGVSNKIDLLDGPIPQIQEATTNVSIAAKMGLNIEGLKQAIIDAVGLHPESEHLFSARQRHISALQSTLSALKNGFVQLQEHAASELLAEDLRLAQQAINSITGEFTNDDLLGEIFSSFCIGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
EC: 3.6.-.-
Subcellular Location: Cytoplasm
Sequence Length: 460
Sequence Mass (Da): 48761
|
A0A7S0W2Y2 | RAEAKRLRNRTTMMYLGAVTLFTISFTYLSVPLYRIFCQKTGFAGTVKAREDVKYEEKARPVSGKRMLTIKFTSDVAPTLPWTFLPQQQSVNVVPGEACLAFYTAHNKTPQPVIGVSTYN | Function: Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 120
Sequence Mass (Da): 13528
Location Topology: Single-pass membrane protein
|
A0A2H6JXZ2 | MAEFVVTPWEVTGEIDYEKLIDKFGTSPIDEALLKRIEKHTGKLHALLRRKIFYSHRSLNWIVNEYEKGNSFVLYTGRGPSGHTHLGHLMPWIFTRWLQEKFDVKLIFQLTDDEKFLFNPDLSLEDTRKFSYENALDIIALGFDPEKTEIFLNTEYIKIQYKIALNVAKKITLSTAKAVFGFKNETNIGMIFFTSMQSAPCFLESERENRAVPVLIPCAIDQDPHFRITRDVAPSLGYPKPALIHCKFFPSLAGGDKMSASKPETSIYTVDNPREARKKIMQAFTGGQESVELQRKVGGNPDVCSIYQYLYYFFEENDEKIKERYSACTSGELLCGECKKYLADRVEKFLVEHQKEREKAKELLEEFIVRD | Function: Catalyzes the attachment of tryptophan to tRNA(Trp).
Catalytic Activity: ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-tryptophanyl-tRNA(Trp)
EC: 6.1.1.2
Subcellular Location: Cytoplasm
Sequence Length: 371
Sequence Mass (Da): 42896
|
A0A1G0HS76 | MQLFTLGINHRSAHLSEREKFAHTFQQTPHLMDTLFKTQAVEEAVVLSTCNRTELYTVTRCHHAVKEWLRRQQSFDEKLLTTAIYEHHDLNMIKHLMSVASGLDSMVLGEPQILGQMKQAYHHALRQGTVGKQFHKLFPAVFEAAKLVRSQTDIGCHPVTLTYAVIQLAKKVCPPLEQSNVLLVGAGETIELVANYLHRHNVQRLLIANRTLERAHGLARHYGAVPIRFEEMLTTLAEVDLVISATTSDTAILYKESVAGVMAKRAQRPLFIADLAVPRDIDPAVGELSGVHLYNIDHLQSMVSENQQSRQGAIFQAQAIIEVQAAHHLRQLRVLDASDMIRNYRKKMEQWRDQELDNALKTFAHHQDPVMAMRELARRLTNKFMHQPTSKLRDAAYTQHALLLNLLRELYEL | 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: 413
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): 47081
|
A0A517PD33 | MIRIVDYGSGNLRSVQKAVQSLGFEATISARPEEFSKGDKLILPGQGAFGDCARGLAESGLREVVLDQIAADRPLLGVCVGLQLLFDVGREDGDHEGLGVLRGEVVKFDGPAFEGPDRAKIPLMGWCPLLSPASRSLEETPVLRGLGPNPHVYFVHSYHAAGVDPAVVAAEAEHGGRFVAAVHRGALTATQFHPEKSQAVGLQILRNFATL | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
Function: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF.
Catalytic Activity: 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H(+) + L-glutamate
EC: 4.3.2.10
Subcellular Location: Cytoplasm
Sequence Length: 211
Sequence Mass (Da): 22429
|
A0A136KFT3 | MLAKPHRLRTTADFDRVYKQGKCYKTRFFRAYIRKHVKLSPKEGITALPRFGIVASKKTGTAVQRNTAKRILRTIVKEQLPSLHSEFEMVIIAYNTLLDADSNTLKLELEEILTAADLKKRQKS | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
EC: 3.1.26.5
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Length: 124
Sequence Mass (Da): 14276
|
A0KEF2 | MANILVFDSGMGGLTIYREIRRALPAHNYFYCFDNANFPYGELSEAALTEVCTRLVSHMVVEHDIDLVVIACNTASTIALPSLRAAMTVPVVGVVPAIKPAAALTRNGCIGLLATPGTVSREYTHELIAQFAPGKRVLLKGATELVVEAEHKLAGLPVNMALLREVLADWLEGEEHPDTLVLGCTHFPLLDEEIRQLMPACQLVDSGSAVAKRVAHLLAGLVTTPTRLEDVGGKAYCTRLDAQTQKLTAPLQAWGLSSLEEVRF | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Provides the (R)-glutamate required for cell wall biosynthesis.
EC: 5.1.1.3
Catalytic Activity: L-glutamate = D-glutamate
Sequence Length: 264
Sequence Mass (Da): 28511
|
A0A1G2LE23 | MLRKLFAGLQNSLAGLAHAYRRDASFRMEAWTAPAFLIFGYFASPLSPSEFLFLLLSFTLIMMAELINTAFERALERLHPERHELIGATKDIASAAVFIAVCFALVVISVISWNRF | Function: Catalyzes the ATP-dependent phosphorylation of sn-l,2-diacylglycerol (DAG) to phosphatidic acid. Involved in the recycling of diacylglycerol produced as a by-product during membrane-derived oligosaccharide (MDO) biosynthesis.
Catalytic Activity: a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-phosphate + ADP + H(+)
EC: 2.7.1.107
Subcellular Location: Cell inner membrane
Sequence Length: 116
Sequence Mass (Da): 13041
Location Topology: Multi-pass membrane protein
|
A0A9D9H1S0 | MKACGLNQHVGSDPVTFRQWKEAFRQRLGVLYEQAEADSLFYWSVEEITGISKARLLAEMEQPVPLKSVPLLKSVLQRLEKAEPVQYVFGKAFFAGMELRVGPGVLIPRPETEELFQWACESLPLSGHSASARILDLCTGSGALALALAKTFPDAQVYACDLSSIALSTAGRNAHDLGLSVRLFQHDVLEGNLPESVVAGGPFQLMVSNPPYVLPSEKDLMRSNVLDYEPDMALFVDEEDPLAFYRALARIARAHLAPGGFFLAEINESFPRENKDLLVAAGFEEVEVRHDFRGKHRMVRARMPLFI | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
EC: 2.1.1.297
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-homocysteine
Sequence Length: 307
Sequence Mass (Da): 34088
|
A7U509 | ASLQTGSEELRSLYNTVATLYCVHQKIDXRDTKEAXEKIEEEQNXSKKKAQQAAADTGNSSQVSQNYPIVQNLQGQMVHQPISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPVQAGPVAPGQIREPRGSDIAGTTSTLQEQIAWMTHNPPVPVGEIYKRWIILGLNKIVRMYSPTSILDIXQGPKEXFRDYVDRFYKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPXATLEEMMTACQGVGGPXHKARXLAEAMSQVTNSATAAIMMQKGNFRTQRKIVKCFNCGKEGHIARNCRAPRKRGCWKCGKEGHQ | PTM: Specific enzymatic cleavages by the viral protease yield mature proteins.
Subcellular Location: Virion membrane
Sequence Length: 359
Sequence Mass (Da): 39935
Location Topology: Lipid-anchor
|
A0A1G0HIQ6 | MTLQELLKQIQNKLSITSQTPKLDAEIIINAALQASPTIFYTDSQRNITESELKRVHALLQRRQQGEPIAYLLSEKEFWSLKLEVTPDTLIPRPETEHLIEWALTYLPNNKPLKIADLGTGSGAIAIALAHEQPNWQLHATDESFAALKVAIRNAQRFNLQNISFYQGDWFSALPQIKFDAIFSNPPYIAEQDPYLNAPEMRFEPKRALIAGTEGLDALQIIINNATHYLQEQGWLIVEHGYDQANRIDALFDQAGFSQIKTLHDLAEIPRFTVGQSKSATPVKR | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
EC: 2.1.1.297
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-homocysteine
Sequence Length: 285
Sequence Mass (Da): 32242
|
A0A1G0HXR1 | MKFSEKWLRKFVNPPLEVNQLAERITLAGLEVDSISPVAGEFTGVVVGHVLSCERHPDADKLNFCKVDIGVGDCLQIICGAPNVKKDLKVAVATIGAVLPGNFKIKKAKLRGIESCGMICSESELGLSEGRMGILELPADAPVGQDFREYLELNDHCIDIELTPNRGDAASVLGIARDVSALFDVPLNQPVIKEIEVSHHHTIDIEGVEAAACPRYFGCLIEPIDNTRSSPIWLSEVLRRSGLRSINPVVDVSNYVMLELGQPCHVFDAAKLSGTMGVRYARSEESIELLNGDSLKLKPENLLITSNNQPVALAGVMGGAHAEVSAATTTVFIESAYFNPAVIRRSASLHHLYSDASYRYERGTDWQLPERVLHRVVELLLQIVGGEAGPVSRFESTEDLPRIHKVSLTHAKLTDYLGLEIDEQVAASILKRLGFAVTLKEGVFETVVPSYRSDVTLDVDLIEEIGRIYGYSNIPTADIQFDVALTLETELRPLQKLRQQLVVLGFSEVINYSFIDPLNCQKINSLPPMILANPMVTDQSVMRTSLLPGLLNNAAYNIARQQKQLSIFEIGKVYLPHASVVAEKNKLALLMTGDRIAKQWFASSRACDFFDLKGDVNLLYDAFGLKGHWKSAVVDYFHPGQSAQYFLAGNSVAVMGKLHPALQKHFDLKQDCFLLEMDVDVFCRDAREIFSAISKYPSVKRDLAFLVDEAVSIAELDTHIQHSCKGLFKEVVVFDVYRGEGVPAGQKSVAVGLILQNPTQTLDESEITAIIQRVIAGLQREFNITLRA | Cofactor: Binds 2 magnesium ions per tetramer.
Catalytic Activity: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe)
EC: 6.1.1.20
Subcellular Location: Cytoplasm
Sequence Length: 788
Sequence Mass (Da): 86862
|
A0A1M5RPY6 | MKEYALIVAGGKGTRIKSSTPKQFLELDGKPVLLHTLEAFYRYSENIHIILVLPADDFATWEMLCTRHKFHKPLILQRGGDSRFQSVKNGLDKIDGDGLVAIHDGVRPLIHEDIIGASFRLAAVHKSAVAAVRLKESIRMTDQDTTKAMDRSRFRLIQTPQTFQVDLIKKAYSLKEDDTLTDDASVAERAGHAISLFEGSYENIKITTPEDLVVAEALLRSRKGRG | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
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: 226
Sequence Mass (Da): 25257
|
H0VDL6 | MLIGQEASELCEVTACRSGRSRRSMVEMLPTAALLILAVSVIARDNTTCDGPCGLRFRQNLQGSVRIIGGQTAQPGAWPWMVSLQIFMAHNNRRYHACGGILLNSHWVLTAAHCFDSKKKVYDWRLVFGAEEIEYGNNKPVRAPLQERYVEKIVIHEKYNIVNEGNDIALLKITPPVSCGPFIGPGCLPTFRAGPPKIPQTCYVAGWGYIREKAPRPSPVLLEARVELIDLDLCNSTQWYNGRVMSTNVCAGYPEGKIDTCQGDSGGPLMCRDNANSPFVVVGITSWGVGCARAKRPGIYTATWDYLDWIASKIGPSALHAIQPATPSPPTTGPLPPARPPSSRPPTAKPPWYFQNLARPPRPPRPPRPLQPFAPQPQPPAAQAPPPPSLSSPPPLPPLSPTRPAQGLSFAQSLQQLIEALKELGNSGTKSSYSMEIPELSEPISLS | Function: Acrosin is the major protease of mammalian spermatozoa. It is a serine protease of trypsin-like cleavage specificity, it is synthesized in a zymogen form, proacrosin and stored in the acrosome.
EC: 3.4.21.10
Catalytic Activity: Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
Sequence Length: 447
Sequence Mass (Da): 48625
|
R7LT19 | MRLKIITQERVVFDEDVDEIYSKGIDGEFGILKGHIPIMTALDIGVTRAKQGDEFKTFTTMGGILQFKDEECLVLTTLAEAGEEIDEARAREALERAKRRLREANARLDAKRAEAAIARAEARLKAKLVN | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 130
Sequence Mass (Da): 14561
Location Topology: Peripheral membrane protein
|
H0VAL4 | MLVPGLGATASQTVLLLLPGILFCTETCAGSHSLRYFHTAVSRPERGDSRFISVGYVDDTQFVRFDSDAESPRMEPQAPWMDRVDQEYWDRETQGAKRDADDYRVDLRTLRSYYNQSAEGSHTLQKMYGCEVGPEGSFLRGYKQWGYDGEDYIALTEDLSSWVAADTAAQITQREWVKARKAEHHRAYLEGECMDWLLRHLEHGKETLQHAEPPKAHVTRHPVSKDQVTLRCWALGFYPKDISLTWQRDGQELTQELELVETRPEGNGTFQKWVAVMVPSGEEQNYMCHVEHEGLPEPRTLRWAPLSQTPPPNSKSPSIPILGVVAAVILLVAVLTGIAFVMWKAGRGGVRGNYTQAARGDSAQGSDSSLMVGKGETPGGLKWERWAEAEGTQQGPCLTVNPVCEQRAPLLVFIRTWVLCPVFVFTLESWCSCVTRLCFLLLCVPRSIPCLHV | Function: Involved in the presentation of foreign antigens to the immune system.
Subcellular Location: Membrane
Sequence Length: 453
Sequence Mass (Da): 50888
Location Topology: Single-pass type I membrane protein
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.