ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A7S8HAY0 | MGKTMGRGLSRLIGMRLLAVLAVFALSAEPLAAQERFATEAPYAFLMDAGSGTILYEKRANELMAPASMSKLMTLVMAFEAVDRGQLELDDRILITEEAWKRGGAKSGGSTMFAELDSHVPLRDILKGIAVVSANDACIALAQALAGSEAAFADLMTTRARELGLERSTFTNATGLPDPGQRMTVRELAMLARYIVRDFPEFYELFDIREFTWNDIPQHNRNPLLDRVPGADGVKTGYTKEAGYGLVGSVQRFGRRLILVVAGLPSADAREEAAVKLIDWGFGNYQAYVMFEPGQTVEKARVWGGDAAWVPLVTRIPVDI... | 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-alanin... |
A0A2N5KE22 | MHTVDRLYTLFQPEHYNLTLNLLRKERQFTGSVTIAGTITDSAQTIRLHGKELTILSAKVGGETAAFTTNPDLDEIIITPNGELPAGTQTVEISFSGVITDAMHGLYPCYFEHDGSKKELLATQFESHHAREVFPCIDEPEAKATFDLTLQTETGITVLGNMPVAQQNEDETGLQTVFETSPRMSTYLLAFVIGELHSVQAKTSNGTDVRIWATPAHDSESLQFALQTAVGAIDFFNDYFGVPYPLPKCDHVALPDFSSGAMENWGLITYREVALLVDETTSLSMKEYIATVISHELSHQWFGNLVTMKWWNDLWLNESF... | 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... |
A0A6A4SK40 | MSCLIVDATALMLLKVLSLKALSQKLVMTRTGEADKQLIYRLMDDPGFLMSDHISSYKMAEGRHAQVATATGREQRESCPRSGVVLDHSRRHRTAFTREQLSRLEQEYGRESYVSRARRCELAAALNLPESTIKLVRAAGRTPGTEPPGSVHRQLNVKCLTLGLPCSVRVCRCKDTPVAITSESRSTSSLYYGTVPAMYACAKFVTSPAVLRGGSRVLARPVSVSLFNRPEATVEQQALLPLSQSVVPTRSFQTSAVSRDIDTAAKFIGAGAATVGVAGSGAGIGTVFGSLIIGYARNPSLKQQLFSYAILGFALSEAMG... | Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramemb... |
A0A173V5V1 | MEWSFVFFLNSVLLGVGLAMDAFSVSMANGLHDPKMNKGTMCKIAGTFGIFQAAMPMIGWVCVHTIVELFASFERFIPWIALALLSYIGGKMLADGIRGEEAEEAAQLSAGALFMQGVATSIDALSVGFTISEYGWLMALTAAIIIAVVTFFLCMAGLCIGKRFGTQLSGKANILGGVILIGIGLEIFITGVF | Function: Probably functions as a manganese efflux pump.
Subcellular Location: Cell membrane
Sequence Length: 193
Sequence Mass (Da): 20494
Location Topology: Multi-pass membrane protein
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W1V7C2 | MGSRVRARGLMALWGTTRRAWIVSGQRPNGGGPTLADVARERERVHRPDRSCTVNEMPGDVDLVNSPEVTYGYYVTQPTLASARCKEGCEKTMTDQTWAVRAACATVEPDQLFGKGAEQRDARSLCFSCPVRMECLAEALDSESSFGVWGGLTERERRALLRRFPEVTDWGAWLRREDDELIAEIHARRAPRILARVR | PTM: The Fe-S cluster can be nitrosylated by nitric oxide (NO).
Cofactor: Binds 1 [4Fe-4S] cluster per subunit. Following nitrosylation of the [4Fe-4S] cluster binds 1 [4Fe-8(NO)] cluster per subunit.
Function: Acts as a transcriptional regulator. Probably redox-responsive. The apo- but not holo-form probably binds DNA... |
A0A6A4T7C3 | MTEDETTHPNIIRQLKLQQLLLLVYYHGVSPERCVAQVQLQDAAAAAAAATRARDSDDSVISYWPAQLEPAAESSKRQREESRSGSPEEEPPERRLRRGPDVQADRSPSPQPPTSDPQDRLEELQPETLVLDCVWLKAAVIEKHGRLHGCCERRFLRPARSGSGAADPPVQHDPGPPHRGQEAREGAEPRRHGGAAGAREKRRAEDDREGNGELRLQILTLVYLLSTGFVLGGAFGVFTAGIDTNVGFDPKDPMRTPTAREVLKDMGQRGMSYAKNFAIVGAMFSCTECIIESHRGKSDWKNAVYSGCVTGGAIGFRAGV... | Function: Essential core component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. In the TIM22 complex, it constitutes the voltage-activated and signal-gated channel. Forms a twin-pore translocase that uses the membrane ... |
A0A924IPS4 | MKKLFAQRKTNALLSLGALGIVFGDIGTSPLYCFSVIFGNGGDNIAANKTNIYGVISLVIWSILLVVTIKFIAFIMRAGNAGEGGIMALLAQIRNGKVRSRYSKILLLIGLIGVGLFYGDSVITPAVSVLSAVEGLKVVAPHAALIVVPLTLLIITALFTIQHFGTSVVGRLFGPIMLVWFTAIGTCGLWRVWQQPSVLTTLSPTTAISFFIYHPLLAFIAMGAVVLAITGAEALYADMGHFGRTPIAKAWYFIVFPSLILCYMGEGALLVGDPSVAANPLVLMFPATLRIPFVILATFATVVASQSVISGAFSLTKQAV... | Function: Transport of potassium into the cell. Likely operates as a K(+):H(+) symporter.
Catalytic Activity: H(+)(in) + K(+)(in) = H(+)(out) + K(+)(out)
Subcellular Location: Cell membrane
Sequence Length: 632
Sequence Mass (Da): 68710
Location Topology: Multi-pass membrane protein
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A0A4Q2ZHV5 | MAQLGRIGIIGNGSFGTALAKILTDNGHQLQWWMRSEEAVQFLQEKHHNPTYLSSVHFQPQQIAPTTDLNQVLRNCDTVVFAVPSAYSAAVLQSAETCLWNNVHFISAIKGILPGTGKLLNAYLADTCNTDPQQYVAITGPCHAEEVAQERLSCLTFSGMDADLTETVAQTFATPYLHTRFNKDVWGAQFAAVLKNIYAVGAGIAHGLDYGDNFMAVYITACFREMHKFVKKHFRKLHEEEKLPDFLTSAYLGDLLVTCYSLHSRNRAFGMMVGKGYSVKAAQMQLNMVAEGYYASQGMMQVADESGIKLPIASLIYKIL... | Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Catalytic Activity: NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH
EC: 1.1.1.94
Subcellular Location: Cytoplasm
Sequence Length: 338
Sequence Mass (Da): 37500
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A0A8D3BFR9 | MALQELGISLSMIGVAGTILICTLPMWKVTAFIGTHLVVMQVFWEGLWMTCVSEYTGQLQCKLYDALLDLSPDLQAARGLICISLVLGCLGFLIFLLGARCTNCLSHPSVKARVVLSSGAIFCLASLTTVAAVSWTANSIISDFHNPRVPEALKRELGAAIYIGFVTSGLLFCGGAILCTSCPPERARFPSNGYARGRPPPQDSYAIKNYV | 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: 211
Sequence Mass (Da): 22681
Location Topology: Multi-pass membrane protein
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A0A8B8LKI5 | MSETNASFVEGSHSQVRVFVRRNKRSRIIQQKEHLPSNTHNDKKLVLPEIEDFAYSGAKELDHCRKSEMDSDVTPVKSEVASARLSGESPAHWEKVLEGIRKMRCSADAPVDTMGCEKAGNTLPPKERRFAVLVSSLLSSQTKDHVTHGAIQRLLQNDLLTADAINNADEETIKKLIYPVGFYTRKATNLKKIANICLMKYEGDIPSSIEQLLLLPGIGPKMAHLVMNVGWNNVQGICVDTHVHRICNRLGWVSRLGTKQKTLTPEETRGALQRWLPKEEWVPINPLLVGFGQTICTPLRPRCGECRISELCPSAFKEAS... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster does not appear to play a role in catalysis, but is probably involved in the proper positioning of the enzyme along the DNA strand.
Function: Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base exc... |
S9PDP8 | MNYHLRTQAELDASLDQVLAAAPHDVTRSDSWLLVYGSMLEEPPFSPEDRRPATLEGWERVFCLADPKMRGTGRRPGLCLGLVRGHRCRGLAYRLAARTVREDLRRVWEREMLLPFYVPCWLEARTPRGLITALTFCTDPDSPLYEPSLSEPAMIERLARCEGENGSNAEYLDETVRQLAEVGLPDTGLDHLAERVRAVRAARLELR | Function: Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides.
EC: 4.3.2.7
Catalytic Activity: glutathione = 5-oxo-L-proline + L-cysteinylglycine
Sequence Length: 207
Sequence Mass (Da): 23516
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A0A935G8N0 | MRSAPPPRATCTTCCLPRSCTRSDKPVFRPGSGKNDLEVGGRKIAGLGIHVNPHGAAQFHASLLVDLDIPLMLRVLNIPLQKIGDKVNIQKVEQRIATVSGLLHRPVATDEVRQLIKSAYAAHFGVQLACQPLAPAEHQAIRQLAEEKYEHADWVFQRSPQPDMTGMGLKKTAAGLLRTYVALKGETIKSVLITGDFLGLEPLFQHIEAQLKWSPLDQQHIEKVVELAFEKHNTAEAGIEPAELCQAIWRAALGAMKEVQHTYRGSCYYPKISL | 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: 274
Sequence ... |
A0A8N4EXK5 | MQKSKSISQIQAPTYGNLITILSIDGGGIKGIIPATILTFLESELQKLDGEDARLADYFDVIAGTSTGGLVTAMLTAPNEENRPLFAAKDIKDFYMKHSPKIFPQCGGPLGQAAKILRAISGPRYDGKYLHEWILTKVE | Function: Lipolytic acyl hydrolase (LAH).
EC: 3.1.1.-
Sequence Length: 139
Domain: The nitrogen atoms of the two glycine residues in the GGXR motif define the oxyanion hole, and stabilize the oxyanion that forms during the nucleophilic attack by the catalytic serine during substrate cleavage.
Sequence Mass (Da): 15111
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A0A091Q337 | KQLLFFITFITFAFAVCVYLHHNWYCGPGVYTIFAFLEYLIVLSNMAFHMTAFWDFGNKELVVSSLLEEKHF | Function: Involved in the lipid remodeling steps of GPI-anchor maturation. Required for stable expression of GPI-anchored proteins at the cell surface.
Subcellular Location: Membrane
Sequence Length: 72
Sequence Mass (Da): 8521
Location Topology: Multi-pass membrane protein
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A0A1I5CPE8 | MHTVTPPHTPSGPAAGSGAGERAGWTDLPPPLDRRIAFALDTSSWVVLVVMSVLGLWGLRDTGSMVLAGALCLVYGLLDAVGRRHAAVPRYPSLLMALQTLVVAILLALPSDYRDAFAFLLVMLSIRCVLFLGPRAGAAWIALFWLLSSAAALWEYGLSGLVVAGFNLGVYPLCGMVGYALAALARSTAERADALAELQLAQARLRRVAVDEERRRLGRDLHDSVKQQVFATTMQIGAARALLADRPERASEALDRAEQAARRAGTELNTVIHELRSAELDGGVPLALQRLTDSWAQETGTPVRVGLAETVQVPEQAEHA... | 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 tr... |
A0A8B6XHE7 | MERKRKHSFDNEPSEKKSKEDDCSDNFVSSYSSVAQRMMSKMGYAKGKGLGKNETGRVNIIEASNQRGRRGLGLKLDGLDAKPDASWEVEEKIMVRQDPDWVPKNELDMPNASEMRNWMIESDRKEFITDEYEFCEPDILDGIIKNKNVFDKLGQKEFLHARTRANPYETIRGAIFQNRAAMKMAEIDASFDYMFTNHIERDLNNPLDLLYFADICAGPGGFSEYVFWRSKWRAKGFGMTIKAEWANDFNLADYIAGTPESFDCFYGEGGYNGDGDIFKKENLIAFRKYVLENSDNKGLHFVMADGGFSVEGQENIQEIL... | Function: S-adenosyl-L-methionine-dependent methyltransferase that mediates RNA cap1 2'-O-ribose methylation to the 5'-cap structure of RNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-capped mRNA to produce m(7)GpppNmp (cap1).
Catalytic Activity: a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucl... |
A0A936P3V5 | MLVFLIGFMGCGKSYVGRNLAPLMGFDYLDIDKHIEEMEGLTVKEILEQKGEAYFRQREREIILALDSSENRIVSTGGGAPCFFDNMDLMNEKGLTIYLNRTKKLVVYRLLKGQHKRPLLTGLSTEELEKFYDERLEIRKSYYEKAKIFAGDAGVEEIREMIDNSSQHNQ | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
EC: 2.7.1.71
S... |
A0A8B6XKX8 | MMKFLVLLLCFVSHVTLSWVPEMENKNLFEGDMVLTPDDINSNGYASIVGGRWPNNIVPYELSRMSSSNHIHVLRAIDEYHKHTCLKFVKRTNQDAYLSFYPGGGCSSLVGYVRGRINDVSLAGGCLRLGTVMHEIGHSIGLYHEQSRPDRDDHVTIIWNNIQSNMRFNFDKFDRNKINSLGFPYDYESMMHYDQTAFGGGQVTIRTKDPSKQKLIGNRQGFSEIDKQQINAMYNCNRGGSTLPPSVPPTVSPVAQCVEGQDLDNRCLGWATSGYCTATDPAHLETMKKKCCKSCKESAICNDKNTRCDEWAKKGECKAN... | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease.
EC: 3.4.24.-
Sequence Length: 336
Sequence Mass (Da): 37751
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A0A8B6XKZ6 | MARADTSNGSLYNNTKLKRIKKKSKTEEYFDEHLTEILPDSYQNGDVVSSERLLAFADVIMAICAAFLVVPIRNLVSLKNGQTLLEFIYKIQTEVIMFFLGFAVILAIWENINIRAMVIKRIDDIVLTLVISELLITTVLPFLLALQGFYPFEIASTILTCCILGLIQIIDIVLICYATSSPRILHIEMQKWSNCELRKVRTIFLIKPIVSFLLVLAGGLFCFIHFAISWSFIAVLVFMPTIRNLHLFIRQRIDKRSKMEKYQFYFFFSKGSILKDRVEVMSDTIIAIVACILILDITEKNFPSKERIQKYGLLSALDNM... | Catalytic Activity: H(+)(in) = H(+)(out)
Subcellular Location: Membrane
Sequence Length: 530
Sequence Mass (Da): 60505
Location Topology: Multi-pass membrane protein
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A0A385ZHT1 | MPATHHSSAPPTTSTEASTRALDTGPPPPERSSAAADRTPAVGRIPVLDVRPVVQRGRRPAKAVVGETFEISATVFREGHDAVAANAVLKDPEGRIGPWTPMRELAPGTDRWGATVAADAPGLWSFTVEAWSDPVSTWRHHAQIKIPAGIDTELVLEEGARLHERAAAGVPDDGRNGVLLAAVRALRDDTRPAAARLAAALTPEVDAVLARYPLRELITASESLPLLVERERALFGSWYEFFPRSEGTPDRPHGTFRTAARRLPAIAAMGFDVVYLPPIHPIGTTFRKGRNNTLSAGPEDVGVPWAIGSPEGGHDAVHPD... | Function: Maltosyltransferase that uses maltose 1-phosphate (M1P) as the sugar donor to elongate linear or branched alpha-(1->4)-glucans. Is involved in a branched alpha-glucan biosynthetic pathway from trehalose, together with TreS, Mak and GlgB.
EC: 2.4.99.16
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + alpha-m... |
A0A0A0MI16 | ELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLISSSIVESGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMRPNGMSFDQMPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTS | 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-cytoc... |
A0A437UX63 | MACPSLPDRIALRAPAKVNLHLGVYPGRDSRGYHRVDSVMIALELADEVSVSRAETAGVSFSLPLGIDIEKTAAYKAICAFEAAFTPWCSYHADITRRIPSAAGLGSSSTDAAAVLRAMAELDGIPTNDPLLIKIARALGADAAFFLQPNPALFVGSGDIHSRSFPQLRMPIVLVKPEAGVSTAEAYGAFDEDPASPPAPGTMVQALLDSDIPAIAASLYNNLSPAAVRLAPETGECVAWLRGQEGVLGAQVTGSGSCSFAICASDEAAARIASASPWWACATRTRVSDGRSSNG | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
EC: 2.7.1.148
Catalytic Activity: 4-CDP-2-C... |
A0A1X0QDN4 | MYIIKXXXXLKVIKLLIILKYKRVKWIYLVTIIILLLYISYMYIIKFDYRLNKIFCGTLVVIGTVASLIIIFNCKELLKNSISYWICLYLGFLIESMDFPPLFNYTTDSHSLWHMMLLLSIPCYYKMLETEFLLIKF | Function: Involved in the lipid remodeling steps of GPI-anchor maturation.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 137
Sequence Mass (Da): 16437
Location Topology: Multi-pass membrane protein
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A0A1W0X0A2 | MVMCQLILQSESAYSILAELGDAGVLHFCDVSVNDAQFRRIFVNEIFACVEMERILDSLSLAVAHLKVSPYFIHLPTPSPREYVTLLENLAEIKVDVFKVKDYMSMLEDRKMDLQLQADVFRQIDIFLQQANVVLPSPNQLANSDDQGGATIAEEKTALLHHKISSSLKLQFVNSDMQSNITGAQLKVKVEKACIAYRAKLYPFIAYPQEREEAQNRLRTEVSDIITVLEESKEHQRKLLADIASKLPAWRSKVRKLKAIFYTMSLFNLDLSDHCLIGECWCPAEEQTTARAAIERGSELAGASKPSLLLNIFTTKQPPT... | 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: 785
Sequence Mass (Da): 89010
Location Topology: Multi-pass memb... |
A0A1W0X150 | MSTGRDLTASLLVALCFRLTLIGGASGSTADLYKIVTCINPKFDPSVIGMFYGCYCGPGGQGTPVDDIDKCCKVHDDCYQTFEIQRSCQWYWPVLTTVSFVCNVNSTEPIKCRDENLCRKTQCNCDAAFSQCLHKLNATTPATRPKCPDWSRNNKFDLSWLLH | Cofactor: Binds 1 Ca(2+) ion per subunit.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
EC: 3.1.1.4
Subcellular Location: Secreted
Sequence Length: 163
Sequence Mass (Da): 18182
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A0A316JB29 | MAIQDIDEAGHLMPLEHNRFFSPVTFVLCIFLLMGGWAGKWAGDNFRLRDERADMNIYMNALQAHADRIIISAHNVLDEANRSPFQACSADDRVYLRKLIFTGYHIKDIGRLADDRLICSTLLNNVRSSSRRPMEDVRLADGTYIYRDGNLITPGSHGAIIGRGNANIVLSSVAFDAMQTPGYAFAIYMANEGRTQFARLYSFPHDYMKGADAALAFAGSGATEAASTVPLHEQHCNPATGICISLVSAPLPNNPSDQLLLILFTSFGMLLGSGAVMVWLYYRSRNRSLNAMLKRALAARKLSIAYQPVVRISDEKICGF... | Catalytic Activity: 3',3'-c-di-GMP + H2O = 5'-phosphoguanylyl(3'->5')guanosine + H(+)
EC: 3.1.4.52
Subcellular Location: Membrane
Sequence Length: 557
Sequence Mass (Da): 61292
Location Topology: Multi-pass membrane protein
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A0A178MWZ4 | MFAAYIATAIGGMTLASLPPGNLTVFWLPAGIGVAVLLVLGRRGTVVVAAASFTANGLMMGDQGQVLLATALSAAVDSLQSWLGWSLLRRHWDNLVGAPVHDPRRLRGLASICLIPPLATVWLLPLIHDLARTAGPLTLHAFLERTLMLLLADTSGLFLVVPVVVGFSAGWPAMRLPAALALLAVAQVAVSAIDPLLAPLALLGLALMAFIFQFPGAAAGNLVCATVMVVQAAFDLGPLRGQGTAQAIVVLNLTIVGVGIAVLYMGLLQDEQHRMRATLRDEVERRTRQLEERSRALAASNGELEQFAYIISHDLRQPLR... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 522
Sequence Mass (Da): 56423
Location Topology: Multi-pass membrane protein
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T2M902 | KEKVMDKIKRTISGKQDDEAGIVAEISDATTLSWSTRIKCFIGCFLFGICFSILGAFLFFKSLKLFGVFYTFGNLASLASTCFLMGPLKQLKNMFKEKRLIATIVMLGALTLTLCSAFWWNKKGLVLLFVVIQYFAMTWYCLSYIPFARDAVKKCIESLSWLRLTSSNFYFYLFFFVFILIIFIYN | Function: May be involved in fusion of retrograde transport vesicles derived from an endocytic compartment with the Golgi complex.
Subcellular Location: Membrane
Sequence Length: 186
Sequence Mass (Da): 21456
Location Topology: Multi-pass membrane protein
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T2M574 | MTNTCDPRPTPLSGIFKGTFAYLTIRDRMPAILTKVIDQMSRLASQYYNSNSLSKAEDAKEIVSKLCKLKNEMQTNKVIRKLNDFSNDSDMWNQFIEKMPILVEGETKPSWFTVAWLHCECYMYRRIIETFLESNSKLFLGGKRFLSDEEAITTMEQYFGELLENLYRDGTKLLEDYQYSLWSNKCDLSISFNGNNQIKSADEQNYLKANIISNHTDQLWTYLDCMRLSTGKGIITFVLDNVGFELFSDLCLADFLLTFKFCAEVHFYVKCMPWFVSDTTAKDFFWTIEQCVNSTDKNISDLGKKWQSYLDNNLFSIVED... | Function: Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate. Its preference for fructose-1-phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-control function... |
A0A6I9SEW7 | MAAPAKEAEYDFEWSPSPSITGGSPAARITPDFSPPLIAMVAVVGTAFLIVLYARILSRLLLLFRRRWRRWRRHRRLLQSAAASDLESPPPTGGAASFGSSSDYFRSPYGLDDSAIKTLPLSLYSKSKAKHLAATNRDCAVCLLEFEDDDSLHTLPLCSHSFHVDCIDVWLRSHATCPLCRAAVIRHESPFVPMRAARIRPSLDDLLLDQPPEAPQPVLDPESEIAAAAASPPSIRGDDRFGIRDMDFLLKRSYSFGFERSLAADRMVLETSMASPWRYRYRSFWSKRWPSPFGGISGGGSSSASRAARVFSFRSYRSVA... | 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: Membrane
Sequence Length: ... |
A0A3S0DKL3 | MPNNFLPGASKRMEVLPVGVFSIAATLLVLEIKVPHFEQNYSNAELWEALKNIAFICRLCIQLPEHTDLLG | Catalytic Activity: K(+)(in) = K(+)(out)
Subcellular Location: Membrane
Sequence Length: 71
Sequence Mass (Da): 7965
Location Topology: Multi-pass membrane protein
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A0A6A4SPG5 | MDTMMSEVDSWRRDPESFLRRRGLNPEDTTLTVEAEDVYVLIVEGFLIFNYRPLNELFDKRYFMDIPYDVCKRRRSLRVYTPPDPPGYFDGHVWPMYLKNRQEMENMVSGIVFLDGLKPKEELLDAVCKDVCWEIDRLSVFLKRVRDKTLDENDLQLQHMELYSWRLDRGCQNHREPDVFDISGQCCESVPHLCSKLPGLFFIFRLKPARLLFEFQVCRVKPSCSRVISFATIAQTCSDPSSCSSSCTQNHRNFYRKVRTCQQNIYVCLSESTCLTGMFSTAMPTTLNEPSLNDRPVIGILAQVVSDDDLKPFGTTFIPA... | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + (n-1) H2O = (6S)-5,6,7,8-tetrahydrofolate + (n-1) L-glutamate
EC: 3.4.19.9
Subcellular Location: Secreted
Sequence Length: 688
Sequence Mass (Da): 78754
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A0A4Q3E7Q2 | ISILYGGSVKGNNAKEIFSKADVDGGLVGGASLNAEEFIQIIAALK | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
EC: 5.3.1.1
Subcellular Location: Cytoplasm
Sequence Length: 46
Sequence Mass (Da): 4679
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A0A1W0WXF3 | MDVIFNETVRLMGNATAGRRLTRPGSFPWDYRIVATVLQSLIFLLGFCGNILLIIVVKRTRALHTPTYCYLVSLAFADLMVLVSAVPEAIMSNHLYFRQWVLGQVGCSVLIFGNFLGINAGSLSIITFSIERYIAVRHTMLAQRICTVARAKLISLCVWAFCILYCSPWLGLTLVKPHPRDPRLEVCDFRVSHQQYVYYFTIDITLFYFIPLILSVYLYTRIAQVLRSRNQLKGLTEAVPINRVKDSQTSITSPNGRKLGWQEPTAKGAAANVVVRMEDVSVSGIWKQRFSSMTSSRHKSRMNENANTQAIQMLVMVVFL... | Function: Receptor for thyrotropin-releasing hormone (TRH). Upon ligand binding, this G-protein-coupled receptor triggers activation of the phosphatidylinositol (IP3)-calcium-protein kinase C (PKC) pathway.
Subcellular Location: Cell membrane
Sequence Length: 403
Sequence Mass (Da): 45891
Location Topology: Multi-pass ... |
V4HAC3 | MDDSRVTVLRYGHRPGRDDRMTTHVGLTARALGADRVVFPDNAGQAADTVRGVTDRFGGPFEVELRDDQRAFTRDWEGPVVHLTMYGERVQDVEREVREAHAEGPLLVVVGGEKVPFDFYEHADFNVGVTNQPHSEVAGLAVFLDRLFEGRELEREWADAERRVVPQETGKRVVDPDDADGGAE | Function: Specifically catalyzes the AdoMet-dependent 2'-O-ribose methylation of cytidine at position 56 in tRNAs.
Catalytic Activity: cytidine(56) in tRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(56) in tRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.206
Subcellular Location: Cytoplasm
Sequence Length: 184
Se... |
A0A832QBY7 | MKNFKELSDLKVSEVEKKISEKWEEQNILQKTIDNREGNKNFVFYDGPATANGMPGLHHMLAKFLKDTFCKYKTMQGYRVLRKAGWDTHGLPVEIEVEKELGFTSKADIEKFGIEEFNIKCKESVLKNEKAFRDYTKKMGQFIDLDNAYLTYDNDYIETEWWILKRFFDEGYIYEGHKILPFCTRCGTGLASHEVAQGYEEIPANTVIVPMKMKKEDAYFLVWTTTPWTLISNVALAVHPNEKYVLAESRGYKFIFAKALVSKILGEEAKILKEYLGKDLEYTEYEQLLPFITPDKKAFYVTCADFVTMEDGTGIVHIAP... | Function: Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves ... |
A0A1W0XAT2 | MTPRRNILLLNFAHYGHIIPLLELGKKLSQHHDVDFLVSSVRVPEIAFRGLLPADTLTTGSLNVIGLADGLTLEMCNEIGDGAEVSFVQRIEIIVNAYRQFLPSHTPAVVIADHFLYGAAEITHSHGIPFYFFHTASTKSALEVLDFNGPTGREFEDAMYPSMKAATVYTVGIIVNSTRELDLEAARKLQSNPLLRGKDLKLVGPVFSATEKPNEEADFRAWLDSQAQQSVVYVSFGSLVCPSANQLHEIGLALLSLGRPFIFSLPEAHRRHLPRELHDGADGRRDGADRRRDGADRRRDGADGRRDGAAGDRKNFLIPG... | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 467
Sequence Mass (Da): 50956
Location Topology: Single-pass membrane protein
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A0A5P9KIQ0 | MLYFILGLWSGMLGTSLSMMIRLELGTPGQLIGNDQIYNSIVTSHAFVMIFFMVMPFMIGGFGNYLVPLMIGAPDMAYPRLNNMSFWLLPPSLFLLIMSNLIGGGVGT | 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-cytoc... |
A0A432FD29 | MKNKGMFLESLLNKTISFYEKNMVGMFHKKPIPINFNSVKKGREVNQAWIASKSTVDYYGIYKGIFIAFEAKSTRLKSLPLVNIKYHQIDYLNKVNTLGGLGFFVIYYDTYDEYFLLLPGDLEGLDQKSLNIDVARKKGYSLEVMYPGILDFASVLDNLL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Endonuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves mobile four-strand junctions by introducing symmetrical nicks in paired strands. Promotes annealing of linear ssDNA with homologous dsDNA. Required for DNA repair, homologous ... |
A0A090SWZ1 | MDVVLSGELNEMSMVLDFGKVKKQIKHLIDEYVDHRLLVPMKSNAVRHQASNQLHQVRLS | 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: 60
Sequence Mass (Da): 6927
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A0A098S841 | MANALFFFKALHVVGFVSWFAGLFYLGRIFVYDEEASGKAEPERSTLKQQFNLMEWRVYRIICNPAMMITWTAGLIMVGLGLFSPLVPNYLTSGTPGWMHLKLLLLVLMTIYHLWNKRIIRRMEAGERPFSSWQYRLLNEMPTLFLISISYIAVYGKAGTLNYLYLVGGIIVFVGLIFLGARAYKKAREKVQRS | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
Function: Catalyzes the oxidation of protoporphyrinogen IX to protoporphyrin IX.
EC: 1.3.99.-
Subcellular Lo... |
A0A496NEZ8 | MKIHSIKQPMTFALFKQTPDDFIVTEKIDIDFNHEGEHLWIYLQKVNLNTLFVARLLAKWANIAISDIGYSGLKDRNAKTYQWFSLRIPKKQKPDIDFDNFISKQNLNAGEFVCILNYIWHNKKLNRGTHKHNHFTICLKKVIGDKEKINHRLQQIKEIGVPNYFGKQRFGRDGANIEKTYQFFEDILKSNKSYKPHKKDREKHSLYISVAKSLIFNAILEEREQSDNWQTPILGDVFNLDGSHSIFTNNIDSTIYQRLHIHDIHIASILFGIGERKSSLLARQIEDKILNAPQFINLTEGLLKINSQLSWRSLRLLPQK... | Function: Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
EC: 5.4.99.27
Catalytic Activity: uridine(13) in tRNA = pseudouridine(13) in tRNA
Sequence Length: 375
Sequence Mass (Da): 43711
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H2E2E0 | MVVYVVFFMLFMMVVLSLMATVWVFSGMSVMVYVMMMEVSWGMVKVGVVLDEISVVVSMVVLVVSMMVMVFSAYYMVDDGSLSYFVVVVCVFVFGMLVLVLSGSFLVSYVGWDILGVVSFMLIMYYGNYTSVGGSLVTMLMNRVGDCLLIIAFVWVLMVDQEWWAVGKVNSVGMACLSLLVIMAAVTKSAQFPYSVWLPLAMAAPTPVSALVHSSTLVTAGVYLMIRWNGVMGQWGAGALLVMSMVTVLYSGLMLVSEEDFKKVVALSTLMHLGIMMGMVSLGGWYSGYVHLVLHAVYKSLLFIGVGVVIVNMSHDQVFG... | 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 ... |
A0A085EIB0 | MKKDFYEILGISKGADAAEIKKAYRKCALKYHPDKNPGDKEAEENFKLAAEAYEVLSDPAKKAKYDQYGHQAFDGSGGFGGGHMNMDDIFSQFGDIFGGGFGGFGGGGGGPRRAKGSNLRIKVKLTLEEIANGVEKKVKVKRKVQAPGVTYKTCSTCNGQGQVMRVTNTILGRMQSASTCPTCGGSGQILDKKPSNADSQGMVVEDETVSIKIPAGVVDGMQLKVSGKGNDAPGNSVPGDLIVVIEEVEHEFLKREGENLHYDLYISFAEAVLGISKDIDAVNGKVRIKLEEGIQSGKILRLKGKGIPSINGYGSGDLLV... | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction... |
A0A6A4T7P5 | MAASVAATARAHRKVLRVGSIYEPLKLSNLKREDEPLWEKLDRYYNAVKTTILNYQSPTTGLFPVNTCSTCKEAKVRDSLYCAAGAWALAMAYRRIDDDMGRTHELEHSAIKCMRGILYCYMRQADKVEQFKQDPSPSKCLHSVFHVDTGDEVHSYSDYHHLQIDAVSLFLLYLVEMICSGLQIIYNTDEVSFIQNLVFCVERAYRVPDYGMWERGSKYNNGSTELHSSSVGLAKAALEAINGFNLFGNQGCSWSVIFVDLDAHNRNRQTLSSLLPRESRSHNTDAALLPTISYPAFAVDDDALYSQTLDKIVRKLRGRY... | Pathway: Glycan biosynthesis; glycogen metabolism.
Function: Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I.
Subcellular Location: Cell membrane
Sequence Length: 431
Sequence Mass (Da): 49316
Location Topology: Lipid-anchor
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A0A4Q0M528 | MLIRERAAAKVNLTLHIHGRRADGFHELDSFVAFAGCAADALTLSPAPALGLHVVGPFAAAAGEGGDNLVLKAVQAATERIDGLKLGLFSLVKRIPVAAGLGGGSADAGAALRLIAEKNGLALNDHRLHCAAAAVGSDVPACLGSRAARMTGRGEKIDLLKDFAPIPAVLANPMKALSTAKVFSALALRSGESLDAAAPLPAPRQRGGWTGAPALSRGGIGGVERGPSVGLDNARFPPDPVGAGPPSHFQGEGSAAAIDVILTGRNDLELPARALMPEIALGLDALSASEGCRLARMSGSGATVFGLYDDQRAARRAARA... | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
EC: 2.7.1.148
Catalytic Activity: 4-CDP-2-C... |
A0A6A5DUX1 | MAVSRENCVERQVLSRLFPFKRGLCHAYWAPNIWALYNTLDKILATLGVRVKLLQEAELPRASMTGGLVQEFQHAVLPSITPSITLICTLLSILVSHSRETELRAASIWWRPRGARGFLRCLLLCALGSFVFGWHVHEKAILMAILPLSILAVENREDAGIFLVLTTTHYSVPLLSPRR | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 179
Sequence Mass (Da): 20143
Location Topology: Multi-pass membrane protein
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A0A1N7KAR9 | MPSSALPVQEKHRDKPYAPPTYNGSMTDLDLRCYFVTGAGAPDQIVETARAAAQGGAGIIQVRSKPISARDLYDLGLSVVTAVHEVNPSTHVLIDDRVDVALALKPHGVAGVHIGQDDLNPRIARDLLGPDAIIGLTTGTLDLVEAANDFADVVNYIGAGPFRDTPTKDSGRTPLGLDGYPALVEASKLPIVAIGDVTVDDAEALARTGVDGVAIVRGIMNADNPRDYVEHVIANVDRGRL | Cofactor: Binds 1 Mg(2+) ion per subunit.
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-met... |
A0A1H7W7Q1 | MAQIPIKRSIERVPGGMMIVPLLAGSLIATFLPDAPKFFGSFTNALFTGALPILAVFYVCMGAGIDVKATPYILKKGGVLLVTKVGAAVIVGIVLGHFLGERPVSSGLFMGVSTLAVVAAMNDTNGGLYMALMGQYGRKEDVGAYTLMSLESGPFLTMVTLGVAGLSAFPWQTLVGSILPLVAGMLLGNLDRDMRDFLARAVPVMIPFFALALGAGLDLHKVWQAGLLGIGLGIAVVVVTGIPLYFADRLTGGTGVAGVAAANTAGNAAAVPALIAAANPVYTDAARSATLLVAACVVVTAILSPILTSTVAKRYQQRHP... | Function: Catalyzes the proton-dependent uptake of 2-keto-3-deoxygluconate (KDG) into the cell.
Catalytic Activity: 2-dehydro-3-deoxy-D-gluconate(in) + H(+)(in) = 2-dehydro-3-deoxy-D-gluconate(out) + H(+)(out)
Subcellular Location: Cell membrane
Sequence Length: 336
Sequence Mass (Da): 34661
Location Topology: Multi-pa... |
A0A8N4EZ01 | MVVHNDEWTWEYIYHCLYIEKAFDNIVISPGPGSPTCHKDEYALKYLVSARIFQSWVFVLATRFCYNILALGFVHGAKIVHALEPIHGRLSEIDHTGCDLFKEIPSGMESGFKVVRYHSLVIDADSLPEELIPIAWTTSVHTLSFLGTQQSDIILGSFGDKATLQPIGFLDGKVKDKGISTINNNVNGLKSTKVLMGVMHSNQPHYGVQFHPESIATSHGRQIFKNFKKMTIDHGLRTSLLHERKVHNSGKQQMFLVSHACQSSEFPRSKILLNKSDMTHHLDMCKPPIFAFKSMEVKYVRMQWKKIEGLASQVGGSENI... | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 4-aminobenzoate from chorismate: step 1/2.
EC: 2.6.1.85
Catalytic Activity: chorismate + L-glutamine = 4-amino-4-deoxychorismate + L-glutamate
Sequence Length: 618
Sequence Mass (Da): 69191
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A0A141IPC2 | GMVGASLSSFIRLELGQPGSLLMSDQIYNTIVTAHAFVMIFFMVMPMMIGGFGNWLVPLMLSAPDMAFPRMNNMSFWLLPPSLTLLLTSSFTSMGAGTGWTVYPPLSSNMAHGGPSVDLTIFSLHLAGVSSILGAINFMATILNMKPKSMKVEQIPLFVWSIFITTILLL | 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-cytoc... |
S9R3F6 | MAIILGHSVEPPGECSYLPDQSSSMEQFVMKDVTAEEYERMLVRGWRRFGPMYFRPACQACFQCVSLRIPTATFQPNRSQRRARAACAHLRVEVGPPRVDEERLALYRAWHAEREQTREWNASPIGPREYFLQFAFPHPCAREVAWYDDTAEGGPRLVGLGICDEMPQAWSAVYFFYDPAYARASLGSANVVFQVELARARGIPHVYLGYRVQECASLRYKGAFRPHELLEGRPAPDEPPRWTPAEDPGDTPP | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu from its aminoacyl-tRNA to the N-termini of proteins containing an N-terminal aspartate or glutamate.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-aspartyl-[protein] = H(+) + N-terminal L-leucyl-L-aspartyl-[protein] + ... |
A0A385ZT53 | MSQGPRSGLAAVSSALLAMSRHLEVRDVLKTIVASARELLDAQYAALGVPDDHGGFAQFVVDGVSDEQWKAIGPLPRQHGILAAMLHEATPERLADVRKDPRFEGWPSAHPEMSDFLGLPIRDGDEVIGALFLANKNCDKPEGGCGFTEEDEQLLSILAQHAAIALTNARLYERSRELTIAEERSRLAHELHDAVSQKLFSLRLTAQAAAALVDRDPSRAKGELHQVAVLAAEAADELRAAVVELRPAALDEDGLTATLRTHVQVLDRAHTARVTFTARSFRALPAAQEEAMLRVAQEALHNALRHSGAEHVDVTLDRRG... | 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 tr... |
A0A8B7D7F2 | MLPENHHRGDIVSSNRMLAYSDAVMATCATFLVLPFRNLKVIEELKRNNSTCNLSRNSTKNSTFNLNEYYENNILSVYFCHNYTEFIMFFIGFLIVLTIWENMNIRSLVIKRVDDFILTLVIFEMLLTSFLPFSLALQGHYPDQKSSIIITCVVLGILQIIDIGIILYSLHSPKLLHIDLKVWSQSDLQELILIMVFRPLISFLIVSIGGALCLVHYGASWACIGSVPKERVEIMSDAAVAIVACIVILDITVEEFPKKDKVKKEGSSKAAPYVLYVTVLAVPCSFFVSKLILMNHIGKAAVYFTHSIIRKLTSKRNKPK... | Catalytic Activity: H(+)(in) = H(+)(out)
Subcellular Location: Membrane
Sequence Length: 336
Sequence Mass (Da): 38095
Location Topology: Multi-pass membrane protein
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A0A1W0WV49 | MDISKIRSKKPDEEDLDESFTPKVLIFDSADESINEDGGENAGEDDEILEVTVRIPLKKMTSLPTKKRKMDVALSPNFLTGLDLGGPPRKRLSTLDGNTVHSARRLGTTPGMTKPPPAVMKPPPKSLSSPLNADGTPFCVIRKKTQTGDGSTTLLLPTVRGAHSDLKCISPATLIDVLRQKKPYDVAEVSVVDCRYPFEYQAGHIQGAINIYTPDDLKARFLNLSVENPVEKKARKIIIFHCEFSSERGPDLYRILRNEDRILNEKRYPALHYPELYLLHGGYKAFFEQFRTYCFPQVYMPMNTPGHEDDVSQCKRKAKL... | Function: Functions as a dosage-dependent inducer in mitotic control. Tyrosine protein phosphatase required for progression of the cell cycle.
EC: 3.1.3.48
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Length: 338
Sequence Mass (Da): 37811
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M1F8Z2 | MVDVKLIEPLFLILVPLLYFIGAITSSLKIPLNSPLICNLAFVAALAGAMSGWLLPGSASWLNLAPLAYIMLLLITLLGAILARFSMRYLAGDPGQRRFMVWLQIILGAVSLIVTTNHLLVFLASWIVISISLHQLLMFFPDRPRAALAAHKKFIFARLAELCLGLGFALLYFQYNTLFIDQILAASAETDAIPVVAQFAAVLMAVAALLKCAQLPFHGWLMQVVESPTPVSALLHAGVVNLGGFLMILMAPLISQVSAAQWLLLLVAGPTAVFASLVMMTRISVKVRLAWSTCAQMGWMLVECALGLYELALLHLVAHS... | Function: Part of an energy-coupled inorganic carbon pump.
Subcellular Location: Cell membrane
Sequence Length: 517
Sequence Mass (Da): 56290
Location Topology: Multi-pass membrane protein
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A0A2M7R531 | MKVREIFTSIQGESSYSGIPCTFIRMTGCNLRCSYCDTTYAYYDGRELSEEDIIGEARRADINIVEITGGEPLLQKEVFHLIKKLLDEDYKVLIETNGSMNIKDVDKRAVVILDIKTPGSGMSEKMDLSNLKNIKSTDEIKFVVTNRTDYEWSKDIIHKYNLINKCRLLLSPAYGSLPPEDLARWMIEDRLKARLNLQLHKYIFGSDKKRI | Cofactor: Binds 1 S-adenosyl-L-methionine per subunit.
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
Function: Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7-deazaguanine (CDG), a step common to the biosynthetic pathways of a... |
A0A6B9VT58 | TLYFIFGAWSGMIGTSLSMLIRTELGNPGSLIGNDQIYNVIVTAHAFVMIFFMVMPFMIGGFGNWLTPLMLGAPDMAFPRMNNMSFWLLPPSLSLLLMSSIVESGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRPSGMEFDKMPLFAWSVVITAFLLLLSLPVLAGAITMLLTDRNINTTFFVPQE | 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-cytoc... |
A0A8D2ZL77 | MSQKDDVCRNRMKSLRSDNMLESGCAAGGSPESLDVVKPADSRRISQRRCFCFILVFAAIFLIFYNTNIIEMADEWNPKWWIQYNSTKWWVPFKSQRQNVAFDNTTDTSTSTSTSTSTSTSTSTSTSTSTPAPAAETSSSVAPQATQNNSGPPAPVPYVSPGPYLVEYPHQYHFRINEPQTCEEQKPFLVLMVPVAPHNRAHRDIIRSTWGGESSVLDKVVKLFFLLGRHRGEGAEQLGEQLLKESNEHRDLIQSDFLDCYKNLTIKTMVMLEWLDSYCSSASYAMKIDSDMFLNVPNLINMLSNAPKTNYMTGLVARGA... | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 438
Sequence Mass (Da): 49428
Location Topology: Single-pass type II membrane protein
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A0A8D3CC44 | MVLTLFVAEMYSLTATTLLVCFLKQLLSVLGLPDDLIQKGKDIKSISEIEETGDNFKVTVTTGTKVLVNIFTIGQEAELETVTGEKVKAVVEREGNKLKVCLKGIVSVTELVDGNTIVNVDRLKAEIEQICVASRPVCITFFFLSPLPRQ | Function: Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport.
Subcellular Location: Cytoplasm
Sequence Length: 150
Domain: Forms a beta-barrel structure that accommodates hydrophobic ligands in its interio... |
A0A2G6C2R9 | MRSSNRRQTVRVGNLGCGVELSLEGFVADKQPRIVLVGGGSGGHITPLVAVAESLRRYEPQCHLVYVGQKGDALATVITQGNIVDSSRLVSAGKFRRYHGLGWRNLLKVKTMLLNVRDVFRVVIGFGQSVVLLARLKPKLVFIKGGFVGVPVGLAAALLRIPYVTHDSDALPGLANRIVARWARLHTVALPAEIYSYPSDKTVTVGVPVAAAYRPLDSQRRQAARRAVNLSESALILLVSGGGLGAKRLNDAIVQQAQRLCSTFDDLHIVHQAGRANQQAVQAGYDAAGLHERVTVLGFSDDFVQYASAADVVVARAGGS... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-t... |
A0A024UKW7 | MAAQGVSAMHHCDSDPSLEAPPPSPMNPPMSPRVHVHSGERGITQLLDRNRAWADSMLEKDPDFFTRLASQHSPEILWIGCSDSRVPANEILALSPGEVFVHRNIANQVSTFTIVCAHRLLVTLMSRTHPRVSLVSTDMNCLSVIEYAVKYLQVRHIIVCGHYGCGGVHAALSQDEFGLVDNWLRSIKDLYIENHKKFGHITDTTTKADLLTEENVARSVYNVCHSRIVQNAWENGQTLSVHGLCYRLQDGIIRDLQICISGEDQVEAIYRRMMTKSKPEL | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 281
Sequence Mass (Da): 31494
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A0A2U9BXQ4 | MWDFLLFKTGGGEDSQKKNEEKETECQQWTDSQTDEDSDTEGILMGIQESCATDPHHHPQLETDVEAVRTLYSGSAASVRVYGSIDDVDVDLNINANFLDEEVAKAWGINQSEPIVIRLHFSLSQYLDGPAPSVQVFQPSNTDHFSLGKQLQNILAVFISREWEHLTNEKIVVQQKCRHSWYRPSGTIKKFRARLSIWLPLSKSNDLQHPTKRGRIFLPTMKLNRFTNHTTSYSIKNPTGELFTYTPSGKRVVVSAVKSSTQLSTKQLMELLFSSQAIGHCKTPPTLKHGFLVQIMRYAEQRMPTLNEYCVVCDERHVFQ... | Pathway: Energy metabolism; oxidative phosphorylation.
EC: 2.4.2.-
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 906
Sequence Mass (Da): 102465
Location Topology: Peripheral membrane protein
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A0A1I5I9L2 | MSGAEVYAALFGGQVDPDWESYASCREVDADLFFPEERESAGRVKAICRSCSVRDECLATAIRRGESHGIWGGMTARERGALARSLRDDGFAVPRAARRPA | PTM: The Fe-S cluster can be nitrosylated by nitric oxide (NO).
Cofactor: Binds 1 [4Fe-4S] cluster per subunit. Following nitrosylation of the [4Fe-4S] cluster binds 1 [4Fe-8(NO)] cluster per subunit.
Function: Acts as a transcriptional regulator. Probably redox-responsive. The apo- but not holo-form probably binds DNA... |
A0A4Q5ZH14 | MKNSSSYLLDFQEIDQTNRPRVGGKCANLSELSRIEGVQVPDGFCVTTEAFTESVGKSDALNDLLNQLAGLKAENRKAISETSARIRQVIEATAIPEAIEMTIVRHLEQSGERDAYAVRSSATAEDLPTASFA | 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: 133
Sequence Mass (Da): 14433
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A0A3B9AMC4 | MLFTHKTHSNLSQYGWSVATVLAIAAICFPFTDLIGYRTVSLILLMVVSILAMRFSIGPVSVAAILSALIWDFFFIPPHFTLTVGHGEDALMLLMYFIIALLNGILTNQMKVYDRIMRRREDKESTLRLYNTLFNSLSHELRTPIATILAASENLTSKDQQWSEQDKLAMNQVIHTGAERLNRLVDNLLNVSRLESGHLTLKWDWCDVGELINTAALRLKPDLDNKTLDVKIPANWPLMRLDFVLMEQAIYNLLHNAATYTPPGTRIEVDGAYQNHQLTIRISDNGQGFKEEEDLLRIFEKFYRPAGSKAGGVGLGLSIV... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 359
Sequence Mass (Da): 40392
Location Topology: Multi-pass membrane protein
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A0A955F7X4 | MKPDQFTLKETMLPVGNGHRLYVQLWGDPNAEQTLIWLHGGPGSGSRDEQKDLFDPKRHRVIFYDQRGCGRSRPYGSLRANKTDDQVADLSKILDAFSVDSCTLVGGSWGSLLALVYAIRNPKRVKRMVLRGIFTGRQSEVDFVDGGGCREFFPEVWEQFVTSVPSAHRMDPAGYLLPRLFGKYAEQAKRAAFAFNMLEGSLTKLDYQPLDVDFDTFDLVNTIIEQWYVSQGCFLPDSYILDNAALLTMPIDIVQGRYDMVCPPITAYELHQRLPNSRLTWTLAGHSWADRANLDAVKNLL | Catalytic Activity: Release of N-terminal proline from a peptide.
EC: 3.4.11.5
Subcellular Location: Cytoplasm
Sequence Length: 301
Sequence Mass (Da): 34044
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A0A1W0XD71 | MLELHVRKTMMLHVFIVAASLLDILTTVLGAPEKSKISAKDASIPDDLSAEVNKFGVPRDTPIAFLDGIQAFNNLQPIEKCRVHHISRASWTGALIDLYQTSAESPLIFLLLQNLFRSQEISALKRTATEACKFQQEDWDSLLVYVAAFYDNFGNYFTYGMKKFVPRVSSSKLECLINSTAALAKQAGESASSLQSLWNKTKELIYQLGSRHQSLAFGPGGITTYFSSNCNASDATLVKDFMVSKNVEAWNSRVIKTFDTQTGQPKYEIRFASALATGKAVVVDELKLGVAIEYKGASFTFTRGDFKQLLVRVNQQLTQA... | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.14.4
Catalytic Activity: Release of an N-terminal dipeptide from a peptide comprising four or more residues, with broad specificity. Also acts on dipeptidyl 2-naphthylamides.
Sequence Length: 797
Sequence Mass (Da): 88740
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A0A1X0Q6T8 | MLTALSGYIYGQSSDKFTFDKSNNFPHNFDYVGMRRMHAAIGSLISLFAFLTLRNFKFSRKRSFLGSLIIIFDNGFTTICRLIILDAHLLCFTSFILLAFSYYYKTKGSILSQLLLGVGLGCVVSVKWLGCLTMLYVGIFIIYELYMESITKSVKNVLKFLVQRSMFLIVIPLLIYLFSF | Pathway: Protein modification; protein glycosylation.
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: Membrane
Sequence Length: 180
Sequence Mass (Da): 20614
Location Topology: Multi... |
A0A4R3EFU1 | MRGLNIVFRSNLRPLGVIFAASLVWILAVAVAAQESASNKGANQEPITPLENPPALDPSKVALGESLFKDPILSGKNNLACSSCHDLNTGGAIHVQRTVGHDGQMHRFNTPTIFNAANNYRLGWLGRFTTLEAQNEAGLLDPNLMASNWDDLISKLNASKNYNAQFEKVYGHEARRVDVLDALATFQRSLVTPNSRFDRYLRGNAAALSPEELRGYELFKSYGCTSCHQGTNVGGNLFEKFGIFDAPPSPAGTTDESDLGRWTVTHAEQDKGVFRVPSLRNVAVTAPYFHDGRTASLPEAVAIMARVQLGHAASNDDISA... | PTM: Binds 2 heme groups per subunit.
Cofactor: Binds 2 heme groups.
Subcellular Location: Periplasm
Sequence Length: 346
Sequence Mass (Da): 37445
|
A0A7K2YVS4 | VAACVAGHRSAEPGHAAALAKLSLRPLVELELRLGEGTGAVLALPLVQSAVRVLHDVATFDSAGVSGKTD | Pathway: Nucleoside biosynthesis; alpha-ribazole biosynthesis; alpha-ribazole from 5,6-dimethylbenzimidazole: step 1/2.
EC: 2.4.2.21
Catalytic Activity: 5,6-dimethylbenzimidazole + nicotinate beta-D-ribonucleotide = alpha-ribazole 5'-phosphate + H(+) + nicotinate
Sequence Length: 70
Sequence Mass (Da): 7041
|
A0A4Q2ZZ48 | MNLIFLIGMPAAGKTYWGEKMADALNMHFIDLDMYIEQRAGQRISDIFERQGESAFREKETQAVFTIMESVDQPTVVACGGGTPAFNDNLSAMQSAGYVIYLKASIDTLVMNVRRSELNRPLLQGKDIKTTLHELLEKRKKYYEQAHYILDVENLSVATFAQIIARCTDRPS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
EC: 2.7.1.71
S... |
A0A2E8JQN3 | MKKTNLLFLTLLCTAAVGCSTLAPSVDFPDEQKTSSTERKRLEAIQADRAELRSRDAEDAQYAREEAIRASGTSDGSIFNTASYSGLFEDRRARAVGDLLTIDIQENIDSEQQNETSVSRDDDLSITTPEIRGFFNLRPIGGAVNSSKDFNGQGATRANNRVRGRVSVVVTEVLPSGNLRVKGERQIGTNREVESIKFYGIVNPETIRSGNRVSSSEVAEARIEYRGKGAIDSAQAMGWMSRVFLSIMPF | Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Subcellular Location: Cell outer membrane
Sequence Length: 250
Sequence Mass (Da): 27451
Location Topology: Lipid-anchor
|
A0A2G6HKT6 | MITREPFWKEVLGFARKTAINWLNALRQKRYTSSMNTAILQETKLDLPDEKAVYHGKVRDVYDFGDRLMLVATDRYSAFDRVLATVPHKGALLTQTSRWWFEQTTSIVPNHIISYPDPNVAYCRKYDVIPLETVVRGYITGVTNTSLWHTYSGGQRDYGTFVLPDGLKKNDKLPEPVLTPTTKFETHDRNLTPAEAVATGLLDRDVWERVSRIALELFRFGQQKAEAAGLLLVDTKYEFGLTPEGEVVLIDELHTQDSSRYWLRESYAERLAAGEEPENYDKEFLRLWFKARFDPYAQDSEAPVVPDDVIAELERRYRFV... | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
EC: 6.3.2.6
Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(... |
A0A090RPV4 | MGKIKGSHTAMKSGMIAAEAIFEQISAGLAHQEADYQTRFESSWLYKELASTRNFGANLHKFGEPLGGLLNVIEQNWWSRLFKASIPWKVTDSIEDHMMLKTKDSTTPINYQKPDGVLSFDRPSSLFYLAHSMKKPTCHLHLTDPTLVLDTHIPLYNEPSQRYCPAGVYEIVDVEGKRKLQINATNCLHCKTCDIKDPSANIDWTAPEGGGGPSYRGM | 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: 218
Sequence Mass (Da): 24404
|
A0A0P6XV57 | MAKVTNILSIVLKVAVVLTLLTGNLLSLAVAYIVFAPDDLPKPFYLSYSYPGQARNDGAPIASEAPTLALPTPTPHILPGQGVMIDTGAKIINLADPTGRRYIRINVVLEFRPEALPETQSTKAKGESQPTDPNQSLKDDINQKLPLINDVIITLISTKTFDMLYTAEGKEQLRQDIMNGINTRIPEHQVIAVYFSEFVVE | Function: Controls the rotational direction of flagella during chemotaxis.
Subcellular Location: Cell membrane
Sequence Length: 201
Sequence Mass (Da): 22043
Location Topology: Single-pass membrane protein
|
A0A098S4F8 | MQIKVCGLREPENILEVAPLPVDWLGLIFYANSPRAVKPKLAQWLEEQAEALSGKKRVGVFVNAEIEEVLNAVHDFQLDLVQLHGEESPEYCQLIRNLMETTSMRKAKLMKAFQVGDVFDFNRVYPYAAHCAYVLFDTKGKHYGGNGEQFNWELLQQYQGVTPFFLSGGIGPEDAAEVLAFRHPQLFGIDLNSKFETAPGVKGPGLLKPFLETLKNNTL | 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: 219
Sequence Mass (Da): 24614
|
A0FK90 | WAGMVGTALSMLIRAELGQCGSLIGDDQIYNVIVTAHAFIMIFFMVMPILIGGFGNWLLPLMLGAPDMAFPRLNNLSFWLLPPSLTLLLLGSAVESGAGTGWTVYPPLSSTIAHAGASVDLSIFSLHLAGISSILGAVNFITTILNMRSL | 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-cytoc... |
A0A5C5WCW8 | MLLRVTPNGCTALAPAKINLSLEILGRRADGFHELRTVMAPLRWYDSLQVERLAPNQPSEPNPRGTDLQAEGVTGRFVLQQACDPAADIPADASNLVVRALVLLARATGNPLHAAVTLIKRLPSQAGLGGGSSDAAAALVAANRAWRFDLSPEKLTALAAQLGSDVPFFVQVLLGGGRCRAALCEGRGEAIRPTPVAGAIPCVVVKPVRGLSTAEVYAMSNAEEHGERGSSEATLAALRTGEWRHAANLLTNTLQPAALRVAPWLEKLAVLFSRLPVIAHQLSGSGSAYFALCQNWATARRVGAAVRGANLGRVTITSTL | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
EC: 2.7.1.148
Catalytic Activity: 4-CDP-2-C... |
A0A8B7DVU4 | MVLSINCSKFGCMFLLLISRVFAYSVNRTQTHKCRDANIAVESQSSLCYKDESKCDEEICDIEMSQCQAIYRNISGKLRHWFFSCFHHGDQECGTDTCPLHYVPSHDLWYCCCTTSLCNTRIYYPLEPTLNILTENASTTIAAHKNFTTEGSNYLILVYILVPLSVVIVMIGLFACIKWKYKKKEDILLVYERDSSKYEYLNIIHQGQFTKLWLVQHQDQKMVVKLLLPTLQNLWTNEREIFVKYNLKHRNIIKFLAAETENINNKLHYLLVVDYYEKGSLVDYLKKNVITVQQMLKFIFSIVRGLVYLHMPESKKPRIA... | Catalytic Activity: ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-L-threonyl-[receptor-protein]
EC: 2.7.11.30
Subcellular Location: Membrane
Sequence Length: 510
Sequence Mass (Da): 59390
Location Topology: Single-pass type I membrane protein
|
A0A1W0X918 | MQQAENKDTSPASYRSHQRRTSSRDSERSHALPFWMGSEMPWTNSTEAQWETERRCEDLYLEHDVSTDPLESSIALKRKALKKFMLRGFDSLPSSYLTLDSSHPWLCFWILNGLRVLGEDIPVETAQKTISIIRACQTSTGGFGGGPAQAPHLAGTYAACMALCCVGTEEALSVIDRVGLKSFLFQMRQPSGAFTMCEDGEEDTRAVYCAVAVATLLDIPLSPLFDLAPDWLSDCQTYEGGFGAIPGAEAHGGYTYCSFTALYLLNKPTQCRLDDLCRWLSFRQMRYEGGFQGRTNKLVDSCYTFWQGAVFPLLQQVLKD... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins. The beta subunit is responsible for peptide-binding.
EC: 2.5.1.58
Catalytic Activity: (2E,6E)-farnesyl diphosphate + L-cys... |
A0A4S4N1F3 | MSAVSELKTLVKSLQRASTEEETIGILQTLKKEAKITEAVLRESKAGLAVGKLRTHASKNVADLAKEIVKMWKNEVEREKQSHGGKPAAAQSSTSATPAPPAKPPVRKLSMASTNRQSSTPQPATPTNSKADVRNAKSDGVKIGTADSTRDKCAELIYDALASDSGAPIEQILSRAKAIESTILADNVGVTSGYKAKIRSLYVNLKDKNNPSLRESIVTGDLSVAKFCKMTSQEMASEERKAGDNKIREENLFKTLGAEEVQAETDAFQCGRCKQVSVCVFQHLIVPYVTTAIIMDFLHNQLGVVQQQLSFVATEPIDWK... | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: The peptide bond hydrolyzed can be designated -C-|-A-A-X in which C is an S-isoprenylated cysteine residue, A is usually aliphatic and X is the C-terminal residue of the substrate protein, and may be any of several amino acids.
EC: 3.4.24.84
Subcellular Locati... |
A0A5C9A261 | MGAGRSDARRRRSFLRAGSEHHSGDDLPLPGADGGAGGGAGYPGPGEAHPGTELGRANWRRGDPVSTRNPQEAKRRAPRKGGRGATRTVASAPREARQWSLHLSFHWLNRLLILLGGGAVLAAALQGYITLQAIPVERIGVTGKLKHTQTELVQQMVQPALAGGFLNADLGQIREQLEALPWIYEASVRRRWPNSLEIHVIEQLPIARWGQGGFLNHEGVVFQTANADAWNHLPRLEGPEGQQQGMMASYQRLGELLEPLALEVQVLAMDSRGQLSAELSNGIELQLGGDDFRERVQRFGAIYASELAPRADEVARVDLR... | Function: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. May control correct divisome assembly.
Subcellular Location: Cell inner membrane
Sequence Length: 341
Se... |
A0A351F1S7 | DAPYNNPPLREKCLAEGAEYIGGETWLIQQAIHGFKNFTGKWVEREKFAEAIQLATAGNEKGKQPSIALVGPMGAGKTTTGKILAEKLGYEWIDTDQRIESETGMSIEDIFRQKGESYFREIEKKLFSQLVLLSKTVISCGGGIVLDELNRKLLSNHFHTVFLYVKAGQSIKRMGKTTSRPLLTRSNPVQKAYELMQERLPHYLSTSSVIVNTHGGDVQNITELIYEDYRQTFHH | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
EC: 2.7.1.71
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Length: 235
Sequence Mass (Da): 26508
|
A0A346E0M3 | MKKILIINGPNINMLGIREPKKYGKNKLSYINNKIKEKFEKKIKLFFFQSNSEEKIIKKIHKSYKKINYIIINPAGFSYNSYSILDAMLSVDIKYIEVHITNIFSRKDRDRSIFSRNAICIISGMGYMGYISALKFLIKI | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
Function: Catalyzes a trans-dehydration via an enolate intermediate.
EC: 4.2.1.10
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Length: 140
Sequenc... |
A0A8B6XIH5 | MLSKIILSLLLVVATSAKKCSKSCEKISPYPTNFFEDIVPHFVNNRPTVGVVAMEILGQKMLVEVPWSENKDYFGSSFVKLLDAAGARAVPIKEDITKKDLNILLHKINGVIIPGGDADIGDSGYERISKQIINHSKKMAKKNITFPVLGICRGAQMMMIAEADKDFLVETDSLNYSIPLDFTDEARESRLFGHAPQGLFDALGTKAITFNAHKAGIPTVNFYNNTKLMETFRAISTNYDRNGTQFISTFEGRHAPLYGLQWHPEKSLFVFNPVLAVDHSIISIIAAQYISNFFVSETRKNPNSFRDRADEQNHLLLSHY... | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + (n-1) H2O = (6S)-5,6,7,8-tetrahydrofolate + (n-1) L-glutamate
EC: 3.4.19.9
Subcellular Location: Secreted
Sequence Length: 353
Sequence Mass (Da): 39759
|
A0A8B6XET3 | MRGLNCLKLRSGFGSTIWLGLKILVIVLLCLGILHMVLKTKITTNTVVRTRNSADSAYLSSWSCELNKRMLQELQREIEEKDKLLKYRGKVIASLRTLVQDLNATNKVLTNTLTNLTEVLVAKNFSNNLMHENKQKDSFYLRSNEPTPFPPHLRDSVERPSRPCCLALKRMTDILRIYMETTQELREQVAVFQNLNITEQINDLAEQEKKKFAVENCSIYFTNDVKNRTKPEKYSLYQTFSNGYFYETFPWHKLEKQNSKSKSYHRNIDFQRAVNFSLKEILKINKLPSKYFHVENALMKYDEIHGVEYKISFLYNKTRS... | EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 603
Sequence Mass (Da): 70540
Location Topology: Single-pass type II membrane protein
|
K6YYK5 | MPFAQLVTSGIELALNQLLKLDDDSQQRLKKLSGKALQVTIKELPWPLLFSFSEQIDVRTVMTPNNDSEPEPEPVDCLIELNLETLPKLKDSSQLTQLIQKKQLNLIGDIYVAQTFSALLKDLDVDWEEQLSRYTGDVVAHQTFSSMRTIFDTAKTQIEQGVIGLGEYLTKSDSIAVKPSEMIEFSRGVSDLRSSTERLSAKIALLEQAKKVDTGLNN | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Required for ubiquinone (coenzyme Q) biosynthesis. Binds hydrophobic ubiquinone biosynthetic intermediates via its SCP2 domain and is essential for the stability of the Ubi complex. May constitute a docking platform where Ubi enzymes assemble and access... |
A0A4S4MBZ9 | MILSSLQVSPHHNHLVLILNVILDAHETTALPTYYAVLAVPRSASFSEIKSAYHRALLVSHPDKQQQSKETTVSPHDVDVDIDLIKQAYVTLSSAESRATYDVSLVRLPAGPRPAQVVSLEDFEEAEEDGDGWWYGCRCGGRYQITEADMEKGQHVVGCGSCSEVVWVGYELVDAEANEGGS | Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
Function: Required for the first step of diphthamide biosynthesis, the transfer of 3-amino-3-carboxypropyl from S-adenosyl-L-methionine to a histidine residue. Diphthamide is a post-translational modification of histidine which occurs in elongation facto... |
A0A8B6XHF9 | PSQVENLKKFIQILTKHLHDRIPDSEVIWYDSVLSTGQLKWQNKLCSENKVFFDLCDGIFLNYNWSIYDLQHSLFTSGEARKLDVYVGVDVFGRGCFGGGGWNSCKAMQVIREKKLSAAIFAPGWVMENHGEEEFTKNNKKFWELLAVYLYPHFLSELPFVTSFCQGYGAKVFVQGKMLQNKPWTNLSAQSFQPTFSNNLYQLGPKEGMQVDCIEFQTEEAYNGGGCLCIKGLAKPCEEQTRTVLRLFKTDIKLMESTNYSVEFTYKCSSDRVQLFLLVLLEDNPSYIVFNPSKA | Catalytic Activity: an N(4)-(oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein] + H2O = an oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta-D-Man-(1->4)-D-GlcNAc + N(4)-(N-acetyl-beta-D-glucosaminyl)-L-asparaginyl-[protein]
EC: 3.2.1.96
Sub... |
A0A8B6XRN9 | MSCYVVNHCCKTGVSLYLINSQLSFKRYIFITPKNMQQTVAQFVELSKKWFYGVESATPIFLANGKDIQVLTHPEEFYKELLLQSSIANKRISLASLYLGNGEKEEKLIQVICDNLKKKEKPFEVNILLEYTRGSRGAKSSRTVLLPLKKHFGSTSTVALFHTPNLRGILKAIIPPRFDETVNVSHVKAYVFDDTLILSGANLSVDYFTNRQDRYIIFRNNKILCDYFQDLIKTISSFSFALQSSGDVTFALPHIHPYKGSKNGFNKFANKQLCEFTERYKSQYSITDAIKLITQLNTLNSTYDTLIFPLLQMKNMGITT... | Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
Function: Functions in the biosynthesis of the anionic phospholipids phosphatidylglycerol and cardiolipin.
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-diacyl-... |
A0A2N6DFS7 | MKNVLLIFILVMIYSACFASENVHWGYEGHEGPANWGDLSEDFHVCKSGVSQSPINIDTGDVIKVSMEPISFSYKTSGVTLVNNGHTLQANYDRGSYITIKGQKFELLQFHFHSPSENTVNSNYFDMEAHLVHKSAKGELAVVSVLLKGRAENQFLKQFWSAMPDKSGVTRVLNIKFSVMDFLPTNQSYYHFDGSLTTPPCSEGVHWFVLQNPVSVSKKQVEAFTTNIIKHNERPTQPVNARNVLSNPL | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 249
Sequence Mass (Da): 27930
|
A0A1J4WT63 | MKIIFIGFMGAGKSFFSKRLAERLGLERIETDELAIKKSSRNSVKEIITQDGEIKLRELEIEIAKEFQEKDSVVIDTGGGVVLNKIILDYLRKNGVVVFLNSSLEIIEKRLQGDEVRPIWQDKERFRQQYGLRMPLYRQYADVEIDTSGPIFFSPDGKSHKMTSEAEKILEEIIEKIRAYLKK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
EC: 2.7.1.71
S... |
A0A0S8FJZ4 | MIRQRLITALVLAAALLLVLFVIPPTAASVVLALFVCVGVWEWSHLAGLQRAAKQTAFIVAALAWGLAALALAGRGALPFLQWLDVAVWIVALYWMLRFPVPVPSAFAVGSGLLVLPLGWLFLALLLIEWGPAWALFLFLLVAGADVGAFFAGRSFGRNKLAPRVSPGKTWEGVAGGLACAAIVALLGALWFDLPIAPAVALGAGVAGFSILGDLTVSMLKRNVGLKDSGAIFPGHGGVLDRIDSLLAAIPLYMIGFGWISGT | 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: 263
Sequence Mass (... |
A0A841CCK3 | MWLHRAMHAGFYVLLAASAARYVAYHGVDPTVLGVAAVLGAAYPLGVRWTGALPLVLVTWLALVWLAPSFGWCAIPLFFQCLRQLRPRHSVPIAAVLTLAVVFGQVRLADTVEPSLVLGPIGVAVITAAVFFDRRRLIHQAGVLQERQRLAREIHDTLAQGLSSINLLLELGDTRRAAEVAKENLAEARRFVRDLSPLQGRSLEDALRGLCDRVEVHGEPYPLTVQTEVALLRVAQGALANVREHAEAHAVVVTLSYLGDAVTLDVCDDGRGFDPSAVTPGQGRGFGLASIRGRVAELGGTLSVESAPGEGTALAVTVPT | 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 tr... |
A0A7L2JVJ6 | QNMSDAMAILHKLQTGLDVNVKFTGVRVFEYTPECIVFDLLDIPLYHGWLVDPQVADIVKAVGNCSYNQLVEKIISCKQSENSELVSEGSWQELPLXRIKSQVVVLYVNMAYSDCKVCSKCYSGITHYSGLLYLLVTDQGFLTEEKVVWESLHNVDGDGNFCDSEFHLRPPSDPETVYRGQQDQIDQDYLMALSLQQEQQNQEINWEQIPEGISDLELAKKLQEEEDRRASQFYQEQEQAAAQVQQVQGAASPASARQSGSNERKRKEPREKEKEKEKNSCVLL | Function: Hydrolase that can specifically remove 'Lys-48'-linked conjugated ubiquitin from proteins. Has exodeubiquitinase activity and has a preference for long polyubiquitin chains. May play a regulatory role at the level of protein turnover.
EC: 3.4.19.12
Catalytic Activity: Thiol-dependent hydrolysis of ester, thio... |
A0A4Q6AWC5 | KMLPVAASEHGEKYDSMLNVTLVVTGIVFFFTQALLFWFAFKYQSTEKRTSFFYAHNNKLELIWTTIPAIAMASLVAIGLKNWFTMTDEAPANSQVVEIIGKQFNWIIRYPGADDVLGVRDFRKINDANNVLGQDWNDKANMDDIIAENGEMHLIKGRPVKMIIGSRDVIHDVGLPHFRMKMDAVPGIVTTIWFTPKYTTEEMKKISGNPNFVYEISCDQMCGKGHYSMRGTIIVETEAEHQAWLAKQKSYYATMNAPAAAPADSAAQQTDSVKAITMK | Cofactor: Binds a copper A center.
Function: Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
EC: 7.1.1.9
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(... |
C7Q477 | MADVSRLPGPNADFWDWQLRGSCRGTDSDLFFHPEGERGQARTSREEAAKEVCLHCPVCKPCREHALRVHEPYGVWGGMTEEERDESYAREKSAARAAKLAALAAAKNTKPARKPSTKVPVKLQAKPNGAPATAPSNGMTMTRPANAVSAGVRAKAKSKP | PTM: The Fe-S cluster can be nitrosylated by nitric oxide (NO).
Cofactor: Binds 1 [4Fe-4S] cluster per subunit. Following nitrosylation of the [4Fe-4S] cluster binds 1 [4Fe-8(NO)] cluster per subunit.
Function: Acts as a transcriptional regulator. Probably redox-responsive. The apo- but not holo-form probably binds DNA... |
A0A1W0X621 | MSEVYSDLSSYPGQQSASNVSMPEEPAERVNVERFDFARHPLLLGLGDSQSNKAADASTSPMVFCRVCNSKIPLEGYDLDEHFIVKCSQCKEATPIRPAPHGERYVRCVCNCLLICRQSANKVACPRLNCQRIITVVGEGGAGDKNGKGMTATQPPPGTCRITCAHCQQPFIFNIKNNSLVKCPCCGNISAVDDEHHRDQMRKSIMLSVTFFILTVVIIFVNALSNHRFAGDLALNPLLFTRSQWSRFPNWVFKAWKVILALYFISWLVVSLEHFSRDYPQSKTDKWMVYLTHWTYLLFTSYLLVSAINACAHAASCGRY... | Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + phosphate
EC: 3.1.3.78
Subcellular Location: Endosome membrane
Sequence Length: 516
Sequence Mass (Da): 58127
Location Topology: Multi-pass membrane protein
|
A0A6A4THT0 | MRIDACLRVWSAAAALAGAGACPAPSQANVSAAIAAALSSRLSNCCTVRSLHRSDRPLCPVSSVSRESGLHTISQVSKAAADLMSYCEQHARSDPLLVGVPTSENPFKDKKPCIIL | Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Subcellular Location: Cell membrane
Sequ... |
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