ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
H0XXH9 | MRLNVNVTVCATCNYWFYLDHLLLVSIKILMYVHSLCLECTVRSQSRPGQPWGQIQALVDTTPFFQYDTDNSTVKYLGPVGEKVNATKALTELTQTLGEVMQELRMILSDTQLEKNKTRGLPTLQVKVFCQREEERCTGASWQLSISGQTALLFDAMNMNWTVMNAEARRTKEEWEDRGLAEYFRKLSIGDCNHWLREFLQHWETMPKQTDREPVHCPSDHWSA | Function: Acts as a ligand for KLRK1.
Subcellular Location: Cell membrane
Sequence Length: 224
Sequence Mass (Da): 25999
Location Topology: Lipid-anchor
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H0XXQ7 | QVLWRHKGKKPATLGANTQLYDWIPQNDLLGHPKTKAFITHGGMNGVYEAIYHGVPMVGIPLCVDQPDNIARMKAKGAAVEVNLNTMTSADLLRALRTVINDPSYKENAMKLSEIHHDQPVKPLDRAVFWIEFVMRHGGAQHLRAAVHDLSWAQYHSLDVIGFLLAFMAAVMLILTKCCLFCCRK | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 185
Sequence Mass (Da): 20728
Location Topology: Single-pass membrane protein
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A0A2E8SIY1 | KEITPEQAANHPNWKMGTKISIDSATLMNKCLEIIEAAILFKIESDKINAVIHPQSIMHAMVTYIDGSSIAHLSNPSMEVPIANMLRGDNRISINFEELLTSERALEFFPIPNEKESLFEIARDVIEYQGNRGAIFNAINEIAVQQFRDSQISFLDIDRVINGTYSAMSMSKLDSIEEVYFYDKEARIKSLEMIKSLSH | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6.
EC: 1.1.1.267
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH
Sequence Length: 199
Sequence Mas... |
A0A2M9U1G2 | MRTSLKLLVLFAVAVAAALLLRDSSGYFMVVTGDERRTISLAAGLVFIVIAFFLFYLVFRFIGFLMDAPTRVRNWNQRRHTRKDYDLLERGWVELLEGRSSPAEKDLTRLLNRSRDSGRQALASLAAAKAAHNQSRYAERDALLLTAQSKARGNPRMQDAATTIRAEMLLEQGEAKQALALLEPLAKAGGANQDHIQKLLLRGYKQIGNQDKLLQVARALNKKGTIDSFEGQRLIEHAGAAVMQATTRDSWTNTWKSFSSAEKTMPLIALAAAEKAQSAGHPDTAGQILEASLRENIDARLLNAYVQCPAEQVNARLTKA... | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis.
Function: Involved in a late step of protoheme IX synthesis.
Subcellular Location: Cell inner membrane
Sequence Length: 470
Sequence Mass (Da): 51991
Location Topology: Multi-pass membrane protein
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A0A545B607 | MIEILTSAQMRATEQAAIASKSTSAWTMMQMAGHGVAEKICSCWPDLDIATRNGTAARALVLCGPGHNGGDGFLAAVALRARGWMVEVVLAGTVANLPENAARACALWRADNPVHDLDHLDDPAHVRPDVVIDALFGIGVSRPLAPDLYATLSKLRTPDGNGNVPKFVAVDCPSGFDVDRGLFLHPDTGTQNLHCDLCVTFHCPKPGHVLGTDAGLLLEVVDIGLPAPYAARAADIAKTPKRLDHIRLIDPDPSADPDTGFPAWYQHMTRLNSHSHKYARGHAMVLSGGAGQGGAARMCARAALRVGAGLVTLAAPQAAM... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
A0A0F6TMI0 | MIIILKLIFFYFIFLLLGLSMKMLVSESMLNIYTDSPFECGISSNLPSRKSFSLPFFFFTILFLMFDMEIILILVFIFFEINTVFFKFLSVVIFILLISLYLEWNYGSLQWL | 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 of complex I.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NA... |
C0P320 | METSLRLRSGGGLRIHAKEKLPLGHSSLLQAHAELDLHTSPAGVTTPSYLALFVRHFYSQLSANLGAGVQLHNGDDLAYSFRAKKAVLFKPDNGFLGLNLKGRLLTDKELKPTKTTGSVELAWTILDLKQGQDVRLKVGYELCDKDRRTGAVIGTGRCRSTAPRLYILDSLRLT | Function: Voltage-dependent rectifying anion channel that facilitates the translocation between chloroplast and cytoplasm of phosphorylated carbohydrates such as triosephosphate, 3-phosphoglycerate and inorganic phosphate (Pi) depending of ATP to triosephosphate ratio in the plastidial intermembrane space; in high trio... |
A0A642UTQ1 | MTDTASFGVTAPISVANPTPAENAINDALIKELKLRNSFEPESATRRRAEVLGTLQKMAEEFVYRVSKRKNMSEGMARDAGGKIFTFGSYRLGVYGPGSDIDALVVVPRHVSRADFFDEFPKLLNERPELEEMTPVPDAFVPIIKLEYGGISIDLICARLDVSRVPVTLTLEDKNLLRNVDEKDLRSLNGTRVTDEILKLVPKLTVFKHALRCIKMWAQQRAIYGNVSGFPGGVAWAMLVARICQLYPNAVGAVIVDRVFNIYHQWSWPQPVVLKKIEDGPLQVRVWNPTLYAGDRHHLMPVITPSYPSMCATHNIGQST... | Catalytic Activity: ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide
EC: 2.7.7.19
Subcellular Location: Nucleus
Sequence Length: 998
Sequence Mass (Da): 112159
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A0A1D6N1I7 | MNYEGIICCDSDSEEPCGKDIPLKGMEPITSCGPPDISRPFQGTPKLQSSTMGSAKLAMPPRRANENFLEAYEVILILDDREKFGSRSRKVADNICSLSHFAVDVRQLPVGDGIWIARHKEDHTEYVLDFIVERKEVMDLDGSIEDNRYRDQKLRMKKCGLRKLIYLVEGDLNRAPKRVKTACFTTEILDGFDVQRTTGFADTQKRYVDLTRSVIAYYDASFSIVGKASPVCPTYDDFKRKCYDLKKKTVSDIFGCQLMQVPQVTEEAAQAVVELYPTPLLLAKAYSILGGDTSAQEKMLKKKNEMVNAGASRNIFHLIW... | Function: Interacts with EME1 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of st... |
A9EPV7 | MSQEQAAVKSGSPGAEGAPSDAAEDPGEDKPMSFWEHLDELRKRLVRSLLVFFAACVVGWEVREELLHFLTVPFVQAWREQSLAGNPSLHFGAPAAAFVAYFKLSMIGGAAMASPFIFYQLWAFVAPGLYAKEKRYVIPFVLFSTILFVGGGWFGWRAAFPISFGYFLSMAGTVGGDGVTITPTVMMGDYLDFVAQLLLGFGIIFEIPLIVLFLSIAGIVNYIQLILFGRWFVFGAFVLAAVLTPPDITSQLVMAVPMCLLYVLSIGLAYVFGKPPTDAQRAAYKARKEKEVTKG | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes.
Subcellular Location: Cell inner membrane
Sequence Length: 295
Sequence Mass (Da): 32268
Location Topology: Multi-pass membrane p... |
A0A961QFN8 | MDALIGLGGMLVLMALGAPIFVALGVAALVMLGFEGRPLMDAAMTSISGINSTTFLAVPFFVMAATFMQRGGIARIIIDAAEAWVGHFRGGLGLVCVLATTLFAAISGSSVVTAMAMGTFLIPAMVARGYHRPFALGTVGASGTLGILIPPSLSMILYGLIAEQSVPRLFLAGVVPGLIQALILAGVVMIISRRNGYASGTRVSGAEFARRNLRALPALAIPLSVFAGIYSGVTTVTESAGVAAIAAVLIAVLVYREVGWKDVFGMTAEAMKAASAVTFIVMFAMLFAHWITGSGVPTRLVRWAVEIGLEPWQFLIALNL... | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 426
Sequence Mass (Da): 44816
Location Topology: Multi-pass membrane protein
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A0A5C2SD41 | MSRAPSSAAYSVTPWEISFLDPLRQSRNALIILNQPFSFPLLHRVWHSSTWHACADGGANRLHDVLKDHDGKDLRHLYTPDLIKGDLDSLRDDVRTYYSSRGVRIVHDDDQDSTDLMKCIAALVEDEKAERHVEQHTIVILGGLSGRLDQTVHTLSLLHKLRRSRKRIFVITDDNVAWLLDSGEHRINIDHTAFGPTCGLLPVGIDSTILTTTGLRWNLTDRQSSFDSMVSTSNHLVPDEPVVTVKTTRPIWWTMELRPIAAPSRRSIEAHDAAFCLGHDSAS | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine: step 1/1.
EC: 2.7.6.2
Catalytic Activity: ATP + thiamine = AMP + H(+) + thiamine diphosphate
Sequence Length: 283
Sequence Mass (Da): 31850
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A0A1G3ZMV9 | ITGNAALLPAVAAISSGKMLGIANKEALVSGGEWICSLAKKHGVELIPVDSEHSALHQCLRAGKKSEVRKLILTASGGAFRNKSLEELKNVSLEEALTHPNWTMGPKVKVDCATLMNKGLEMIEARFLFGLDPWQIDAVVHPESLVQSMVEFVDGSLVAQIANPDMALPIQYALTFPERKPGTLSPFDFTRHPTFHFYPPDVKKFPCLQLAFSALKEGRSYPCFLNAANEILVERFMEKEIPFMAIPEKLEKLMTSHRSESVLTLEAILSIDSLARELARKI | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6.
EC: 1.1.1.267
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH
Sequence Length: 282
Sequence Mas... |
A0A3B3HAL7 | MASFPALMFFLLFTTFLNSGCESGKVLVYPVDGSHWTNMIKILEVLHSKGHQITIFRSSNSWYISESSPYYTSITIPQEKPQNVESQTYMTTFLRKTLEDRQYQGTLWGLFEFYRNFFNLIQGNQQVVANLAASIIENKTLVKELNQTKYDVFLTDPVFPAGVLLAHHLKLPLVLNVRWILGGDAHYPIAPSPLSYIPVLFSHNTDKMSFFQRVKNVFCKGMLVYLYYYISNPPYQALCDRYFEHNVNVMSLMQGADLWLMRTDFTFDFPRPTMPNIIYIGGFQCKPANPLPADLEDFMQSSGEHGVILMTLGTLLSDLG... | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 532
Sequence Mass (Da): 60909
Location Topology: Single-pass membrane protein
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A0A1G3ZNV4 | MSLELTYYGHPALRSKGRRIESITPEICTLVEQMIDTMYEYDGCGLAAQQVGRSLQLAVIDVMPTIEKRPSKAWKDGKAIDVESLMPLVLINPEIIPLGKQKLLDQEGCLSIPGVYADVLRPSRIKIRYQSLENVTLELETEGLLARAAMHEVDHLHGILFTDHLSPQDLEEHQPLLKKLLRENSVF | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
EC: 3.5.1.88
Catalytic ... |
A0A142BC66 | MNDYTAGAVWPLTSKAPIVTRAMAADPIINSLLDTDLYKYTMQQVMFSCYPDAMGKMSFRCRSGQLNLELDELRAQIDALGDLSLSEDELTWLGSLSFITPEFVSWLRTFRLNPAAVHLAESDGHLDITVTGKWAEITHFEIFILAIVSELHCRRAFQGQPERAGELRLHTKIQQLKAGLGSGDGFNLVDFGTRRRFSRQWQEYVVRTLQRELPSTFAGTSNLHLARTLGLKPVGTMAHEWLQAHQALGETLSDFQRDALLTWLGYYEGQLGVALTDTISMKAFLQDFDRELAMAYVGIRHDSGDPVDWGEQALSHYASL... | PTM: Transiently phosphorylated on a His residue during the reaction cycle. Phosphorylation strongly increases the affinity for substrates and increases the rate of nicotinate D-ribonucleotide production. Dephosphorylation regenerates the low-affinity form of the enzyme, leading to product release.
Pathway: Cofactor bi... |
W6K7D6 | MTDRFATADLNDAHPEKVRRCSLPFIDFGGKNHFCGPIRTIVTMEDTKRAKALFQEPGNGQVIVVDGGGSLNTALLGDIQAAVLRDNGWAGIIIHGAIRDAAEMSGIDIGVKALGSCFIRPRQEGVGAVDVPVAFGHVLFETGQYVYCDPDGILVADAPLI | Function: Catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2-oxoglutarate (HMG) into 2 molecules of pyruvate. Also contains a secondary oxaloacetate (OAA) decarboxylase activity due to the common pyruvate enolate transition state formed following C-C bond cleavage in the retro-aldol and decarboxylation reactions.
EC:... |
A0A2E8PMH2 | MTDTTGIDAGGVSTALGRRARRIALRAAGPLAVAGLAVWAMRDRLAEIEGEALIAALAAAPVAAIVAALILTVLSHVFISGYDVFAARRLGLNLGAGRLLAGGFAAGAVAQTLGFGAVTGSLARWRAHAGAGVGPAEAAALTGMASLGFFTGVAGFLALVTLIDPSAAMDLTGASASGAQSVAALALAGLVAVCAATARRRFRVAGLDLRGPDLGWLVRSVALTAGDLIAAGLALWVLMPMAWAPAPLELIAVFAAALGLGLLTGAPGGAGVFEAALIVAFPTVPAAELAASILMFRVIYHGPTLVAALVLLRRAPRRAA... | Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-lysyl-tRNA(Lys) = 1,2-diacyl-sn-glycero-3-phospho-1'-(3'-O-L-lysyl)-sn-glycerol + tRNA(Lys)
EC: 2.3.2.3
Subcellular Location: Membrane
Sequence Length: 739
Sequence Mass (Da): 77508
Location Topology: Multi-pass membrane protein
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A0A920LAR1 | MAIITKKLLKWYAENGRKLPWRVSPRDAALGQVPDPYKIWISEIMLQQTTVNTAIPYFKKFLKKWDCINSLSRANENDILAFWAGLGYYARARNLLKCAKELNDKLGGKIPNDKKILLGLPGIGEYTASAIRAIAFGESEVVIDANIERVICRLFKIEKPINQSKIEIKKYASQLFPKYHSGDFAQALMDFANAVCKPKKPDCKHCIISNSCLSLKHNVVETIPIKPMKKNKLLKKGYVFFTKIKPNKFLLERRPSEGILGGLLGFPSTRWAVEKNVPTVPFKANWTFTNKLVVHQFTHFKLELEIVTAEVENPKFDPSK... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Adenine glycosylase active on G-A mispairs. MutY also corrects error-prone DNA synthesis past GO lesions which are due to the oxidatively damaged form of guanine: 7,8-dihydro-8-oxoguanine (8-oxo-dGTP).
EC: 3.2.2.31
Catalytic Activity: Hydrolyzes free adenine bases from 7,8-... |
A0A355WL88 | MSLSLPGLGWSPHFQSQLSVDEFDTLTPARISQVHRNAVEVITTTGPHRIHLSAEFLQIGVAIGDWVLLSPMLDEITRLLDRKTLLQRRSAAENASAQLIAANVDTLLIVSSCNADYNPARLERYLALAHQADIEPILVLTKVDTCDDPDAFIAGARLDLPNVQVVAIDATTAAGISLLVGFCGAGKTLALLGSSGVGKSTITNALTDAALETQGIRDDDAKGRHTTTARSMHAIKTGGWLIDTPGMRALRLLDVGEGVDMVFQDVADLVPLCKFNDCAHETEPGCAVQKAIKDGTLDPKRLARWLKLSAEDAHNSRDLA... | Cofactor: Binds 1 zinc ion per subunit.
Function: One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyz... |
A0A3L6EHF7 | MSYTISGGGTAPAAWAWLHGDLELTIHEARGLPNMDLLSTLLRRLCLCPPLAGITPARRRSLSDDDDDSAHAHAHTHPHHHHLRGRLHRRPRRRHEPQPHGHLLLPTSDPYAAVVVAGPHETTVARTYVFRNSEAPRWEASFLLPLAHAATGLEFHVKDADPFGSDLIGVAWLPAAAVLASAAAPIESQWLDLARPDARGPSALGGGSAIRVSAAFVPAAAASRGRSGGGVPAYFPPRRGCDVRLYQDAHVAAGELEGVGGVVPGFLPGRCWEDLCMAVLGAQRLVYVAGWSVHTTVRLTREAMSPEMAAKVAELEELGG... | Function: Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond.
EC: 3.1.4.4
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-sn-glycero-3-phosphate + choline + H(+)
Sequence Length: 869
Sequence Mass (Da): 95599
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A0A961M0J2 | MSDIRAEIAGHERTGDAGFGDYVALLKPRVMSLVVFTAMVGLLVAPVRLHPVEALAAIIFIALGAGASGALNMWWDADIDAVMRRTRRRPIPAGRVAPGEALGFGLTLAGFAVVMLALATNMLAGALLTFTIFFYVVVYSMWLKRATPQNIVIGGLAGAFPPLIGWVAATGSMAVEPWLMVALTFMWTPPHFWALAL | Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o
EC: 2.5.1.141
Subcellular Location: Membrane
Sequence Length: 197
Sequence Mass (Da): 21052
Location Topology: Multi-pass membrane protein
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A0A6P4ANZ3 | MCGILAVLGCLDNSHAKRSRIIELSRRLRHRGPDWSGLHCHEDCYLAHQRLAIVDPTSGDQPLYNEDKTIIVTVNGEIYNHKQLREKLKSHQFRTGSDCEVIAHLYEEHGEDFVDMLDGMFSFVLLDTRNKSFIAARDAIGITPLYIGWGLDGSTWFASEMKALSDDCERFMSFLPGHIYSSKQGALRRWYNPPWYLEQIPSNPYDPIVLRKAFEKAVVKRLMTDVPFGVLLSGGLDSSLVAAVANRHLANTEAAVQWGSQLHTFCIGLKGSPDLKAAREVADYLGTRHHEFNFTVQEGLDALEEVIYHIETYDVTTIRA... | Pathway: Amino-acid biosynthesis.
EC: 6.3.5.4
Catalytic Activity: ATP + H2O + L-aspartate + L-glutamine = AMP + diphosphate + H(+) + L-asparagine + L-glutamate
Sequence Length: 586
Sequence Mass (Da): 66193
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A0A1Y4K426 | MLSKTFKTVRETEKASTTYVAALVGVSLARAPFFVAAACLWARGRKGGVAVNLLVDGGRHPRALLALENGMHFFGRSAGAEGETFGEVVFNTSMVGYQEIVSDPSYAGQIVTLTYPQVGNYGINEKDMQADRLHLAGLVVHDMCYEPSNWQSVESLPNFLASRGVVAIEDVDTRALTIAIREGGAMRAAISTTDLDPESLVARVRASAPIADHNYVADVSCDEPYVVPGQDADGQPRLSVVAYDCGEKRGIARRLSAAGCEVTVVPWDTPVEEALAKDPDGVFFSNGPGDPSSVPSVAEAVRACLGRVPVFGICLGNQVI... | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.
EC: 6.3.5.5
Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
Sequence Length: 472
Sequence Mass (Da): 50788
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A0A1D6ESJ9 | MTLASLARALGRICQQLADCGSAASSAALGKPVVDETVDWRYILARPQFRRLFSNDTLGRSASFMILDYENYYPKGKKEVQKGDGSKKSESKRKSSRFGRLQGVKCVIAGRNLYMRFRCSIGDAMGMNMVSKGVQNVLDYLQADFSDMDVISISGFPMSAGRFLLAIRYSDSMQYSRSNLFGMQYSRKRYFVLEDAALRCFKSAPSSKGEVSWQLSYVSSTNQKYTRGNENVFDAFFCCATCCAGGFFHGVRSISFGVDLQEIRLMGVLQTGRKPSRLCGAALYIAALSHGCNYTKADIVSVVHVCEATLTKRLIEFENT... | Pathway: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3.
EC: 1.11.1.11
Catalytic Activity: H2O2 + L-ascorbate = 2 H2O + L-dehydroascorbate
Sequence Length: 606
Sequence Mass (Da): 67067
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A0A3L6EHP0 | MPPPNNRLCVALAIALVVFSSLHTPAATSAVDGDTLAAGQALAAGDKLVSRNGKFALGFFQFRQNLPGGGGTGTSAAVVVPSPGWYLGVWFNKIPVCTPVWIANRDRPITESELKVAQLRVASTDGNNKLLVVVTSNTNTSADNSIIIVANTTTNGSSVHVVLTDTGNLVLLPQTEALLSSASAPAASSSSSSSSSSSLWQSFDYPTDVGLPGAKIGWTKLAGGRYFSRRFISKKSLVDPSPGSYSISIDTNGFMQLTRNAPSVQYWSWTSGSLGNLVTALTALIDMDPRTKGLLKPGYVATADEVYFTYSITDESASVF... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Membrane
Sequence Length: 879
Sequence Mass (Da): 93546
Location Topology: Single-pass type I membrane protein
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A0A314VT42 | MNCFSGEQDHVPVLISSIIDRLPQIRGVWIDGTFGAGGYTKAILSSGANFVIGIDRDPEVEGHATRILNRNIKKFIFVNDTFSNLCTISKGLGFHEVQGVMLDLGVSSMQIDTPKRGFSFRYDGPLDMRMSKNGVMAEEVVNQFSEFELANIFYKLGEEKKSRQIAREIVRCREKAKISSTLDLAKIIESVIPSNAENRIHPATRCFQALRIYINHELEELEKALHAAQEVLSIGGFLIVISFHSLEDRIVKNFLRNSSVSYPKSNRYYPEFNLPNPTFEIVTRKPIIASKNERKNNPRASSAKCRIAIRNDHNNHLKEE... | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.199
Subcellular Location: Cytoplasm
Sequence Length: 324
Seque... |
A0A965DB40 | LAVEATHDNVLGAATQVILEETRASNDGVAVDIPYTAFSILGSLGQDRVFYRVLVGDETVTGYDDLPLPLQPTGTLSSVFYTANYRGETLRLASGMRQYLIQSKIVNVTVVLGQTQSAKAAIMSQMTPRAIMVGIGFFIIAGVLGILATRLVLRAITTLTDAVGRRGPQDLRPVTRPVPSELKPFVLSINGFIGRLANALTRTETFIGEAAHRIRTPLATLRNSLELALVETDDPVLRQRLQTSIRAVDDSARSASQMLDQAAVSYRTDQGSFQNIVLNDMVCDVAEAFRPSAAMHDIRIFCRLPDQKVVVLGDPIMIET... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell inner membrane
Sequence Length: 425
Sequence Mass (Da): 45824
Location Topology: Multi-pass membrane protein
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A0A4Q0IAJ2 | MNKIINFCIFAALSYSEMKRRTFSPGGIHPPQLKSTAGSRIIAVDAPVSIVLPLGQHIGRGAIPVVGKGDRVEAGQPVAVAGPDGVSAAVHTPFSGRVSAIGQKRDSRGLPVESVSIDVEPGQSVADVDRTLADVGPVGLGDVVKVASDAGIVGLGGAAFPTAFKIGGCEGLAIDTVVINGAECEPVLTCDDAMMRVHPDEIVAGARLIKSAVGATRVIIGVELNKPEAIFRLQEASAAHGDVSVVGLQTKYPQGGERQLVQAVTGRYIAQGCLPMTVGVVVQNVSTARALYRAMAFGEPLVNRIVTVAGEAIGRPGNYL... | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
EC: 7.-.-.-
Subcellular Location: Cell membrane
Sequence Length: 456
Sequence Mass (Da): 47554
Location Topology: Peripheral membrane protein
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A0A2E0UHL1 | MRIISGEFGGRILKSPSKSLPVRPTTDRVKESLFSMLTNLVDFDGMTVCDLFAGTGSLGFEALSRGAAHVTFVERSAQVGRLLRGNTSLLRVENRCKIWNLPTESFLMKCDQSFDLIFADPPYAYEGYPRLLELIAEKQMFNVRGLLIVEHGKAPLPQAPESLKVHETRQYGDTSVTIYKRIPEEGEPI | Function: Specifically methylates the guanine in position 966 of 16S rRNA in the assembled 30S particle.
EC: 2.1.1.171
Catalytic Activity: guanosine(966) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(966) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Length: 189
Sequence Mass (Da): 21151
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A0A1D6H657 | MDDSSVKAEDQTMLLEEGGQAMAAKPAYTSLTSQILRLIFMDQLLLENRLTLRAISEFGGYLLYFYICDRTNLLGESAKNYSRDLFLFLYFLLIIVAAMTSFKDIKQRDEFICVQREIRRQPQHWTDHAKKQLRVMQQLDEDHTLTQLTNAWVDLVLGGSKIQEARLIFQDLSDKYPTTCTILNGKALCSTHMGNFEDAEGLLLESLNKDAKDTKTLANLTVCSLNLGKPTTRYLNQLKLAHPDHALVKRMSSAVESFDRACQAMA | Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. The coatomer complex is required for budding from Golgi me... |
A0A3L6EHM1 | MAADGVVAANAPSPTGWLRAHATFYGGADASGTMGGACGYGNLYSQGYGSRTAALSTVLFQDGASCGQCYKIACDRKTAPTLCKPGVTVTVTATNFCPPNSALPDGGWCNQQRPHFDMAQPAWEKIGRDVATGIIPVIYQSVPCVRRGGVRFMINGHNYFNLVLVTNVGGAGSIKSMAVKSSDSTDWMPMARNWGANWHSMSYLSGKRLSFRITITDDQTLVFNNVVPAGWTFGLTFASNLQFK | Function: Causes loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found.
Subcellular Location: Secreted
Sequence Length: 244
Sequence Mass (Da): 26029
Location Topology: Peripheral membrane protein
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A0A2D6SHM3 | MRIVGICGGYACLGLSFLIFFEIIARKLFNHSLQGVDEIGGYVVAIIGTFGMALAAVERAHTRIDVLLFRLPKKVQAILNLISYIALGIGAAFMGYMGWYTLDESLTFGSVSSSPLQVPLWIPQSLWMAGLIIFGLSALWTAFRGVLALRIGLKEAEDVLAPPTISEEIEEVRK | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 174
Sequence Mass (Da): 19008
Location Topology: Multi-pass membrane protein
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A0A804LRX1 | MLSALFLRNNYLSVGASGALFGLLGSMLSELLMNWTIYSNKATAIITLLFIIALNLAIGILPHVDNFAHIGGFATGFLLGFVLLARPQFSWMESHELPHTNQPPKYKAYKYILWVVALVLLLVGFVISLVMLFKGKNG | EC: 3.4.21.-
Subcellular Location: Membrane
Sequence Length: 138
Sequence Mass (Da): 15213
Location Topology: Multi-pass membrane protein
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A0A1X7PYU2 | MADFRTLDDIGAVKGKRVLVRVDLNVPVQDGAVSDATRIERVTPTILELSDKGAKVVLLAHFGRPKGAPDPAQSLAPIATATASVLGRAVAFADDCIGPSAASAIAALPDGGILLLENTRFHKGEEKNDPDFAAKLAENGDLYVNDAFSAAHRAHASTEGIAKILPAFAGRTMEEELSALEKGLGNPVRPVVAIVGGAKVSTKIDLLMNLVTKVDALVIGGGMANTFLAARGEDVGKSLCEHDLAATAKQIMIEAAATGCAIVLPTDGVVAREFKAGAANETVDVTAVPSDAMILDVGPKTVKAVTDWIDRAATLVWNGP... | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
EC: 2.7.2.3
Subcellular Location: Cytoplasm
Sequence Length: 398
Sequence Mass (Da): 40871
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A0A356CH50 | MVPFEVGKLTGAIGKAGGQTGEFAIEEAKRLSEITVALVEKSLKKNEIPEVERIQDIVEQVLMAAGHYKTAKAYILYRQARSEERRVERIIGVKDDLDLSPNQLKVLQSRYLLKDEEGRVIETPSQLFRRVAKTLAKGEGKKVEDNFYEVMSRLEFLPAGRTLNNAGTPQSQLANCFVLPVLDSIEGIFESVKQMALVHQTGGGTGFNFSKLRPKGDAVTKSSGGFATGPVSFMKVFDIATRQVMQGGKKRGANMGILNVDHPDILXXDYR | Pathway: Genetic information processing; DNA replication.
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
EC: 1.17.4.1
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [... |
A0A1D6KR35 | MAKDYPASPKAQQLQESKKQRLTYILVVSALCIAFYVLGAWQNTTLPKPIGNSAITRVGCDPTAATAQSSGSVPSFGPGSGEVLDFDAHHRLTINNTDGDGELQQFPACPLNFSEYTPCEDRRRGRRFDRNMLVYRERHCPGKDEQVASWGAYLLKRNIIAMSFAPRDTHEAQVQFALERGVPAIIGVMAKQRLPYPSRAFDMAHCSRCLIPWDEHGEYSKDIFQKPKNHLECANIKKTYKTPHICKSDNPDAAWYTQMEACVTPLPEVSNQGEVAGGAVEKWPERAFLVPPRIKRGMIPGLDAKKFDEDKKLWEKRVAY... | EC: 2.1.1.-
Subcellular Location: Membrane
Sequence Length: 484
Sequence Mass (Da): 55048
Location Topology: Single-pass type II membrane protein
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A0A482H1X3 | SFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALTLLLASSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTS | 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... |
A0A4Q0II97 | MTSTDNRQTVSLIAAVGRNNEIGCRGDLAFHIRADLRHFKELTIGKPVVMGRRTFESLPKGALPQRRNIVITTDTGYSAPGIETAASLQQALAMTADAPETMIIGGGMVYSEAMPVASRIYLTEVDASLDEADTFFPEIDRNQWTATSQSDTFTDEPTGLSYRFINLHRL | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
EC: 1.5.1.3
Catalytic Activity: (6S)-5,6,7,8-tet... |
B4YE15 | TSDYAGQVYDQLTPLCPIMLALSAASPIYRGYLADLDTRWRVISQSVDDRTREERGLETLKKDKFVINKSRYDSVDSYLSASICSDIKLVYDKDIYHQLREGGVDDLLAKHIAHMFISESR | Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2.
EC: 6.3.2.2
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Length: 121
Sequence Mass (Da): 13837
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A0A2J9DXX9 | MTKASLWLLPAALLGVTVSAAADPTGSNQFEMSSSGNSSTSTPSFGTSFGMTDKLTTDNRFGSLYTQPRRRQPELDLPDLGSGGGRFIESNQHKAIGEWSLQQLSRSAPLLNDPWSQEQLERMAWQINAQARTQAPLALLLINNASINAFAIPGGLMGIHTGTITESGSMDEVSSVIAHEVAHLSQRHYEHREDASRKALLLQIGGLLAAIAASAADGDAAAAVMMGSQTAALNSQMAFSRSNEREADRIGMQLMAKSGYDPRAMPKFFATLNQKAQLNMSKNAYLPSFIMTHPLSSERLSEAQSRASSYPPVALSEQRD... | Cofactor: Binds 1 zinc ion per subunit.
Function: Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state.
EC: 3.4.-.-
Subcellular Location: Periplasm
Sequence Leng... |
A2WFK1 | MTLLARIKGGLVVSCQALPGEPLHGSDHMCAMARAAAEGGAAGVLANGGDDIARIRACVELPLIGVVTRGYAGSDIALTATMTEIDEIVAAGAQMAGLDATDRRRPDDDTLDAFFSRIRERYPSLLLMAEIATVAEAIRAQEIGFDCISSAAYGYTPDTAGRRLSDHDFAHFSALRAATTRCPLVAEGGIGQPAHAARVLELGADVVVVGSAITRPQSITATYRQAMISVSR | Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 3/5.
Function: Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P).
EC: 5.1.3.9
Catalytic Activity: an N-acyl-D-glucosamine 6-phosphate = an N-acyl-D-... |
A0A642UKM3 | MRPQPIHIYSDRSSVVEIQYSRWSHVRKFVVPLVIPQYVSRDRVDVENCEVHFDGMSKLGQVFWIAGIIRVVVPTIYPQIVDTLAQTVEISTPINSFETLKEAFFYIRNGINLYDGDDITIPPVYVALMQLLDWPYVGSLLYNLLFTAIDLWIAWRMVAINRWYQKHQTRRLGKYAEVKGFNDDLIASFVLFNPLIILTCISHSTLPVQVVLIVESIYQVCVGHSISRSAITLGVASYIGFTPVYLAPSIFALAHALKLEEPARVYVHGIAILTTTIMLLALISATMTGSTQFLTCYKSIIWGDKISPNTGLWWYLFTEM... | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Function: Component of the GPI transamidase complex. May be involved in the recognition of either the GPI attachment signal or the lipid portion of GPI.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 565
Sequence ... |
A0A6P4B186 | MEKKQLHRQIAVMRQSLFDQGYLDEQFVQLEELQDDANPNFVEEVATLYYRDSSRLIHNIEQALEKSPLDFHKLDSYMHQLKGSSSSIGAKKVKAECTQFREYCRTANGEG | Function: Functions as two-component phosphorelay mediators between cytokinin sensor histidine kinases and response regulators (B-type ARRs). Plays an important role in propagating cytokinin signal transduction.
Subcellular Location: Cytoplasm
Sequence Length: 111
Domain: Histidine-containing phosphotransfer domain (HP... |
A0A0F6YKT0 | MLREISLVLHIVGVLLWIGGSASAAWTAAQLALVSSAEQRKEGLLAVRRALLAIVTPGLLLAWAGGLTMFFTALDVYSRAGWMHGKLTIGIVVAALHGVLVARVRKGASGEREVSQGFFGGVAMTIVVLAAVVVALVIFRPGS | 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... |
A0A2P6G357 | MNKIFVSAFFIGFLPFAPGTFGSLLGVLLGFLVQTVSGFPIFMSLTILLFFTGWYASKKYIAKNSVKHKIDDPQEIVIDEIVGQLISYSPISFYIWVSKSDYFYSNFYDWLIAFALFRLFDIFKPWPINLADKIPSALGVMLDDVIAGLYSATIICILLNIN | Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 2/2.
Function: Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG).
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate... |
A0A2D5TF31 | MKAAFPLLHNWLQDSYPAATVTGTVILSAFTTKLAIYALARGFAGTEILIYIGAVMTLFPIFFAEIENDLRKVLAYSLNNQLGFMVVGVGIGTEMALNGTAAHAFVHILYKALLFMTVGAVLFRTGTSKASELGGLYRTMPLTATFCLIGAASISAFPLFSGFIAKSLILSEAAYKHYDYVWLILVFASAGVLSHSGIKIPFFTFFAHDSGKRPAEAPTHMLIAMGISAALCIIIGIVPDVLYSILPYAVDYEPYTVAHVIGQLQLLLFALLAFGILYRIGMHPPEVRATNLDTDWVYRKMAPSVVLTCARGIATIWAHV... | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
B5YGD1 | MKVCEIFTSIQGESSLAGIPMVFVRLTGCNLRCSYCDTKYAYYEGEELSINKVLEKIHSFPFQYVEITGGEPLLQDETYKLINELVKSHNVLIETNGSIPIEKVNPEVKIIMDIKTPGSGMSEKNYIENLRFLKKIDEVKFVLTNRDDYEWAKNFIKNHEIKANEILFSPAYGILNPAELAKWLINDGISVRLNLQIHKYIFGNIRGV | 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... |
S5DPE3 | MAILRLSIIYMKNIKKIYYQGSKGSYSESVLKDYFPNKEYIECQTFREVVVQAGEENYGLLPVENSLVGTVVDSYETLIRSELIVYGEFKKKITHALIGLKNTKFENIERVISHPQALQQCSNFLEEMNAQLQPVFDTAGSVLSLIDEQSNTTAGIAGEHFEGDSRFKILKKNISNHIENYTRFFLVGNKDPNLEVSKNKRSAILIADDKPGSLLSALKIFEETDVNLIKLESRPLIGSPWEYKFYIDYQNANDDIDNQIIDKLELVTKKFKIIGKYGTIDL | Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
EC: 4.2.1.51
Catalytic Activity: H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O
Sequence Length: 282
Sequence Mass (Da): 32156
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A0A963UDB8 | AFVGIRSDGAALLETRPGRGLLGGMLGWPGGDWAASPPDTEPPSDGNWQRAGEARHTFTHFHLLLEVRAARLPQGTIARQGAFVPREAFRPGDLPTVMRKALDVALGAFAAVEGTDDPH | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Adenine glycosylase active on G-A mispairs.
EC: 3.2.2.31
Catalytic Activity: Hydrolyzes free adenine bases from 7,8-dihydro-8-oxoguanine:adenine mismatched double-stranded DNA, leaving an apurinic site.
Sequence Length: 119
Sequence Mass (Da): 12648
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A0A3B8JFW2 | GLVNNIKAAKKLIQRGDPSVWDVLEEVIAGHPVLLNRAPTLHRLGIQSFEPILVEGRAIQLHPLVCPAFNADFDGDQMAVHVPLSLESQAEARLLMLASNNILSPATGRPIVTPSQDMVLGCYYLTARNPAGNKTERYFANLDDALKAYEHKQVELHDYVWVRFDGPVETEVPDNEVISTERLSDGTVAKIYRERRVRETADGELLSQYVLTTPGRIVYNKAIQDALTS | Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
EC: 2.7.7.6
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Length: 229
Sequence Mass (Da): 25455
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A0A848XG13 | MTMVERSKTDRSGKVYVAQGEYAIGAAPEDVISAILGSCVAVCLWDELAQVGGMNHILLPELDKTGSEPVDRSARIGAYAMETLINALIRKGALKGRMGAKVFGGASIVKGLSDIGERNANFAMNYLKAESIGCDAKSLGGSRARQVRFWPFSGQARQRFVPDADIEILAPQPQPGQNTDIEIF | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
EC: 3.5.1.44
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Length: 184
Sequence Mass (Da): 19746
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F4Y5G7 | LLGLCLGAQILTGLFLTMHYCSDITAAFSSVAHICRDVNYGWLIRNMHANGASFFFICIYLHIGRGLYYGSYLYKNTWNVGVVLLLLVMMTAFVGYVLPWGQMSFWGATVITNLLSAVPYIGNSLVQWIWGGFSVDNATLTRFLAFHFLLPFIIVAMTMVHLIFLHETGSNNPTGLNSDADKISFHPYFSYKDLLGFTILLLGLTSLALFVPNLLGDPDNFTPANPLMTPPHMK | 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 membra... |
J4WIB2 | MLEMRDLGQEPKHIVIAGVLRTTLANQRVKRSELGKVRISGEILLG | Function: In vitro catalyzes the addition of water to fumarate, forming malate. Cannot catalyze the reverse reaction. Cannot use the cis-isomer maleate as substrate.
EC: 4.2.1.2
Catalytic Activity: (S)-malate = fumarate + H2O
Sequence Length: 46
Sequence Mass (Da): 5127
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I1PP46 | MATGLSGGAMTSFAVKKPLLAAAVRRRSWPPPSGRALPFSPLTRTPRSRGLGTVTCFVPQGTESQQAPAPPSPPPTVPVPVPSLEEEAAAAAARRIAERKARKLSERRTYLVAAVMSSLGFTSMAVAAVYYRFHWQLEGGDVPMTEMFGTFALSVGAAVGMEFWAQWAHRSLWHASLWHMHESHHRAREGPFELNDVFAITNAVPAISLLAYGFFHRGIVPGLCFGAGLGITLFGMAYMFVHDGLVHRRFPVGPIANVPYFRRVAAAHKIHHTDKFEGVPYGLFLGPKELEEVGGLEELEKELARINRSL | Catalytic Activity: a long-chain fatty aldehyde + H(+) + 2 NADPH + O2 = a long-chain alkane + formate + H2O + 2 NADP(+)
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 310
Sequence Mass (Da): 33878
Location Topology: Multi-pass membrane protein
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A0A963U6L0 | MKVLLTRRSADNTRMAALFASAGLEAVSLPLIELEDTGSVLPGRTHDFSVFTSAAAIEVLSSREERRLCGSPAYAVGPRTAEMLRQEAYLDVRQGPGDAEGLANLIAADFVGRDTVCGIYPCGEARAKDLAAMLEPVSITLDLAEIYRLTECEASRDTMAAALGSTKGGAVAVFSAESGKRLVAQARRLGLENAFETISAAVLSQRVADALGADLFRDVRVAAHPDAESMVELLVDTRQRQES | 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... |
A0A0D2AMG8 | MQHCERNGNRGYRDGTHQKRVDGPDTRREDEGRRHLFWSLTIVCDGCASRFRKDYIQRTPITTSKFYGLEKKDAVLPAPYHGHVILGDSSPILLYQIGTHETRALIDVKDGCRSSPKSRIIPIRITSTACLFPWLAKKPQRTEIASHILFHRGITAAARRSSHLVRVSLRTIGSVCHAICAEGGKALCMSR | Function: Catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, and is considered to be a rate-limiting enzyme in steroid biosynthesis.
Catalytic Activity: O2 + reduced [NADPH--hemoprotein reductase] + squalene = (S)-2,3-epoxysqualene + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
EC: 1.1... |
A0A0D2AAL1 | MAANDYYTSFPPSSQHHDTAYYGSGAITPEYGRTNAPLPPVPATSSPRPYKPPLDSHLPQGGSPFDDRQYPAYPPPTQPEPGSGQHSPPYYGRPGDNASPYASNDPFADNNAIPLQNQGRDYGKNGGVGAALRPFETEQGPIRPDDRRYRRRRRKQGWFTGKITWACYTLFLIQAGVFVGEIVKNSVLTGSPIELHPSFNPMIGPSPYVLINMGARYVPCMKNVDAKITNNATNTVTYTPASSPDIPFQCPNTTTNDGNCHLQDLCGFGMDLTEKDGKTPMPNQWFRFITPIFLHAGIIHIGFNMLLQLTLGRDMELQIG... | EC: 3.4.21.-
Subcellular Location: Membrane
Sequence Length: 543
Sequence Mass (Da): 60253
Location Topology: Multi-pass membrane protein
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A0A142BCM0 | MSVLKDLKFYATQPHACSYLPDRQAITLFMDPATELDSGLYSHLSDIGFRRSGRHIYRPRCNGCNACIPARVAVKQFNRRRTQKKNWNKNQDLVVTAHKAVNDDETYRLYQSYINTQHKDGDMYPASQEQFESFLVQCPDFCTFYKFRLGDELVAVAVTDKLKHGLSAIYTFYSPNHPRRSLGRYCILWQIEQTRKMGFDYLHLGYWIKDCQKMNYKIQYRPLEIYINNRWVTLK | 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] + ... |
A0A7I4YZ00 | MPFRKDFVSQSCSQKRTLLGILLFIAALFAVFGYITDTTWQTHGFFVFHAIVANFNQTANLSTTRPSTISYQSSFLPSPRNNQTVSSLEANFSSLSTVSYQSSPQTILQNSSGSFSVLQSLTGLDNQSAISSTSLPTTTTHHSNSSSTRYSNTTNNYPSCSQRLKFAGRINVSMEEIPLKQLEGKFKYLKPGGHYIPDGCKPLNRVAIIIPFRDRESHLHILLNNMHPFLIEQMLDYLIIVVEQVANQTFNRAKLLNVGYVEANKMYDWQCYIFHDVDLLPEDDRNLHVCPDENPRHMAVAVNKFNYKLYYEEMFGTSTA... | Pathway: Protein modification; protein glycosylation.
Function: Catalyzes the transfer of galactose onto proteins or lipids.
EC: 2.4.1.-
Subcellular Location: Membrane
Sequence Length: 461
Sequence Mass (Da): 52951
Location Topology: Single-pass type II membrane protein
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A0A7I4YBZ4 | MPPPAYMRSGSETSFPSASDSREDSIHVTGLREKRLYAVIGCLVILSILALALLTVNIMIVMSLQMTHHGMRFLRFHTIHDPHTDTTEKIVEFDGNHIDLGTVVTNGQVAGYKDQELNIYGSRLLISGGKNGTRLTIQDNRCRLENTKHFQVIKVISTKTSRPIFSAQHPVVSIDEKIKKLSTAKIVTNKIRSPIDETLKIEAENLSIRGNEGIRMEANSAKFIGATSVIFNTTRDGSIHLRGRLLFDTTRGLPLSPSPALAASIDAFRVCVCGGTQQKLFLTPGNKPCESSNALCT | Function: Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix.
Subcellular Location: Cell membrane
Sequence Length: 297
Sequence Mass (Da): 32614
Location Topology: Single-pass type II membrane protein... |
A0A804P6G5 | EAHRPRNKARTYSSAVGKEGKREQRTLARVWRVVRRRGCSCSSRRRISAPPARSLVSSPVRRGATMAGKGGPTNLEKEQMFGMAEKEMEYRVDLFNRLTKTCFEKCVEKRYKEAELNMGENSCIDRCVSKYWQVTNLVGQMLGNQPQM | 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 me... |
A0A6L5F2V4 | MSGERAVRPWRVALTLFTVIPMAGRAGLDRREAARALLWLPAVGALLGAVAAGVLLAVQAVADGAAGRLLAAVLAIGTVAALTGAL | 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-riba... |
A0A2P6GHU7 | MKISEGSELPXFNLLXKVNXEILEXKYEDLFVGKTVALXGMPGAFTPTCSRQHLPSIIESEKDLKKKGVDIIGILTTNDPHVLNAWGXANNVDXKKIMLLCXPDAKFTEASGXMFSVPQIGLXRRSIRYAMIAKNGIXLSLQIXESRXYCKTSSGEALIKNTNWQD | Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
EC: 1.11.1.27
Catalytic Activity: a hydroperoxide + 2 glutathione = an alcohol + glutat... |
A0A3P9LD26 | MEILKFTTFVLFFFLHFIYLFFLFLLILSQMSTPIRYGDILQWDFEDTFFNLTLKDILFWSWFSRNCGQTLFVFKGDDDVFVNTPKLISYLHEELKKPQYFVPDSFYKGIYPSYAGGGGVVYSGHLARRLHYISKTVHLYPIDDVFVGMCMLRLNALPIHHPAFLTFDFPSTIKEDPCADHTVLLVHKRGPEQLVEMWAELKRTWTQCRDVPLWAPVIKKP | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 221
Sequence Mass (Da): 26036
Location Topology: Single-pass type II membrane protein
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A0A3Q7SVQ8 | MSSAGRGRCDPGASDPPVSSGMKAFGVLVVFASCLMAPAHSSFWQFQRMVKHVTGRSAFFSYYGYGCYCGLGGKGTPMDDTDRCCLAHDCCYGKLKQLGCQPVLNGYQFHIANGTVACKCALGPSVSCLCGLRACECDKQSAYCFRASLPTYEKNFKQLFSSRPRCGRRKLQC | Cofactor: Binds 1 Ca(2+) ion per subunit.
Catalytic Activity: 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate
EC: 3.1.1.4
Subcellular Location: Secreted
Sequence Length: 173
Sequence Mass (Da): 18802
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A0A2E3PR16 | MIVGWLILPLIVSVCLGVVAAQLGINQLIDWEGSVPFFDEALTVNSMLDLQWHIFAMVVLFGGVYAYRDREHVSVDFLAAHFSKRRKGWVDMLCDLFFLLPFCAIVVWFGTKFAYRAYLTGEGSTYGGMIDRWFVKACIPAGFLLLGTAALARILSTAAFLFGPRAADDETRPAQ | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 175
Sequence Mass (Da): 19479
Location Topology: Multi-pass membrane protein
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A0A0D2BAE2 | MTLAEEFRSRNWSIYGQWAGVVSMVLCFALGIANIFNFGTPLLIIFSAICLASSFVILFIEVPFLLRICPTSSKFDDFIRKFSTNYMRAAIYGVMSLVQWLSLIVGTSSLVAAAVFLLITSACYGFAAIRKDEFMSSKTLGGQGVAQMIV | Function: Golgi membrane protein involved in vesicular trafficking.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 150
Sequence Mass (Da): 16497
Location Topology: Multi-pass membrane protein
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A0A0D2DNK9 | MPAKQELGRSAAEVAITYDFVKANEEYLNEGHKPEPSDLTRGPRSYTAVITCIDSRATPEHWYDLRPNEVWSLRNGGGRANDPGLLRSLMILQATSEVKEIRVLHHKNCGSLYYNNQWVHDLVQKNSPSRSGQYSPSAYPHCQSMGTLPFIRRGDKDEKEIIIDSIKQDVEFLRSHPLVKERVKVTGFYQDLSNGLISEVDVP | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 203
Sequence Mass (Da): 23025
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A0A0D1Y2P9 | MHRAEVDSGTLRCRSNSYVINKLLIILLPWRHKPWARKQASFGSSETVQYLPPREDVNSPDAYIPTMGVVTYVLLSVLLAGLRGAFDPALLSSVLTWAFLMIGLEIMILNLAKYFLSINSVSSLLDLISYAGYKFVGINVTILLAEIYNRGGGTGGWFGWAVFLYTYNANAFFLLRSLRYVLLPQDSGAPGVAYGPGVSSRSLKQSRTYALAGYAYLAQFFFMYILSNNV | Function: Has a role in transport between endoplasmic reticulum and Golgi.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 230
Sequence Mass (Da): 25541
Location Topology: Multi-pass membrane protein
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A0A804MDZ5 | MPTCAKHMKRYFPHAPQPHAPNTSISRYSWTTTVVARERTDEEIVSSVVIRDVLSMPMAVSKNPNIAFMFLTPGSLPFDKLWEKFLQGHDGRYSIYINASLSHAYYLYILSLFLLGVKFTVKSDTSVGVAHDAFNTFFSKTGSGKHVPRAIFIDLEPSVIDEVRTGSYRQLFHLEQLISGKEDAANNFARGHYTVGKEIVDLCLDRVRNSDKQMYSSEGRAPFGNCYCLRVAQQRQTNVLIRRQSTIRRRDHLGGLGDGVILDLADSDFAQLRKESYAQVQIGRPILGKGVGLTWEEAKLHMSHPPPGEDSASSIGAVSP... | Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers a... |
A0A520ZNT4 | MTLPLDVMPEVADALSDNRPVVALESTIISHGMPHPRNIETAREIEAAVRAEGAVPATIAVLDGRLKIGIDDAMLARIGDPEARDIVKLSRRDLAGCLAAGGSGATTVATTMIAAHLAGIRVFATGGIGGVHKGAEVSFDISADLHELAETPVLVVCAGAKAILDIPKTLEMLETLGVPVVTYGQSLFPAFWSRHHPDRIATPASASDPHTIARQFEMARNIGFRGGMLVANPIPEADEIPGEVMGPIIARAVAEAEANPDAKGKNATPFLLNRILELTDGRSLDANVALVLNNARLAAKIATELEKAAGNR | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Catalyzes the reversible cleavage of pseudouridine 5'-phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway.
EC: 4.2.1.70
Catalytic Activity: D-ribose 5-phosphate + uracil =... |
A0A1D6LVF1 | MEGRGAEQAPEAAAEVKNPRCFMDVTIGGEMEGRIVVELYASVVPRTAENFRALCTGEKGIGAASGKPLHFKGSCFHRVIKGFMIQGGDTTAGDGTGGESIYGSKFEDENFVLKHERKGMLSMANSGPNTNGSQFFITTTRTPHLDGKHVVFGRVMKGMGVVRSIEHVSVGEADCPTLEVKIVDCGELPEGADDGVVNFFKDGDTYPDWPNDLEEKPAEVSWWMDAVESAKAYGNDNFKKQDYKAALRKYRKALRYLDLCWEKEEIDEGKLYSL | 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: 274
Sequence Mass (Da): 30152
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A0A7S1VUS3 | NGQLYILGDKLARRMGSYTFLDTDEIVEKVTQKSIPEIFEADGEAGFRTVEGQVLDSVHAYVRCVVSTGGGIVIKLDNWSKLQSGIVVWLDVAPEVIVKRLEASQGTENRPLLQEDDPLQKLKDLLEERQNKYSQADVRIEITEDMDETAVCDTVVREIHDFIDDNPPAWKAAKAKAQAEGLDWVQ | 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: 186
Sequence Mass (Da): 20858
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A0A804NWW5 | MVGLSVGSAVGQSSIADEVSSLVPKPKQEFYPTIDEEYVQMEPQTKIDILVATPERLMDHINMTNGFSLEHLQYLVIDETDRMVREAYQSWLPTVIQLTHSISQGVWSVYLKVNAIQDWGRWFYLLH | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 127
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): 14600
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W6K7J9 | MPQFDPTYFSSQAIWLIITFGIFYLLMVKLALPRIGEILDERQSKIDADLKSAEQAKAEAEAAAGSYELVLAEARSEAQANFRVVNAEVSEKAAVQDAALRERLSGEIAEAEGRIDKLKQDAVAKIAGVAAEVSQAVVQRLAGIDVTQKVAEAAVTKVMKERS | 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 membrane
Sequence Length: 163
Sequence Mass (Da): 17636
Location Topology: Single-pass membr... |
A0A2E0UG74 | MAITYNFLTRTEGCIVETQTDTPLKRSRLLYEGRSKRVYETSDPDSVFIEFKTEFQQKNNDNDGPSKAECAARVTEYVFKYLNSFRIPNHFMERRDTSELHVRKMSMIPVAVVVRNFAYGSFCERFGLDEGTELEFPVVELVYKNNQIGYPLVNETHILAFGVSTSTEMKTMQRIATKANAVMRSFMERRGFRLIDMWLEFGRFEGEVLIGDALYPDSFRVQEIKSGDLYDGSLYRLEIGDYREEYTRLHDKLTA | 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-(... |
A0A3L6G0Y4 | MCQGGDFTRGNGTGGESIYGAKFADENFKPRHTEPSMLSMANAGPDTNGSQFFIYTVQTPWLDGKHVVFGKVVDGYTVVDKMEVVSSSQVIMDGWGGDLIKTSVFVTLGKSAA | 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: 113
Sequence Mass (Da): 12076
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A0A2E0BNE7 | MKILITRPLQQSRRFAKALDKQFGESLEICISPVLEIKFFRVEINLKPFDGLIFTSESGVKAFAHLNKKTDKKVYCVGAYTSEVARKSGLSVSHTEKDVGDLKTWLVENDSEKTLLYLCGKHISNNLEMAFEESKITIVSQIIYDQIPRKLLPDAIQFLSDVRPVLVPIFSERSYEILSRQFKSSMKSSRMAICLSSAIANKIRDDDFEKVLISPRPDLESLINLVQEFFQNS | 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... |
A0A642V3N1 | MRVTRATAKRAVTATNTTTIVTKRIRRASTENETSAKPITVKQESNDTRSTTTIKTEEISNTSEPITVKQEFDNVSVIKQEITDQFEAKQETNDTIPIKQESMVKDESTVKQEPPVKEDFTTTSSTSFPSFDSMKTTETCSPKLIDQYNKIVSVRNQIVAPVDTMGCERIPYTVDPTSAPKMFRFQLLVSLMLSSQTKDEVTHAAVATMHQHFPRGLCLESILEASEAEIDTLIGKVGFHRRKANYLKRSAEILRSEHNGDIPKSIEEIVKLPGVGPKMGYLLLQAGWDISSGIGVDVHLHRIANLLGWVSSKTPEATRQ... | 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... |
A0A642UZG5 | MYVLDNPVFRWIWAHVWYFVGFYCSLPVLAYVVLPFFATKKVHKSRPTVSVMVLGDLGHSPRMCYHARSLSKLGHFVNLCGYVESEPFEFVLDDPYIDVHEIMPIRNVHGLPFALFAAEKLVLQSVRLFKMLLELGDSDYYLIQNPPSIPLVLLVVAYIKLLNRNAKLVIDWHNLNWSILNLRYQNDQHWAVKLLKLYEKWVVAKQSDLHLCVTKSMKRVLIDDFQIPKNRIHVVYDRPAEQINPLEDPKATRAKLFEKYRIDAPENSKLVVSSTSFTPDEDFNVLLDALEKLPEDIGPLVVVVTGKGPLKQQFLSRVRD... | Pathway: Protein modification; protein glycosylation.
Function: Participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. Involved in assembling the dolichol-pyrophosphate-GlcNAc(2)-Man(5) intermediate on the cytoplasmic surface of the ER.
EC: 2.4.1.142
Catalytic Activity: GDP-alp... |
A0A2E0ULU5 | MDVSGHLLLGAMWILWCTLHSAFISQTFTRWQERTFPRFSRFSRIAYNLFSLITFGVVYWYYRTLPSPTLWAWPEAWVYLQYLLLAAGGIIILLGAREYNQRYFLGIEQLEGTSTASGKGLKASGILRHLRHPYYTGGIIILAAWGDFTWASIISKAVLIGYLIIGTFIEERKLLDEFGDEYREYMRRTPRFFFRLTKTPAG | Function: Catalyzes the methylation of methanethiol (MeSH) to yield dimethylsulphide (DMS).
Catalytic Activity: methanethiol + S-adenosyl-L-methionine = dimethyl sulfide + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.334
Subcellular Location: Membrane
Sequence Length: 202
Sequence Mass (Da): 23490
Location Topology: Mult... |
A0A7U1BII6 | YTPDYETKDTDILAAFRMTPQPGVPAEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYDIEPVAGQENQYIAFVAYPLDLFEEGSVTNLFPSIVGNVFGFKALRALRLEDLRIPPSYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFVFVAEALFKAQAETGEIKGHYLNATAGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLAFYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHVHAGTVVGKLEGEPGVTLG... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in... |
A0A2A4WYN0 | MAEDESTEKEKPKGSMVTKVLLFGVLPMMTALILVVGGLFVAGVLPGGGDKGGDHSEDDGDGEDEEGDEEDSDEEDDGETQPAVYLPIDPAFVVNFASQGKARFLQITVEVMTRDVTVPDKVILHMPVIRNNLMLLFSNQTYDTVSTLEGKESLREEALEVVQQILEEETGDPGVEAVYFTSFVMQ | Function: Controls the rotational direction of flagella during chemotaxis.
Subcellular Location: Cell inner membrane
Sequence Length: 186
Sequence Mass (Da): 20260
Location Topology: Single-pass membrane protein
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A0A3D3TXY3 | RPRRQLGLDPEAPVLLLLPASRPQELRYLMPPLAQAAALLQQRHPDLQVLLPAGLAQFEAPLAAALHEAGVRHARVIPAAEADGLKTTFCAAADLALGKSGTVNLELALQGVPQVVGYRVSRLTAWVARHVLRFQVDHISPVNLLLKQRLVPELLQDELTAEALLERALPLLTDTPERQAMLEGYARLRTTLGAPGVTERAAKAIFDQVIG | Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
EC: 2.4.1.182
Catalytic Activity: a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydrox... |
I1PBG6 | GRCYRAFACCXSTXATGFTLNRESSVFEENKQLCSRCQVCGQEGSVKVVGLERTERVLPTGTTFTVVGEAYKDRGTVLIKRPRELGRFYVXRRGIDQIISDLKEASTGKDATAAIFAFCGGVLLAFHALL | 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: 130
Sequence Mass (Da): 14225
Location Topology: Multi-... |
A0A1X7PYR6 | MTAGPDPLRRVLVTRPEPGASATARALRLAGFEPIMLPLTEIRPLPAEATDTRVIDAVAVTSANALRHASPELLQELAKRPLYAVGEATAETARNAGFLDVAAGPGDAAGLVRLICDSLKAGAAVAYLCGRLRRPDFEEGLRLHGIRTIPIETYETVPMGIGEDTMNRLATAPFLAVLVHSAEAARALAALAARPTFASSLTNARLVAISRRAAEPAAPLFPGRIAISRVPTDRAMVEALSQLL | 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... |
A0A3L6E8P2 | MPGAGRVAETVASVLWRRAEETGVEGMEAATRVLALILASDGIDDSNKKRVATGLAADAAASTASLARVKHGGSGLEARIDAARLAELLLVNAAGEAKAAATKSSELVRLVGTVDEMGALDRNAVDTSLSCLAAICGLCRVARGEMVRHGAVPAAVRALRALRASTESGASAKALRVLESTVGCAEGRAALCANAEDAIPAVVAKMMKAGRDDAEAAVAVL | Pathway: Protein modification; protein ubiquitination.
Function: Functions as an E3 ubiquitin ligase.
EC: 2.3.2.27
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
S... |
A0A804RAT7 | MINMVKVRHNNVVPTMALGVQQLKKELGRSRKVPFEFDEIHEFLDRFYMSRISIHMLIGQHVALHDPKPEPGVIGLINIRLSPIQVAQAACEDARSVCLREYVSAPDINIYGDPNFTFPGNYGVSHLLERMAFKSTVNRTHLRLVREVEAIGGNVSASASREQMSYTYDALKSYTPEMVEVLIDNVRNPAFLDWEVKEQTHDRLACIVEMKRMQLLSSDKKDSKKPLLVFLHCCLSSCSKTIAVLQVVAAPPTPASAIGFEGYEKHLEISFYEAPVFADPNGRGFLFVYPYKILIKTCGTTKLLLAIPRILELAKELSLP... | Pathway: Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.
Catalytic Activity: H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine
EC: 2.7.11.-
Subcellular Location: Mitochondrion matrix
Sequence Length: ... |
A0A2T7H994 | MKLKSLMLGVAAAAAATTAQAADLPVAPEPVDYVRVCDAYGARFYYIPGTETCLRVGGRVRTQIVANNVLEDGNWSDRDSDGYSWLARGYLFLDARTATEFGTLRAYVSMYGDSSNGDASGFTMDNAYIQWGGL | Function: Forms passive diffusion pores that allow small molecular weight hydrophilic materials across the outer membrane.
Subcellular Location: Cell outer membrane
Sequence Length: 134
Domain: Consists of 16-stranded beta-barrel sheets, with large surface-exposed loops, that form a transmembrane pore at the center of ... |
A0A6N9B702 | MKFFLKSFTCLFAILALVLPVSSFETSGKTILVGDFDTGLILVEKNIDTPFPPASLSKLMTLYLVFEALEDNQLKLDDRLLVSDFAYRSYRGGSTMYLDTTDRPTVEELIRGVVVLSGNDACVVLAEALSPTGNEKGFVQLMNEKAKELGLTNSIFANSNGWPDPEQKMSSRDLYILTRKLISDFPEYYEYFAEKEFPFDNRTPANRFNRNPLLKKDVVGADGLKTGYTSDAGYGLVGSAIRDGRRMIFVINGLPSSKQRSDEGEAIIEWYYRQFRQVTLIEKEQEITVAPVWLGSAKEVRLGLAEELSVLIPVANKDNL... | 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... |
A0A1F4CBG6 | MSLGRLARLLDRAASRISGFLHALGGITLVLLMLLTAADVGMRYFLNRPISGAYELSMFMMAIIVAFGIGYCATRDEHVKVEILVGALPPRARAVVDSITWFLSMVLLALLTWQAALYSKTVFHDGTTSPDLLIPTFPFMGVVAVGSAVLCIVFLAQFIDALSRSLTGESK | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 171
Sequence Mass (Da): 18497
Location Topology: Multi-pass membrane protein
|
A0A7S1UZX7 | VLYNSACCVGWAVVLAATVKSLVENVPNVGFVEALASVYESEGVGTVLAYTQSAAMMEIVHSAVGFVRSPLLVTAMQVMSRIVALVGVVYSPEAKVQWGAGLMILSWSMVEVPRYLFYVFAILTGDATKKTPYALFW | Pathway: Lipid metabolism; fatty acid biosynthesis.
EC: 4.2.1.134
Subcellular Location: Membrane
Sequence Length: 137
Sequence Mass (Da): 14773
Location Topology: Multi-pass membrane protein
|
A0A943NME1 | ASKENIVLIGMPGVGKTSTGEALAKLLNRPWIDTDFLIKQKAHCKASTYLQTHGEAAFRHLEHEVIQEISSMSGAVISCGGGVVVTPSNYQLLRQNGKLVYLTRPLEDLAIAGRPLSERMGVQNLAAVRIPLYEAWADVTFSCLCSPDADAKGLLDTL | 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... |
A0A804PZ10 | MQSLGTTEEDLIDRMNFIDDRMNSRAASTPPACTKCAQCHTVERGGAHRQGPNLHGLFGRQSDTTLGYAYSTANKNMVVV | PTM: Binds 1 heme group per subunit.
Function: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrie... |
A0A804PQT5 | MWLLAMVLSSPCLVLIDHGHFQCNCISLGLTLGAIAGVLSRNKLVTATLFTLAIIHKQELELLSDGANVYKLIGPVLVKQDLVEAKANVKKRIEYISAELKRMDRALKDLEEKQNNKKESLLHICNSPFVAADQLGYDDGADTFYADEYGCWSPAGAAGAHRRSFSLSNAEATASWRPYMYYARGYCKNGSSCRFFHGVPEDDAAEREMAGT | Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 212
Sequence Mass (Da): 23399
Location Topology: Multi-pass membrane protein
|
A0A5P8DJ16 | TMYFIFGAFSGMIGTSLSLLIRMELGHPGNFIGNDQIFNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLMLLLQGSMSDIGAGTGWTVYPPLSSIIGHNGISVDLTIXSLHLAGISSIL | 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... |
A0A517VIC6 | MNLSRIILGSRSPRRKELLTQLLPETQIEVVPPADPEEAGFEQLHEWDAIQQQLISICTAKNEDVFQQRPADASVPILTADTIGVVKRETGDLVVLGQPPVESAWQETVKEWFLNDYAGRTHLVLTGVCLRYQQRVTIQIAETEVTFHDQEYVRERLDWYLSTQESRGKAGGYAIQGAGSIFVNRIEGSLSNVVGLPLETVFEMLNRSQTV | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + UTP = diphosphate + H(+) + UMP
EC: 3.6.1.9
Subcellular Location: Cytoplasm
Seque... |
A0A804NTX5 | MAGRYHQDQGGDGGASMEVVSTPNQELALTNCAYVSPADLRRFPNGLALVADAWVFTLRDHNAVASGRIALNAIQRRQAKVSAGDSVTVSSFVPPDDFKLALLTLDLDYAKARANRNDELDAVVLAQQLRKRFLNQVMTSGQRVPFEFYGTNYVFTVNQALLEGQESSTPLDRGFLSSDTYIIFEAAPNSGIKVINQKEAASSKLFKHKEFNLEKLGIGGLSAEFTDIFRRAFASRVFPPHVVSKLGIKHVKGILLYGPPGTGKTLMARQIGKLLNGKDPKIVNGPEVLSKFVGETEKNVRDLFADAENEQRTRGDQSDL... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo p... |
A0A554LPY7 | MKSIAEVDVENKAVFLRVDWNLPLKDGKIVDDNRIKSTLPTINYLRKKNCRIIIGTHLGRPEGKIVHELSTKILAKKLLELLPETNILQTDFVVEPEVKKFVENLETKEILILGNLRWHREEEENNPKFAKILASYADIFVNDAFAVSHRAHASVEAITKYLPSYAGVLLEKEVVSLSVLTENPRHPFILILGGAKIKDKIGLIEKFAPVCDKILVGGCLAITLQYSRGKKVSKSKFESNVSDIAKRIFKVAGKKLILPVDQKIKKIGKKDFSIMDIGDKTLLLFKKEIRNAKTIFWNGNVGYSESKKFESGTLGIARAV... | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
EC: 2.7.2.3
Subcellular Location: Cytoplasm
Sequence Length: 376
Sequence Mass (Da): 41930
|
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