ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A7V8SWA7 | DASRPMRGEPLLPAGRLREPLSAMSRANVVVFTRTEVVPGAPEAIEKLSHFPVFAATTRLLGFRRHGGGMQLESATGISAGPFFAFCGIGNPEAFFGDLETWGLAICGRAVFADHHRYTEQDVLRIKKAGTDGGAKAFITTEKDAMNLSGLKFEGVPLFTAVIDMAVSPEADFLNVLDRLLARKMGAAA | Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form te... |
D7G294 | MERDRPLKGKGGGKRGKGRGGGGGRGRGGRPKSSQGRGHGHRHHAQGDSWRRNGGAAREMIDRERDESGELAQSITVSLRMWDFEQCDVKKCTGRKLCRLGLVREMELGAPFSGLVLSPNGELTVSPADREVVETLGMSVIDCSWARLDEIPFHQMRRGHHRLLPFLVAANPVNYGKPMKLTCAEAIAATLYIVGHQDEAVKVMDQFGWGAEFLRVNEDVLETYAACADGAEVVKAQAAFLARCEEEANSRRDAVSMEDMMPPSYSDEEEYGNHGSENGSENGSENGSSEGVTERGKFCDALLMPAAVLVASVLLFFLIP... | Function: Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine in 18S rRNA. It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi).
EC: 2.5.1.-
Catalytic Activity: an N(1)-methylpseudouridine in 16S/18S... |
A0A2C6KU51 | MAPSRLGRLPPVIPSLLPPLGLRSRGEVKRRWESGRVFLRRIFHAARRQVASSEASTSDLPVHPSLQTCFSEEFPQSRSSYHPHRHHTIPRCLFLSAPLPSIVSSCSFVIDTRCNYVGTSAFSSLSSCANSSLQYIQCASLHQDAYHNDRKDQPSSAMFSARLSFHSEVSSSCPIYRFQSVQSHASSASSSSPSSPCSASSFSFHEPRQSYHRIGAAQVGAPFSSLLLSLCSPRTPKLSSSTPSCLLYSYISDLGFSSASSIPQLGQLTPTHPSSKGEKEESHATVSPNQRHKNAEGQGHGEGGGEGGENKRETRRKLRF... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 728
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): 80773
|
A0A3P7IH62 | MLNIPFLSRFIQKTVKRQKVADSVDYLNYYVTSILLSFFALAISAKQYFGSPIQCWVPSEFRVCRCEEEAFTRCLTSEAEANSI | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 84
Sequence Mass (Da): 9684
Location Topology: Multi-pass membrane protein
|
A0A6A4YVT0 | SYLVHGAALWAAHIPIVPLAPVYTDLYTATASALCRTTNAVQEAPAICLLCGDVVCGGAECCKRNHRGACAQHVTTCGCGQGAFFLMRQCQMLLVSTGGRSCFFASPFVDEFGEEDHNVRRGRPLFLRPNRYMALLQLVFSHAIASEVSKSRRTSEQYIRAYFY | Pathway: Protein modification; protein ubiquitination.
Function: Ubiquitin ligase protein which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation.
... |
K0C8U7 | MQSNEKTVLVTRPAHQSDHLCGLLTAAGFTPIRYPTIAIQAVENTAHISNTLYQHSNYDYLIFISANAVIQADRLIDHQWQKTPSGMIAIGPKTADTLDQLGLKPAITAAKPFNSERLLTQLPSDLKQKKGLIIKGKGGRTLLAEQLQKRGMTVDTLDVYQRTLPNNYKTSHNKKPAYITITSQLALDNLFLIPPRPIGELKQQCTFVVFSERLARYASSLDCQHLLISHGASDKGLVSAINQDKKR | 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... |
A0A484BHT2 | MKHRKPYNLRNIILIYNICQMIYNGSIFLMAFYYLLIDGTYDITCMHTLSLDHPKKSIERWITYIFFMNKIFDLLDTIFFVLRKSYKQITVLHVYHHAMMVYFMYWVTRLYGAGGQYAVMGLCNTTVHFLMYFYYFNAGLRPKMKMNLCNTTADPETKEFPILDSAWPSTLICLGYLLFALKLGPIYMKNRQPYNVKPLMLIYNIVQVIYNGIMFSFGVYRVIINPAYDNKCMETLPLDHPLKPTERLAAYIFFLNKLLDLVDTVFFVLRKSYKQITVLHLYHHVIMVYGTYWVLRMYGTGGQYAMMGFFNSFVHTVMYS... | Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
EC: 2.3.1.199
Subcellular Location: Membrane
Sequence Length: 404
Sequence Mass (Da): 47943
Location Topology: Multi-pass membrane protein
|
E0SA59 | MNNDLLLGQILRVPPITRCMVLLITMVSLLVYVDAVSPYSLYYSPLFLRKFEVWRIFTSFLYFGKPTLDMFMHVVFLYRYSRMLEEGCINTSEYFWLVLVISSTLFAISNIYGISALGTSFSSTITYIWTKRNPRAIVQIFGFISFPAFYLPFILPGFMLLTRRSISIDDVLGIVVGHLFHYFKDIYPRWGRDILKTPCWVKKLFKEHPSGCCKTQKGITIREGREKYKRNIENGNFAKTDENNEVGLIDATDPEINKVDDEYVGEESPSQSCTESLREKDLSIAFSQRPSIVSSTVMTSSIGPEENCLGVVEACSSKEP... | Function: May be involved in the degradation of misfolded endoplasmic reticulum (ER) luminal proteins.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 347
Sequence Mass (Da): 39606
Location Topology: Multi-pass membrane protein
|
A0A2C6KTZ9 | MEVLVRFKGARHKISLPSDATLGDLKHEISVVTDLPSQQQSLKTGYPPRLILLPSSQTDESSTKLRDVGIESKDVVIVEQQTSSSLHQPLSPPQSKSSHLGNSNSKTSSSSSSMPSTSDCRQGVTAPKDLSSRSSLERSSPSSSQASSHMTSASSSFSGSTANQGEKLSSSSSSTSRSPPPPPSTTASSTGAATSSSSSLMYGGKSSCFPPQSSSTSRSSSSSSSSSGKTREIEGDRSDSKGARLTMTNPSSSSSTRSQGNSAMNMDADGTRGSVYTPSSAGDPSSGRHSSYSSANPHFSSKGRSGREEDDEDEEDDEDD... | Function: Hydrolase that can remove conjugated ubiquitin from proteins and may therefore play an important regulatory role at the level of protein turnover by preventing degradation.
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of u... |
A0A1X0RGW5 | MSREDWVDCYRNKTVLITGATGFVGKAILWHLLKTVGGVIDKVYVLIRPKRIPGGSPSQRLLDEIINTSAFKRLMDKKLLGREKLIPISYDLTLSQLGLSMEESMQMKDTNIVIHCAATSEYESSLEWNLEVYINTKCFVLSILKILLDKCVGNNKINGLPQCMLKYK | Function: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
EC: 1.2.1.84
Catalytic Activity: a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain primary fatty alcohol + CoA + 2 NADP(+)
Sequence Length: 168
Sequence Mass (Da): 19041
|
A0A8K0H3V7 | MTHTSPQPTPTLDHQAFIFTVIANGIQARGIPPLLLGKDVLGAARTGSGKTLAFLIPAVELLYHARFTPRNGTGVVVICPTRELAIQTHAVAKDLLKYHSQTLGIAIGGANRRGEAERIAKGVNLLVATPGRLIDHLKATKGFIIKI | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 147
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): 15657
|
A0A336N0L3 | SVLEYQNQAKLLFRKLTPQSPKRCSIETGPYLFHYIIENDVCYLVLCDRQFSKKLAYSFLEEISQEFDNTYGRRVNSVTRPYAFIEFDIFIQKARKGLSDRRRNINSINTQLQDVQRIMVKLHHISKKTYFSYEISSQVQNIDDVLARGAVLSELDTKTQNLSMLSAKYKKDATYLNRKSMYVKAAAGLIVFLVFIFYFWVL | Function: SNARE involved in targeting and fusion of ER-derived transport vesicles with the Golgi complex as well as Golgi-derived retrograde transport vesicles with the ER.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 202
Sequence Mass (Da): 23733
Location Topology: Single-pass type IV membrane... |
A0A7V8T000 | MFMLLAAGAMAQVPAAQPPAGSVAATSLDSGLYAIFNTSMGTITAKLYEEEAPITVRNFVGLARGTKPWKDPRTGDMAAKPLYNNITFHRVIPNFMIQTGDPTATGSHDCGIKIKDEIVPSLKFDRAGRLAMANTGRPNSGGCQFFITEVPYPSLDPPQGAYTIFGQVV | 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: 169
Sequence Mass (Da): 18040
|
A0A2E6GZ59 | MKIAVLGCGNLATAVVSKLEGFEFHTYTPSYIRAEELAKLKNGTAYKELKNIPLTDFVILGMKPQQFEEFAKVYKDFFDDSSVVISLLAGTSTDTIKKALGAKSVARVMSNTPAIIGKGLHALYFSNVDQSSVVESMFKVSGETIVLDSEDKIDGITHFSGSGPAYLFDLARILTSELEKRGLTNEQANMAIKQTLLGSAELLKNSELPAIELRKQVTSKAGVTEKVLESLWDFGIDNAYEKALIAGDERIAQLKGII | Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1.
Function: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Catalytic Activity: L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADH
EC: 1.5.1.2
Subcellular Location: Cytoplasm... |
A0A1F3SIV4 | MFLVIIFSLSAFLAVAGALSVTFSKNLIHACVYLLFSLVGVAGLYLTLGAEFVAATQLVVYVGGVVVLLLFAIMLTGGTNLHHVTSRFGLESTPLMGNLRTYLMGVVTAVLLVVVLCNVLQGSMTGALVSENKFSSTVEQIGVKLLTDHILAFEISSVLLLGALVGAAIIARPHRSSESEN | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy i... |
A0A8K0DTM4 | MDDDSNLEFELEAFPSISREAATEVAACVKVNMVIIMLQLFRDLTVMGTVLSLYTLIHSERQPLHKGLEDHFQCKEVKSASAGLTAAALLAMVPSYISRYVAGSYDNEVVAIFALTFTFYLYIKFALGEATPLLLILFQCMSFYAL | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: a dolichyl diphosphooligosaccharide + L-asparaginyl-[protein] = a dolichyl diphosphate + H(+) + N(4)-(oligosaccharide-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl)-L-asparaginy-[protein]
EC: 2.4.99.18
Subcellular Locati... |
D8LEW5 | MQDMFREFSEELGSPENAGKNKAEIEDIFSYTSVGHKHIVRNVPSEDRIAIHQAVVPTIDDKDRKDLDIDSIDTTPFAMFGVFDGHGGPACAEFLTQSVSTVLAHSPVLYDEDLTPTQRRTFATADSFEELEKVHNKWADEIGDLSGSTAILSTFQDGVLVMAGVGDSAGLYVDHMGKQHNLCPQHSTSNEKEVERVLSMGGTIVNNRVAGCLMPTRTIGDLDCKRALGAIVSPHPEITLAAIYAPPDDGEPHDEPFLVLASDGLWDVLSFAEVAFITRKGLRNLRAHEKQERAKAEKAAAKAAQAAAADGLGGGGGHST... | Function: Enzyme with a broad specificity.
Subcellular Location: Membrane
Sequence Length: 552
Sequence Mass (Da): 58575
Location Topology: Peripheral membrane protein
|
A0A3P7I6C5 | MMRRTLIRYLVLTQAMVFRDVAAGVRRRFPTMNHLVTAGLMTEKELERFNSIKTKNAKYWVPMHWLFSLIRVAKEEGKIPGEVVYVDLMEVYLKITKVQFEKIRQFRVQILSLTLFDWVPVPLVYTQVVHLAVRSYFAIALFGRQYLQPHPDRDLNIDSAKTRIPGNFFTTGNASALPPSSEPGKSNNLVNQFGRQRHNSR | Function: Forms chloride channels.
Subcellular Location: Cell membrane
Sequence Length: 201
Sequence Mass (Da): 23353
Location Topology: Multi-pass membrane protein
|
A0A8K0MSC4 | MASSSHERRRKVSYFYEPQIAHYFYGPDHPMKPIRIQMAHHLISRYELLPHMEVYRPLSITKEDLCAFHAENYVDFLSTASLETPARVLGQFGMGTGDCPPFPGLFDFCTASAGGSIGGAVKLNNAESDIAINWAGGLHHGKRCSASGFCYVNDIVLAILELLKVYGRVLYVDVDVHHGDGVEEAFYHTDRVMTVSFHQFEERFFPGSGYINQTGVGCGKDYAINVPLAQGINDECFVDLFLSIMSKVMEVYKPEAVVLQSGADSLAGDVLGAFNLTTKGHAECLRFLRSYNIPLLLLGGGGYNIGNVARCWCYETAVAL... | Catalytic Activity: H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]
EC: 3.5.1.98
Subcellular Location: Nucleus
Sequence Length: 469
Sequence Mass (Da): 52495
|
A0A4V1XEE7 | MEFRRSSPVLDFFSRQTVFLTGSTGGLGGCLLYKLVVTLGVAKVFALVRGDAATAKRKWAASMGKSKSEDILGTGKIVFIPGDITKPSLGMFPEHCAEVQDSVSLIIHAAADINFRDPLPVLVANNTSSTLELASMARDFKKLHLFVHVSTAYVNSFLEDSEVAEEVYRVGDPEKEIADITAGRGSGRVEAYPWPYGYSKHLTEQLLTLKFPRMPLLIVRPSSIGPAAQVPFPQYMPAASSPLSNFYARLLFPTGGINTFPPCRGSASGTNVLDEIPVDLVANILLQHTYRRTMGVVHASSSLYVPKILDDYLADARRHA... | Function: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
EC: 1.2.1.84
Catalytic Activity: a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain primary fatty alcohol + CoA + 2 NADP(+)
Sequence Length: 412
Sequence Mass (Da): 45508
|
A0A8K0DKV3 | MDVTLTNLRKYFPFLPHNALIKIYKARCARLRLLMDKGMPGDIHWIIEAKVRLAGESSDSIVSYMPRMGKSSYSKRRRAKECKFVTNVPMDLQWRCRSLGMVSINREDKINFIKDESKESLDDILLTLETHPCGVVHRELLNLWHLFKDEQHRHSLGNLTLNDPACQFIRKLDGKHILTHRRRLADSDSGKDKEFLKASTHPSTREKDSFSIWGGSLGLMGTVSLAAHVEGSKVLNIIPKALTATNITGMTVGTEIQVSTMHERISKMLEKSDAFIALPWGYDTLEEIFQMLSCPNEHPS | Function: Cytokinin-activating enzyme working in the direct activation pathway. Phosphoribohydrolase that converts inactive cytokinin nucleotides to the biologically active free-base forms.
EC: 3.2.2.n1
Catalytic Activity: 9-ribosyl-trans-zeatin 5'-phosphate + H2O = D-ribose 5-phosphate + trans-zeatin
Sequence Length: ... |
A0A7V8NTW3 | IGTLLARQLAWRFVDLDERIEEAAGLSIPQIFERFGEPFFRQLEAGQLRAALGRASELKQGTVLALGGGTYAQSGCPEFLRSAGVPVLWLDAPMEVLLARCMTMTGRPLFRDEASFRALHAERLPSYRLADYRVESSGEPVDIVADILRLGVVASGGNQTHLMVEKPLP | 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... |
N1USV6 | MWFKPVMFGLMIIGLLWIIVFYITEAQWPIAAAGSWNILIGFGIAIVGFMMTTRWRS | Function: Involved in cell division.
Subcellular Location: Cell membrane
Sequence Length: 57
Sequence Mass (Da): 6567
Location Topology: Multi-pass membrane protein
|
A0A3P7J5A6 | MLTNSNPYIDFPRPTLHKTVAIGGITVSADLRRNRLPEKWDTILNERNHTVLVSFGSVAKAVYMPDKYKKTLLKVFESMPDTTFIMKYEEEKDTWADHLSNVHLDVWLPQHALLGK | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 116
Sequence Mass (Da): 13396
Location Topology: Single-pass membrane protein
|
B3M840 | MVLGFLLRGSAVAGVVYYTQSVGIWGSTDKTDKLYNNVKSELCPYVQKAKKQLPFEVPQLPKSGEIRFLAKHYYNEGVKSSFRFVHMLPCYAGRGLKKIKDTFEDFAKSPAITGGETGAAK | Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane.
Subcellular Location: Membrane
Sequence Length: 121
Sequence Mass (Da)... |
D7G8E8 | MVRLEGRWASAGSTEPNVGIYSIAGEKAHDPLWKNQDAGLVIAPFDRREGQALFAIFDGHGKNGGQASRECMERLPKHLASASSQSGSPASALRRSCQRLHHDLATGVAGDCGRSGTTLCAAVLAGRRLTVANVGDSGCLRLSRSTAAASSGSSASPSAAAAAIPGKAALASDRGTPDVVDKAGGARGGGTSNRRRLRTAEKLIAGAAAGEEAAPGGGSRGGGLVTERLSRDHKPESKGELERIRAAGGIVFPLPRSGSGGGSGAGGVTGGAPPTAEGSKKGLKTAARGIAAGIPRVWTASGDGPGLAMSRSIGDKMAHS... | Function: Enzyme with a broad specificity.
Subcellular Location: Membrane
Sequence Length: 412
Sequence Mass (Da): 42422
Location Topology: Peripheral membrane protein
|
A0A365TWC2 | MEMPKIARYAGTLAGLVSGVLLLATALLTLADVVGRNFLNAPVPGATELTELALVAITFLLYPRVAWRDTHISVDLLDGIMGPRAKWLQRLLAALIGVAAFGVLAWRLWLLGDRITGYGDVTPYLRIQLGRVYYGMSVLSGVTAIVYALRVALIIVIPRRLPELTGTPSKGIE | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 173
Sequence Mass (Da): 18709
Location Topology: Multi-pass membrane protein
|
A0A7S1CVY9 | QHARKDSKKDAASAVEEPESDAEEALATITPGDADEWELFHFSGGLSEYVKHINRDRISAHEPIFFSRTDGDIQVDVSLQWCSDAFSDTLIGFVNSIKTIDGGTHMDGFKSALTRTVNSLGRKTKALKDNDPNLSGDHIREGLGAVVSVKVPAPEFEGQTKTRLGNPEVRKIVDNAVSTCVAEALEEQPNILNSVLSKALQAYKAAEAAKKARDLVRRKSVLTKSTLPGKLADCSSSLKDECEIFLVEGDSAGGSAKQARDRRFQAILPLRGKILNAERHDDAKLYKNNEISSLIVGLGLGLKGEDLDSLRYGKIIILTD... | Function: Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks.
EC: 5.6.2.2
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Length: 462
Sequence Mass (Da): 51078
|
A0A559MF56 | MRHFTITSGLLACAAAVLGHSTFQEMRVDGYVFDVSTLTVPFINSTNSVDEVSTCARLPLNNNPVTSVTSNDLRCNAGTTPVSLLRTVAAGGNVTVEMHDQPGDLG | Function: Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds. Involved in the degradation of complex natural cellulosic substrates.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
EC: 3.2.1.4
Subcellular Location: Secre... |
A0A2C6KTV2 | MMPNPPLPSSSSSLSSPPLPSSHLLSFSKTSPQKVLSSSSSSAAMALKKKAISLVVAMTPKRGIGRQQDLPWPRLSRDFKHFTQLTTRTHQDLFPSSSSSFSSFTYHQRKEEEQEGEKKKQKKIDGDHLSSSSSSSSCLAECDVGNSSFNAVLMGRKTWESIPAKFRPLPNRLNIIISKTMQEEEKEEVEEENKKENSYSSLQTSSSLREETAEKTKKEEVKSSSRTDKERRRFPYDRPVRICSSLPSALEMLDQDEEYSRTVNRIFIVGGSGIYKEALSLGVVSYIYLTRVGKEFSACDVFFPRFPGDEILSNPPSTSK... | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
Function: Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, DNA precursor synthes... |
A0A484AW31 | MCAKSQSFWERHELKFYRYGHIYASICGQVIIDYAPQQPMRAPFKSLLIAYSHALSLLLIVVLPGYFGYNYRALTATADRRMQLVLYVGLANTLIKYATVIVTYVANTCHFEAINRRCSLQRARLQASFAASYRASGWPKRRFELFMYLKFVLINLMMIVQICAILAVARIDRAGESDSDSDSASGQGRRLRIQFAIYAFVLWNYTENMADYFYYVNSCVLLYFRLLHMQLQAELEQLRRLGRGRLLLGVRIGLLRQRYAQIHALYTDSFRMHQFQLLGLMLATLINNLTNLFTIFNLLARSSRAFISLPVAVSGLYALG... | Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Location: Cell membrane
Sequence Length: 437
Sequence Mass (Da): 50412
Location Topology: Multi-pass membrane protein
|
A0A545W8A2 | MSRNVMFLLGALATIAIAQMPADAYDVPAVPNVVGQPLDGFVSYSIEFASFPEFAGNMSSPNQFSYNLLKNLGDVMGTNPYIRVGGNTQDYALFNGSQPEALIGIVDPNRSPDYPTSITIGPAYFESYNTWPGFKYSHGLNLGLGGNRSAGWQTLVETVPLVCKTLANGKLYIWEYGNEPDLYGVSAQGPVRPPSWDEASFVWQWLNGTKEIRPQVKKSCPSLAEPRYMAPSFAALSSPLKEPKTWQSGLNTNQDIELYSTHNYISGATSPGVTLQGTLMNFGVTQASVNNHVQAYNSIFKARGKASAPPLIFGETNSLY... | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
Function: Responsible for the formation of the pyrimidine heterocycle in the thiamine biosynthesis pathway. Catalyzes the formation of hydroxymethylpyrimidine phosphate (HMP-P) from histidine and pyridoxal phosphate (PLP). The protein uses PLP and the a... |
A0A1B3T857 | HAFVMIFFMVMPIMIGGFGNWLVPXMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVENGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFFDP | 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... |
A0A386B2D8 | MKMLIMSIIFSLMFLISSTSFWSMWLGLEMYNFFFTPWLMEEEKYKKSSKIFFYFVIQVMASGMFLIGMSNPNSGFFYTLLLVSMLLKLGGFPLHSWVLVVVENMKWIKFSFFLTVSKIGPIVVLMMSNPMVSMIKYVLGGVITPILGLKSSSIRIMLAYSSIAYMSWIVTTICVSKSLLLFFVIIYWSIFICSCFFFKKLMMKSVKDFFRNSCSYLEMSVILSLMGFPPFLGFFPKLFTVKVLCMMSMIPEALILSTLSVIPFYFYLKMLMSMMMSFSFKNHSFLPLMTINKIIFFEVLLIMFSLEVLVYTCM | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
V5KD81 | TMYFIFGIWSGMVGTSLSLLIRTELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMRINNMSFDQMPLFVWAVGITALLLFLSLPVLAGAITMLLTDRNLNTS | 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... |
Q66UD9 | IVLHDTYYVVAHFHYVLSMGAVFAIVAGFIHWYPLLTGLNMNNLYLKIQFSMMFLGVNLTFFPQHFLGLAGMPRRYSDYPDSCTTWNIISSLGSTISFLATLFFMFIIWESMISNRSIVYPVQLNSSIEWYQNLPPAEHSYNELPILTN | 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... |
A0A2C6KG07 | MVPLALNRPQELAVYSVSDAVATYYLYEQYIHNFILALCTIIPMTVRIKTVFLTLSFCLSSYPLSVSRRRRDS | Function: DNA polymerase II participates in chromosomal DNA replication.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
EC: 2.7.7.7
Subcellular Location: Nucleus
Sequence Length: 73
Sequence Mass (Da): 8420
|
A0A2C6KZI5 | MVVISSCSPSFFHSSSLSFSSFSFSFLCLLKSFSLSPFFITSLVCLIATIIMSTYGSVLRVHTFGESHGVAVGCIIDGLPSRLPLAPARDIQPQLNRRRPGQSFLSTQRNEKDQVQLLSGVENGYTLGTPLTMIVWNEDRKPSDYTDFSSSIPRPGHGDYTYHMKYHIHAKSGGGRSSARETIARVAAGAVIEKWLRLEYKTKIVAWVDQIGDISIPGPIRREWARSPPSREDVDRLGFVRMSCDGNFFLDAEGKLYDRSGEELKDDKHRQKARLLFASPADRSTAGGGGGGAGEKGVETRCPYPSIAVKMAAKIHEIRE... | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.
EC: 4.2.3.5
Catalytic Activity: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
Sequence Length: 797
Sequence Mass (Da): 83473
|
A0A2C6KWE4 | MHGRTKKSESALSLEEIEARRQKVKKGLKLLSHLLDQKNRGVYTPENFAATGKILDFAPEMGALWAYRREMLLHFLRQLRSEGEKDEEKEEEEKEGRSHANEEKTEEEEERNAEVHKEEEEEKDGEEKEQDGGHSVSKKRRKTNRIISSSSSSLSSSLPSSSSSRPSASSSVSCLTFLSHLHGGKDSQLDSCQKEGGADSSRDLHLLPPSPHLSFRDRAVFSLLYEELLSTRIAIAKKSSKNYCIWIHRTSCTGYLIHFLLSLSSTSPSLSSPSPASSLSSSPSPSPSSSASSLLSSSSFSLALSCILSLLREEMGSVES... | Function: Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to cysteines occuring in specific C-terminal amino acid sequences.
EC: 2.5.1.60
Catalytic Activity: geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]
Sequence Length: 6... |
A0A2C6KMH2 | MPGRDPKPGGGAAAFVASPQVILQQLLHARNEYRTQQQYSQRRDCEADHGDLERPGGCRATSVSSVVDSAPEGRAAPSETGAEQHSPEKRSEPVLANSVPLKTAEAPQSTEDSACIQGRQGDESFHDDHSPMPGGIAPSKEADWNSPSSHEVAKDESSFAPVVYSLASSSGAEPHSESGLLKIRSDRSGFGERVSGQQAVSQGGSFSPYTTAGEGSGDEDEELRTVVVVMRHGDRKPKQKLKFQTEQDLILELFEGRSPRKEVKLKSPEELKDLLERNTEIITSMGREMASLVAGIKTLSEHKAAAEAAAKASTSSDPKP... | Function: Bifunctional inositol kinase that acts in concert with the IP6K kinases to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-InsP4, also respectively called InsP7 and I... |
A0A2C6L1S0 | MVLNSNKKKKRKKKISLLHGSSPCLRLAPYSCSSFSSSSSYPCLFGRIRLKFVSFLLPLRGACHSHIPLQQHPTLPAVFACCKFFSSSSLSRSSSLPSLSSISPFSFSSFPPSYRFFSSSSFSSSSSVSPLLSSPVLLTSSSSLSFHSSSPPTSTRRSSLIHRCSHLSSAFSSSQTSSTLSLQSNTTPPSSSSQSSSSSSSSSSHSSSSSSHSSSSSSSSDSSSSSSFFSSSFIFSLLRRSLPSSLLSKLSAYFHLSRLHAPIGSWLLFWPCAHSALLALPATPHSLTYSLASSAYIREQTEGSTLHQLIQAWKDRHLPH... | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of coenzyme Q (CoQ) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, ge... |
A0A1V5Z5V5 | MNHQVNLDRIKNAMKPATSIWPWSGGKRPQMRSFKEMTGLSGGIISAVDLLNGIGVYAGMEIIRVPGATGFIDTDYQAKARYAIRALEKLDFLFIHVEAPDEAGHMGSIEEKVKAIERVDEMIGTIMKEFDGRIAVLPDHPTPVRIKTHTAEPVPFAILGKDKDSTTRFSEKEGAKGMYGLMPGTGLIPLLIS | Pathway: Carbohydrate degradation.
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Length: 193
Sequence Mass (Da): 21165
|
A0A2C6KXB1 | MSTTATGNPSASPSRSKREGKPAGGFSLLGHLYLCLYNTAALVAWAYVFYLFLEHCLEKRSWMAGGGAPALYRRLEWPLIIAQSMQIMEIFHAMIGLVRSGVVTTFIQVFSRLQLVLFLFRQIPASYNTIAFFSLIGAWCLAELFRYPFFIVQEFLRCFSQGQKAPSSSASSQTGAEVPMALKWLRYSGFTLLYPIGITSEVLCMFESLHTLKLPMFAHYPYPMPNVLNFEANLYFIYIAVLLAYIPGSFLLYNHMLQQRKKNLYGSGSDKEKRQ | Pathway: Lipid metabolism; fatty acid biosynthesis.
EC: 4.2.1.134
Subcellular Location: Membrane
Sequence Length: 275
Sequence Mass (Da): 31194
Location Topology: Multi-pass membrane protein
|
A0A5C7UT17 | GAAVERGGRDPSTAGPPQGASAPSAGSATGQAFGCLNIHASLLPRWRGAAPIHRAIEAGDAQTGVTIMQMDAGLDTGDMLLAQALPIGPRATTASLHDELAALGGQLIVQALQQAAQGRLRPTPQPAEGVCYAHKIDKHEAAIDWHQPAAQIERRIRAFDPFPGASSQLGDTVVKLWSSEIDSCSRPSDARCGQILAVDEGGIAVACADAVLRLTELQRPGGKRLPAREFLRGFALAPGQCLGEGTGGAP | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
EC: 2.1.2.9
Catalytic Acti... |
A0A559M3J5 | MSPLKSAASRALRSKLLAQNPRLFNKAKRSVGLAATARSEPNFPTPFISPGNLLDFHSSTITTPLPRGFPTTRPRERNENDFDGLIANLTQTLTTTRSRTPTLPALHQLMKSYTSDPAHWSRFAHVDPSKQYTRNLVYSVPGVFNLLLLVWNPGKESPVHDHADAHCLMKIMKGSLVESRFAIPSRPGEQGPLVQTARKEFGLNQVTYMADVLGLHAISNPHPTEHAMSLHLYTPPNAALRGCNVYDMRNGAVRHVRQDTYDSVGGESGSDTSLHEEDTNRFFGWGW | Cofactor: Binds 1 Fe cation per subunit.
EC: 1.13.11.20
Catalytic Activity: L-cysteine + O2 = 3-sulfino-L-alanine + H(+)
Sequence Length: 287
Sequence Mass (Da): 31892
|
A0A559M058 | MWVQQYEEMARCNGTYYVVVLVDGERDVIVGTGTLVVERKFMLNLGKQGHIKDVVITASHQGKGLGRALIRALDLIGEQLGCYKTILDCEPKNEPFYRKCGYKRMGIDMEHRYDEDETARSHAA | Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 1/2.
EC: 2.3.1.4
Catalytic Activity: acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N-acetyl-D-glucosamine 6-phosphate
Sequence Leng... |
A0A963M9Q5 | MKSIAQIAAELQGYDPQALPADAVNGFLARLVAPVADVQRVPVMQALGRVLAEDVVSPVSVPPHDNSAMDGFAFRGTELVAGQPLVLRSVGTAFAGAAWQGTVAAGECVKIMTGAVMPAGLDTVVPQEFARVQGDHITVPAGVVRAGDNRRKLGEDLMAGQPALLKGERLAPAALGLVASLGMGEVPVL | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 189
Sequence Mass (Da):... |
G8PCJ7 | MFKVLIGIIVVAVLIYIGIVAYQRFLLRKITDLQNRRANIGELPVKQKIQEVGDLSLSGSSQVNFNKIESDYSELTDKRLPEIDDIAEHAKQDVNEMKIFEARKDTTAMTDALNAIEADSNRIDDQLENFKKVDQEQHDSVKILRLKYQEFRKSLLAQNLTLGPSIDMLEENLSNLDSDFDNFSQTVDDGDHEKADGQLKILQERTNNLEQQINEIPPLYERLKTTFPEQLEEIQGGYDQLINHNYAFPDDNVRKEIHDLDAKISENTETLANLRLDAVRDNNESISKRIDALYDILQREIDARKDVDNSFPVISEFMTH... | Function: Negative regulator of FtsZ ring formation; modulates the frequency and position of FtsZ ring formation. Inhibits FtsZ ring formation at polar sites. Interacts either with FtsZ or with one of its binding partners to promote depolymerization.
Subcellular Location: Cell membrane
Sequence Length: 569
Sequence Mas... |
A0A3B9QEY5 | MAIAVSGVSNRLDYFIASIIGGSLILLATSIKQGTLASVFGVSGAVYIGGLLGCLGLLRVQPDGREWCFVVLFVTWANDMGAYFGGRAFGKRKLAPTISPGKSWEGACFGLGAGVLTGACLSSWTGFAVAEGAVVGALLAVMAQVGDLVESKLKRYCQVKDSGKAIPGHGGFLDRFDSLLFTGAGGLLLKGLYGLLLHT | Pathway: Lipid metabolism.
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: 199
Sequence Mass (Da): 20525
Location Topology: Multi-pass membrane protein
|
A0A1F3SR48 | MQYFRYELYHRELAGPLASLQRWFQEKNLGIIKALSIGELYFIASTERDCLKKVESAFCDPVLCTTTPPHYDMAVQITFRPGVTDNKGQAAHEALQLIGLQAQVRSGRLYLISGDVSHAELLSAAHALLANGLLEECQVYTRSEFEKLPREVEITGPVGEDLSAKLVREIDLAKSDQELLGLSGKNCWALELPEIKVIQAQFKNEDFLAHRRRLALPENPTDVEMEILAQTWSEHCKHKIFSAKIHYSEGPAATHAFGPAEINGAFRTFIKGVSEEIIAERKIDWAISLFKDNAGIVRFDKNIDLCAKVETHNSPSALDP... | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2.
Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent ... |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.