ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
C4Z900 | MKFTKMHGCGNDYVYVNLFEEKLDDPARVSIYVSDRHFGIGSDGLITIGPSDKADFRMRIYNADGSEAEMCGNGIRCVAKYVYDHKLTDKTEISVETGAGIKYLTLYVEENKVSQVRVDMGEPILTPGDIPVVKADGSAYSDDYRVIDEPISAGNREWHMTCVSMGNPHAVVFVDDVAGFELEKYGPLFENHKMFPKRTNTEFVEILSRNEAKMRVWERGSAETWACGTGTCATVMACILNKKTDNKVLVHLRGGDLTIEYIPETNHVFMTGPATEVFSGEIDII | Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate
Sequence Mass (Da): 31778
Sequ... |
Q21SV0 | MRIPFTKMQGAGNDFVVLDETQGRFGLSTAHYRLLADRHFGVGADQILTVRPSPAPGIDFEYLIHNADGAEVEQCGNGARCFARFVRDQGLTAKDAIRVQTRGGVIEPQLNPDGRVTVNMGAPVFELAEIPFDATGLQPQTSGLWKKWPLALVDSGHATTVYVAVVSMGNPHAVQVVDDVDTAPVRLQGPLIEHHASFPKRVNAGFMQIVDRSHIRLRVYERGTGETLACGSGACAAVVAGIRLGLLDDTVHVQTHGGTLTISWAGAAAPVLMTGPATPVFHGEINLPDNL | Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate
Sequence Mass (Da): 31084
Sequ... |
A6TRX5 | MEIKFKKMHGTGNDFIMIYYEDYPFEQHFNQLAKEVCHRHFGIGADGLMIVKESSVADVQMKYFNSDGSEAGMCGNGIRCFAKFVYDEGLVKKEIFTVETLSGVKELQVATVEEKVSSVRVNMGKMVLDPKQIPVNSEGLQFINEQLMIDGEKYTISTVLLGVPHTIIFMETLDLDRVKRVGKIIENHQLFPENTNVNFAQIINQNTIRVRTWERGAGYTLACGTGVSSVCGIANHLSLVGPNVVVEIEGGKLDIEIAPEGDIYMEGPAKDICKGVYLNSLIK | Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate
Sequence Mass (Da): 31494
Sequ... |
A8MH77 | MDVQFKKMQGTGNDFIVVKYDDFPFEEKLSQLAEKICDRHFGIGADGLLIVNPSSIADIRMDYYNSDGSIAAMCGNGIRCFSKFVFDEGFLRTKQFSVETLDGIKEIAIIEEKGTVKSVEVNMGQVTYDTEKIPVVSEDGYFINKKITVGGQDFIITAVSMGVPHVIIFTEKLDLEQIKFFGPLIEKHAIFPKKTNVNFVHRIDKDNIAVRTWERGAGYTLACGTGSTSAVAVANKLGLVNNNVNVEVEGGNIKIKIKESGNLFMEGPAENICSGRFFFN | Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate
Sequence Mass (Da): 30983
Sequ... |
Q8F9V5 | MASLKFTKMEGIGNDYVYIDSTRNDIRLTPEQIQKISDRNFGIGSDGVIFIRNSKQGDFMMDMYNSDGSSSEMCGNGIRCVAKYIYDHGLTSSKNPKIETGAGILEVDLKIGSGNKVDLVSVDMGKPVLVPSQIPVVWKNEETIIDQPLEIGDKNLKFTAVSMGNPHCVIFVDDSDEFPVRGIGPLIERHSIFPKRVNVEFVTIRGKDHLYQRTWERGAGETLACGTGACAVMVAGNLTRRSGKDVQIDLRGGTLRIQWQESGNILMTGPAREIFSGEIEI | Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate
Sequence Mass (Da): 30966
Sequ... |
Q8Y5N9 | MATIHFTKVHGSQNDFFLVDEEGNQIMDWSDAKRADFAIKLCDREHSLGGADGILYVTKSSEAGPIGQMRVVNSDGSIASMCGNGLRTVARYLLEKHALTEAKVETMKAILDVKKATSLGFDIPTYQVEISPVKFNAESLPMNVGVEKLFNQVVPELDAELAFSAVSVPNPHLITFVDQTVLDSDRQETLASYLNSENPYFPDGVNVSFVKRLSDDAIYVRTFERGVGFTNACGTAMSACSLIKKMLDKDTFETPLNVYNDGGRVQVTAKKDEAGDISLQLIGNATFVSTGSVSYESDTVTELTNEATPEQAQYQELVKE... | Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate
Sequence Mass (Da): 36071
Sequ... |
A0LE31 | MGERFIKMHGLGNDFVVLDHLESPRELSPQEARFWADRRRGVGCDQVVQLLPGVEGGDAQMRIYNPDGSRAEMCGNAMRCVGLYLHEQRGMAAALAVETLAGIMRPQVTSALAITVDMGRPQWAGRAIPLDQDGEMIDAPLEVGGQSYRMTALSMGNPHGVVRVADAEGFELAKVGPLVEHHALFPNRINFEVVQVLSRSRIRMRVWERGAGITPACGTGACAAAVACMRQGWVERDCTVVLDGGELQIVWLESDRVMMSGPATEVFRGELVGLPAGF | Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate
Sequence Mass (Da): 30199
Sequ... |
Q0W3B6 | MTKIKFTKMHGNGNDFIVIDEFENPVPEEKKAAFAKKVCHRRFGIGADGVLFLAKPLHTSLHMRIFNEDGSEAEMCGNGIRCFVKYAVDNGHMNPGKDKVETKAGILEVEARIEDGKTLVKVSMGKPLFDPKKIPAAGLNNFINKPLHGYEVTAVNTGVPHAVIFVDDVNAVDLMKVAPEIRYDLKTFPKGINVNFVQREGHNLRVRTYERGVEGETLSCGTGSVASAAVARYLGYTRDETTVYTAGGQLNISFVSDIAYMEGPAETVYEGEIDVDFSAL | Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate
Sequence Mass (Da): 30722
Sequence Length: 280
Pathway: Amino-acid biosynthesis; L-lysin... |
Q58519 | MEFTKMHALGNDYIVINEFDGEKVKEEEKAEFSRKICRRGFSVGADGVIFIQKPTSDEYDVRFRIFNSDGSEAEMCGNGIRCFSKYVYERIMKKNPLKVETKGGLRVSEMEIEGDEVKKIKVYMGVPKFKLKDIPMVVDGYKEDDEFLNGELKLKNPYLPKVKLSVVNVGNPHAVIFVEDNNIDLDFVREHLDVIGKEIEHHEAFPERINVHFVKVLNPNEIRIVTWERGAGYTTACGTGTTASVIMAHKLGKTNNRVLAHLDGGDLEIEIKDDGVYMIGDAVMVYDAKLINIGW | Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate
Sequence Mass (Da): 33442
Sequence Length: 295
Pathway: Amino-acid biosynthesis; L-lysin... |
Q8TY71 | MQFWKVHGARNDFVLVDETEEEVVPESDKPDFARWACDRRSGVGADGVVFIRSDPPSVEMRIFNRDGSEAEFCGNAARCVVKYVTEVRGENVKILRTLSGAHRVEVQGGWIAVEVPEAEIKKVVELGYEVDAGVPHFVRLTERDPIHDFGGLTDEAKTIFSEYEPKGGVNVTYAAPSVDELRVRTFERGVGWTPACGSGVVAASLVYSEIFGPFEEVSVRTAGGCLRVSLSDGPLLIGRAEIVYKGELRGDWRENTDHQRRRHSLSRSPSGRPRLQECR | Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate
Sequence Mass (Da): 30994
Sequence Length: 279
Pathway: Amino-acid biosynthesis; L-lysin... |
Q8E9H5 | MIQFTKMHGLGNDFMVVDGITQNVFFSPEQIRRLADRNFGVGFDQLLLVEPPYDPDLDFHYRIFNADGGEVENCGNGARCFARFVRNKGLTNKNKIRVSTSAGKMTLRLERDGTVTVNMGVPVLEPSQIPFKAKKAEKTYLLQTPQQTFLCGAASMGNPHCVLDVEDVANANVAEIGALLTKHERFPRGVNVGFMQVVNAGHIKLRVYERGAAETLACGTGACAAVVVGQIQGKLDQQVQVDLPGGSLTINWEGEGKPLWMTGPAQHVYDGQIQL | Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate
Sequence Mass (Da): 30063
Sequ... |
Q9UN19 | MGRAELLEGKMSTQDPSDLWSRSDGEAELLQDLGWYHGNLTRHAAEALLLSNGCDGSYLLRDSNETTGLYSLSVRAKDSVKHFHVEYTGYSFKFGFNEFSSLKDFVKHFANQPLIGSETGTLMVLKHPYPRKVEEPSIYESVRVHTAMQTGRTEDDLVPTAPSLGTKEGYLTKQGGLVKTWKTRWFTLHRNELKYFKDQMSPEPIRILDLTECSAVQFDYSQERVNCFCLVFPFRTFYLCAKTGVEADEWIKILRWKLSQIRKQLNQGEGTIRSRSFIFK | Function: May act as a B-cell-associated adapter that regulates B-cell antigen receptor (BCR)-signaling downstream of PI3K.
PTM: Phosphorylated on tyrosine residues.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32194
Sequence Length: 280
Subcellular Location: Cytoplasm
|
P16524 | MEHLLNPKAREIEISGIRKFSNLVAQHEDVISLTIGQPDFFTPHHVKAAAKKAIDENVTSYTPNAGYLELRQAVQLYMKKKADFNYDAESEIIITTGASQAIDAAFRTILSPGDEVIMPGPIYPGYEPIINLCGAKPVIVDTTSHGFKLTARLIEDALTPNTKCVVLPYPSNPTGVTLSEEELKSIAALLKGRNVFVLSDEIYSELTYDRPHYSIATYLRDQTIVINGLSKSHSMTGWRIGFLFAPKDIAKHILKVHQYNVSCASSISQKAALEAVTNGFDDALIMREQYKKRLDYVYDRLVSMGLDVVKPSGAFYIFPS... | Function: Essential for murein biosynthesis . Probably catalyzes the conversion of L-2-acetamido-6-oxopimelate to N-acetyl-LL-2,6-diaminopimelate (Probable).
Catalytic Activity: 2-oxoglutarate + N-acetyl-(2S,6S)-2,6-diaminoheptanedioate = L-2-acetamido-6-oxoheptanedioate + L-glutamate
Sequence Mass (Da): 43536
Sequence... |
Q7ZXQ9 | MSVNLSKNGAALQGAYKDVLDEKTKTDWALYTYEGNSNDIRLAETGDGGLEELVEELSSGKVMYAFCRVKDPNSGLPKFVLVNWTGEGVKDARKGACANHVSTMANFLKGAHVTINARAEEDVEPESIMEKVAKASGANYNFHKESKRGNEGPQGPVGSVYQKTNAMSEIKRVGKENFWAKAEKDEEERRMEENRRANSEKDRLERERKEREQREAETREQRFRERAKEIDAQRKEQEETEKQQTVPASQRSVNPRETFLQKERSLPESGPVSAQPGRLRSPFLQKSACQPESSPPPSPVHRVQEPPSPPVYPAHQTPPE... | Function: Adapter protein that binds F-actin and dynamin, and thereby plays a role in receptor-mediated endocytosis. Plays a role in the reorganization of the actin cytoskeleton, formation of cell projections, such as neurites, in neuron morphogenesis and synapse formation. Does not bind G-actin and promote actin polym... |
Q557J6 | MASLDISDPDITKYIKLVQDGNPANRWIVFSYVPKSNNKIKFCDSGSGDLKELREELDDSSIRFAYIRFVINNMPKFVYIPWCGDGVNGPIKGAFSGHAIEFSKSFKPIHHQVNARSEEDIDEKAITAALNKATGASYDSGSKVQGATKGTFIPQSVSQGREAATKSNAEVKNVINKNDYNKIQESAEYWKQNQANKSEPAKPTRPEYNLSTERDDYWKQQQAEKQKQQQQQQQQQASRVNAPPPSRTVGNKFQEQVSKPTETAPPQPRPAPSKGSVLNRFPAATQQQQEPPAPSRPAAPVPSRVNKPAAPVQPVYQEPV... | Function: Actin-binding adapter protein. Binds to F-actin but is not involved in actin polymerization, capping or bundling. Does not bind G-actin. Controls pseudopodium number and motility in early stages of chemotactic aggregation.
Sequence Mass (Da): 55338
Sequence Length: 481
Domain: The SH3 domain mediates the cont... |
Q9UJU6 | MAANLSRNGPALQEAYVRVVTEKSPTDWALFTYEGNSNDIRVAGTGEGGLEEMVEELNSGKVMYAFCRVKDPNSGLPKFVLINWTGEGVNDVRKGACASHVSTMASFLKGAHVTINARAEEDVEPECIMEKVAKASGANYSFHKESGRFQDVGPQAPVGSVYQKTNAVSEIKRVGKDSFWAKAEKEEENRRLEEKRRAEEAQRQLEQERRERELREAARREQRYQEQGGEASPQRTWEQQQEVVSRNRNEQESAVHPREIFKQKERAMSTTSISSPQPGKLRSPFLQKQLTQPETHFGREPAAAISRPRADLPAEEPAPS... | Function: Adapter protein that binds F-actin and DNM1, and thereby plays a role in receptor-mediated endocytosis. Plays a role in the reorganization of the actin cytoskeleton, formation of cell projections, such as neurites, in neuron morphogenesis and synapse formation via its interaction with WASL and COBL. Does not ... |
Q13409 | MSDKSELKAELERKKQRLAQIREEKKRKEEERKKKETDQKKEAVAPVQEESDLEKKRREAEALLQSMGLTPESPIVFSEYWVPPPMSPSSKSVSTPSEAGSQDSGDGAVGSRTLHWDTDPSVLQLHSDSDLGRGPIKLGMAKITQVDFPPREIVTYTKETQTPVMAQPKEDEEEDDDVVAPKPPIEPEEEKTLKKDEENDSKAPPHELTEEEKQQILHSEEFLSFFDHSTRIVERALSEQINIFFDYSGRDLEDKEGEIQAGAKLSLNRQFFDERWSKHRVVSCLDWSSQYPELLVASYNNNEDAPHEPDGVALVWNMKY... | Function: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function . Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organ... |
Q9Y6G9 | MAAVGRVGSFGSSPPGLSSTYTGGPLGNEIASGNGGAAAGDDEDGQNLWSCILSEVSTRSRSKLPAGKNVLLLGEDGAGKTSLIRKIQGIEEYKKGRGLEYLYLNVHDEDRDDQTRCNVWILDGDLYHKGLLKFSLDAVSLKDTLVMLVVDMSKPWTALDSLQKWASVVREHVDKLKIPPEEMKQMEQKLIRDFQEYVEPGEDFPASPQRRNTASQEDKDDSVVLPLGADTLTHNLGIPVLVVCTKCDAISVLEKEHDYRDEHFDFIQSHIRKFCLQYGAALIYTSVKENKNIDLVYKYIVQKLYGFPYKIPAVVVEKDA... | Function: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organe... |
Q9QXU8 | MAAVGRVGSFGSSPPGLASTYASGPLANELASGSGGPAAGDDEDGQNLWSRILREVSTRSRSKLPTGKNVLLLGEDGAGKTSLIRRIQGIEEYKKGRGLEYLYLNVHDEDRDDQTRCNVWILDGDLYHKGLLKFSLDALSLRDTLVMLVVDMSKPWTALDSLQKWASVVREHVDKLKIPPEEMKEMEQKLIRDFQEYVEPGEDFPASPQRRATAAQEDRDDSVVLPLGADTLTHNLGLPVLVVCTKCDAISVLEKEHDYRDEHFDFIQSHIRKFCLQYGAALIYTSVKENKNIDLVYKYIVQKLYGFPYKIPAVVVEKDA... | Function: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organe... |
P16453 | MMEPSEYHEYQARGKEMVDYICQYLSTVRERQVTPNVKPGYLRAQIPSSAPEEPDSWDSIFGDIEQIIMPGVVHWQSPHMHAYYPALTSWPSLLGDMLADAINCLGFTWASSPACTELEMNIMDWLAKMLGLPDFFLHHHPSSQGGGVLQRTVSESTLIALLAARKNKILEMKAHEPNADESSLNARLVAYASDQAHSSVEKAGLISLVKIKFLPVDDNFSLRGEALQKAIEEDKQQGLVPVFVCATLGTTGVCAFDKLSELGPICAREGLWLHVDAAYAGTAFLRPELRGFLKGIEYADSFTFNPSKWMMVHFDCTGFW... | Function: Catalyzes the biosynthesis of histamine from histidine.
PTM: May be post-translationally processed.
Catalytic Activity: H(+) + L-histidine = CO2 + histamine
Sequence Mass (Da): 73636
Sequence Length: 656
Pathway: Amine and polyamine biosynthesis; histamine biosynthesis; histamine from L-histidine: step 1/1.
E... |
O87873 | MSEASSPLKVWLERDGSLLRLRLARPKANIVDAAMIAAMRQALGEHLQAPALRAVLLDAEGPHFSFGASVDEHMPDQCAQMLKSLHGLVREMLDSPVPILVALRGQCLGGGLEVAAAGNLLFAAPDAKFGQPEIRLGVFAPAASCLLPPRVGQACAEDLLWSGRSIDGAEGHRIGLIDVLAEDPEAAALRWFDEHIARLSASSLRFAVRAARCDSVPRIKQKLDTVEALYLEELMASHDAVEGLKAFLEKRSANWENR | Function: Catalyzes the hydration of cyclohexa-1,5-diene-1-carboxyl-CoA.
Catalytic Activity: cyclohexa-1,5-diene-1-carbonyl-CoA + H2O = 6-hydroxycyclohex-1-ene-1-carbonyl-CoA
Sequence Mass (Da): 27882
Sequence Length: 258
Pathway: Aromatic compound metabolism; benzoyl-CoA degradation.
EC: 4.2.1.100
|
Q9FHR8 | MTMESYKTLEIIRKNTDSSVFHLIINRPSHLNALSLDFFIEFPKALSSLDQNPDVSVIILSGAGKHFCSGIDLNSLSSISTQSSSGNDRGRSSEQLRRKIKSMQAAITAIEQCRKPVIAAIHGACIGGGVDLITACDIRYCSEDAFFSIKEVDLAIVADLGTLQRLPSIVGYANAMELALTARRFSGSEAKDLGLVSKVFGSKSELDNGVTTIAEGIGGKSPLAVTGTKAVLLRSREVSVEQGLDYVATWNSAMLISDDLNEAVSAQMMKRKPRFAKL | Function: Converts 3,5-dienoyl-CoAs to the corresponding 2,4-dienoyl-CoAs. Involved in degradation of unsaturated fatty acids.
Catalytic Activity: a (3E,5Z)-dienoyl-CoA = a (2E,4E)-(5,6-saturated)-dienoyl-CoA
Sequence Mass (Da): 29920
Sequence Length: 278
Pathway: Lipid metabolism; fatty acid beta-oxidation.
Subcellula... |
Q08558 | MSSRVCYHINGPFFIIKLIDPKHLNSLTFEDFVYIALLLHKANDIDSVLFTVLQSSGKYFSSGGKFSAVNKLNDGDVTSEVEKVSKLVSAISSPNIFVANAFAIHKKVLVCCLNGPAIGLSASLVALCDIVYSQNDSVFLLFPFSNLGFVAEVGTSVTLTQKLGINSANEHMIFSTPVLFKELIGTIITKNYQLTNTETFNEKVLQDIKQNLEGLYPKSVLGMKELLHSEMKQKLIKAQAMETNGTLPFWASGEPFKRFKQLQEGNRRHKL | Function: Peroxisomal di-isomerase that is involved in fatty acid metabolism enzyme by converting 3,5-dienoyl-CoAs to the corresponding 2,4-dienoyl-CoAs . Required for ECI1 to be locazed to the peroxisome .
Catalytic Activity: a (3E,5Z)-dienoyl-CoA = a (2E,4E)-(5,6-saturated)-dienoyl-CoA
Sequence Mass (Da): 30058
Seque... |
P51852 | MKLAEALLRALKDRGAQAMFGIPGDFALPFFKVAEETQILPLHTLSHEPAVGFAADAAARYSSTLGVAAVTYGAGAFNMVNAVAGAYAEKSPVVVISGAPGTTEGNAGLLLHHQGRTLDTQFQVFKEITVAQARLDDPAKAPAEIARVLGAARALSRPVYLEIPRNMVNAEVEPVGDDPAWPVDRDALAACADEVLAAMRSATSPVLMVCVEVRRYGLEAKVAELAQRLGVPVVTTFMGRGLLADAPTPPLGTYIGVAGDAEITRLVEESDGLFLLGAILSDTNFAVSQRKIDLRKTIHAFDRAVTLGYHTYADIPLAGL... | Cofactor: Binds 1 metal ion per subunit.
Catalytic Activity: H(+) + indole-3-pyruvate = CO2 + indole-3-acetaldehyde
Sequence Mass (Da): 57981
Sequence Length: 545
Pathway: Plant hormone metabolism; auxin biosynthesis.
EC: 4.1.1.74
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P23234 | MRTPYCVADYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDSPDICWVGCANELNASYAADGYARCKGFAALLTTFGVGELSAMNGIAGSYAEHVPVLHIVGAPGTAAQQRGELLHHTLGDGEFRHFYHMSEPITVAQAVLTEQNACYEIDRVLTTMLRERRPGYLMLPADVAKKAATPPVNALTHKQAHADSACLKAFRDAAENKLAMSKRTALLADFLVLRHGLKHALQKWVKEVPMAHATMLMGKGIFDERQAGFYGTYSGSASTGAVKEAIEGADTVLCVGTRFTDTLTAGFTHQLTPAQTIEVQPHAARVGDVWFT... | Cofactor: Binds 1 metal ion per subunit.
Catalytic Activity: H(+) + indole-3-pyruvate = CO2 + indole-3-acetaldehyde
Sequence Mass (Da): 60024
Sequence Length: 552
Pathway: Plant hormone metabolism; auxin biosynthesis.
EC: 4.1.1.74
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Q5ZJM7 | MSAPAKRRCRGPAADLDSSFQKRLRKISIEGNIAAGKSTLVRLLEKHSDEWEVIPEPIAKWCNIQTSEDECKELSTSQKSGGNLLQMLYDKPTRWAYTFQTYACLSRVRAQLKPISAKLHEAEHPVQFFERSVYSDRYVFASNLFESGNINETEWAIYQDWHSWLLNQFQSEIELDGIIYLRTTPQKCMERLQKRGRKEEEGIDLEYLENLHYKHETWLYEKTMRVDFENLKEIPILVLDVNEDFKNDKIKQEYLIDEIKSFLTS | Function: Phosphorylates the deoxyribonucleosides deoxyadenosine, deoxycytidine and deoxyguanosine . Shows highest activity against deoxyguanosine followed by deoxycytidine and then deoxyadenosine . Shows only very minor activity against deoxyuridine and deoxythymidine .
Catalytic Activity: 2'-deoxycytidine + a ribonuc... |
Q12517 | MTGAATAAENSATQLEFYRKALNFNVIGRYDPKIKQLLFHTPHASLYKWDFKKDEWNKLEYQGVLAIYLRDVSQNTNLLPVSPQEVDIFDSQNGSNNIQVNNGSDNSNRNSSGNGNSYKSNDSLTYNCGKTLSGKDIYNYGLIILNRINPDNFSMGIVPNSVVNKRKVFNAEEDTLNPLECMGVEVKDELVIIKNLKHEVYGIWIHTVSDRQNIYELIKYLLENEPKDSFA | Function: Component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Decapping is the major pathway of mRNA degradation... |
Q8GW31 | MSGLHRSSSSSKNIGNCLPSKELLDDLCSRFVLNVPEEDQQSFERILFLVEYAYWYYEDNAVENDPKLKSLSLKEFTSLLFNSCDVLRPYVTHIDDIFKDFTSYKCRVPVTGAIILDETYERCLLVKGWKGSSWSFPRGKKSKDEEDHACAIREVLEETGFDVSKLLKREEYIEFVFRQQRVRLYIVAGVTEDTVFAPLTKKEISEITWHRLDHLQPASNEVITHGVSGLKLYMVAPFLSSLKSWILKHPSPVARRPNKPLKALCVWNARTSVGGNGTATVESQNRKSELRTTTMESNSRKPELKRTTMESHSTKPELRK... | Function: Catalytic component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Essential for postembryonic development,... |
Q75BK1 | MSLPLRNPLDSVSLERALEDLIVRFIINVPPEDLATVERELFHFEEAQWFYTDFVKLTNPHLPNMKFKTFASYVISLCPLVWKWQDVNPEEALQKFSKYKKSIPVRGAAIFNETLNKILLVKGTESDSWSFPRGKISKDEDDVDCCIREVMEEIGFDLTNYVLEDQYIERNIGGKNYKIYLVKGVPQDFAFKPQVRNEIEKIEWRDFWKLSRSIHKSNNKFYLVSSMVKPLSLWVKKQKQIQGEEQLKQYAEEQLKLLLGIGTQEEAADPGRDLLNMLQSSVGQKKPLVFSDDESQASISTSAPTTVPPAPSTANSQSVQ... | Function: Catalytic component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Decapping is the major pathway of mRNA d... |
O62255 | MEISTENWCKKPKNRSIFSKNISFQKQNKSTEEPPSSVQKLLASLQQAQNKSDLSEQPSTSKPKKNEKRKKAVAQAPASAPAPGPEEKKKQPKRASVGARMQQQAENARISQTKRPRQVSTSKGSSRNTTAPEQQNYQQQQQQYKGPRIPTDILDELEFRFISNMVECEINDNIRVCFHLELAHWYYIDHMVEDDKISGCPNVGSRDFNFQMCQHCRVLRKYAHRADEVLAKFREYKSTVPTYGAILVDPEMDHVVLVQSYFAKGKNWGFPKGKINQAEPPRDAAIRETFEETGFDFGIYSEKEKKFQRFINDGMVRLYL... | Function: Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs . Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP . RNA-decapping enzyme although it does not bind the RNA cap . May contribute to gene regulation in multiple... |
Q8IU60 | METKRVEIPGSVLDDLCSRFILHIPSEERDNAIRVCFQIELAHWFYLDFYMQNTPGLPQCGIRDFAKAVFSHCPFLLPQGEDVEKVLDEWKEYKMGVPTYGAIILDETLENVLLVQGYLAKSGWGFPKGKVNKEEAPHDCAAREVFEETGFDIKDYICKDDYIELRINDQLARLYIIPGIPKDTKFNPKTRREIRNIEWFSIEKLPCHRNDMTPKSKLGLAPNKFFMAIPFIRPLRDWLSRRFGDSSDSDNGFSSTGSTPAKPTVEKLSRTKFRHSQQLFPDGSPGDQWVKHRQPLQQKPYNNHSEMSDLLKGKNQSMRG... | Cofactor: Mn(2+) ion is required for highest activity. Can also utilize magnesium ions.
Function: Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs . Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP . Necessary for the ... |
O13828 | MSFTNATFSQVLDDLSARFILNLPAEEQSSVERLCFQIEQAHWFYEDFIRAQNDQLPSLGLRVFSAKLFAHCPLLWKWSKVHEEAFDDFLRYKTRIPVRGAIMLDMSMQQCVLVKGWKASSGWGFPKGKIDKDESDVDCAIREVYEETGFDCSSRINPNEFIDMTIRGQNVRLYIIPGISLDTRFESRTRKEISKIEWHNLMDLPTFKKNKPQTMKNKFYMVIPFLAPLKKWIKKRNIANNTTKEKNISVDVDADASSQLLSLLKSSTAPSDLATPQPSTFPQPPVESHSSFDIKQKILHLLNEGNEPKSPIQLPPVSNL... | Function: Catalytic component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Decapping is the major pathway of mRNA d... |
P53550 | MSLPLRHALENVTSVDRILEDLLVRFIINCPNEDLSSVERELFHFEEASWFYTDFIKLMNPTLPSLKIKSFAQLIIKLCPLVWKWDIRVDEALQQFSKYKKSIPVRGAAIFNENLSKILLVQGTESDSWSFPRGKISKDENDIDCCIREVKEEIGFDLTDYIDDNQFIERNIQGKNYKIFLISGVSEVFNFKPQVRNEIDKIEWFDFKKISKTMYKSNIKYYLINSMMRPLSMWLRHQRQIKNEDQLKSYAEEQLKLLLGITKEEQIDPGRELLNMLHTAVQANSNNNAVSNGQVPSSQELQHLKEQSGEHNQQKDQQSS... | Function: Catalytic component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay . Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP . Decapping is the major pathway of mRNA... |
D3K0N9 | MVDEVDANSTGDNSLVNMKGFSFKEVLGSDSARKSAFILLDSSNGENAILLADKNAFPVDKTSWSAILTGSTLKPIMKNDIYSSYTLCMPNEFSDVKSTLIYPCNEKHIAKYRDQKRFIINETPEDYRTITLPYIQRNQMSLEWVYNILDHKAEVDRIIYEETDPHDGFILAPDLKWSGEQLECLYVQALVRRKGIKSIRDLTANDLPLLEGIRDKGLNAIKEKYGLDKHQIRAYFHYQPSFYHLHVHFIHVSYEAPASGVAKAVLLDDVINNLKLIPDFYQRSTLTFTAKEQDPIYRREN | Function: Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs of the 3'->5' exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG) and tri-methyl guanosine nucleoside triphosphate (m... |
Q8MJJ7 | MAELAHQQSKRKRELDAEEAEASSTEGEEAGVGNGTSAPVRLPFSGFRVKKVLRESARDKIIFLHGKVNEASGDGDGEDAVVILEKTPFQVDQVAQLLKGSPELQLQFSNDVYSTYHLFPPRQLSDVKTTVVYPATEKHLQKYLRQDLHLVRETGSDYRNVTLPHLESQSLSIQWVYNILDKKAEADRIVFENPDPSDGFVLIPDLKWNQQQLDDLYLIAICHRRGIKSLRDLTAEHLPLLRNILREGQEAILRRYQVAADRLRVYLHYLPSYYHLHVHFTALGFEAPGAGVERAHLLAEVIDNLEQDPEHYQRRTLTFA... | Function: Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs by 3'->5' exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG) with up to 10 nucleotide substrates (small capped oligo... |
G5EFS4 | MKRIADEELVREERAEESTQKWLQDAKFQEILGADSSHKSLFVLLSHPDGSQGILLANKSPFSEEKSDIEKLLATAQLQEISRNDIFGSYNIEIDPKLNLLKSQLIYPINDRLIAKYRQEEKFVIRETPELYETVTRPYIEKYQLNLNWVYNCLEKRSEVDKIVFEDPDNENGFVLLQDIKWDGKTLENLYVLAICHRHGLKSVRDLTGDDLEMLYNMRDKSLEAINQKYGLKTDQIKCYFHYQPSFYHLHVHFINLKYDAPASTTMSAILLDDVINNLELNPEHYKKSTLTFTRKNGDKLMEMFREALKN | Function: Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs of the 3'->5' exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG) and tri-methyl guanosine nucleoside triphosphate (m... |
Q96C86 | MADAAPQLGKRKRELDVEEAHAASTEEKEAGVGNGTCAPVRLPFSGFRLQKVLRESARDKIIFLHGKVNEASGDGDGEDAVVILEKTPFQVEQVAQLLTGSPELQLQFSNDIYSTYHLFPPRQLNDVKTTVVYPATEKHLQKYLRQDLRLIRETGDDYRNITLPHLESQSLSIQWVYNILDKKAEADRIVFENPDPSDGFVLIPDLKWNQQQLDDLYLIAICHRRGIRSLRDLTPEHLPLLRNILHQGQEAILQRYRMKGDHLRVYLHYLPSYYHLHVHFTALGFEAPGSGVERAHLLAEVIENLECDPRHYQQRTLTFA... | Function: Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs by the 3'->5' exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG) with up to 10 nucleotide substrates (small capped o... |
Q99KJ8 | MADPKYADLPGIARNEPDVYETSDLPEDDQAEFDAEELSSTSVEHIIVNPNAAYDKFKDKRVGTKGLDFSDRIGKTKRTGYESGDYEMLGEGLGVKETPQQKYQRLLHEVQELTTEVEKIKTTVKESATEEKLTPVVLAKQLAALKQQLVASHLEKLLGPDAAINLADPDGALAKRLLLQLEATKSSKGSSGGKATAGAPPDSSLVTYELHSRPEQDKFSQAAKVAELEKRLTELEATVRCDQDAQNPLSAGLQGACLMETVELLQAKVSALDLAVLDQVEARLQSVLGKVNEIAKHKASVEDADTQNKVHQLYETIQRW... | Function: Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules. In the dynactin soulder domain, binds the ACTR1A filament and acts as a molecular ruler to determine the length (By similarity). Modulates cytoplasmic dynein binding to an organelle, and p... |
Q9Z716 | MSAFFDLLKSQTASHPPIWLLRQVGRYMPPYQELKGSQSLKTFFHNTEAIVEATLLGPSLLHVDAAILFADILSILDGFAVTYDFAPGPRIQFSPEQPFTFTSDPQTIFSYLLDAIRTLKQKLPVPLIVFAASPFTLACYLIDGGASKDFSKTMSFLYVYPEKFDQLISTIIEGTAIYLKTQMDAGAAAVQLFESSSLRLPSALFTRYVTEPNRRLIAKLKEQAIPVSLFCRCFEENFYTLQATQADTLHPDYHVDLHRIQKNLMLSLQGNLDPAIFLLPQEKLLHYVEAFLVPLRTYPNFIFNSGHGILPETPLENVQL... | Function: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Catalytic Activity: 4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III
Sequence Mass (Da): 37166
Sequence Length: 329
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX b... |
Q8KAW2 | MLKNDLFIRALKRQATPRTPIWVMRQAGRYLPEYRAVREKTDFLTLCKTPELACEVTIQPVDLMGVDAAIIFSDILVVNEAMGMNVEIIETKGIKLTPPIRSQADIDKLIDPDIDEKLGYVLDAIRLAKKELNDRVPLIGFSGAAWTLFTYAVEGGGSKNYTWAKKMMYREPKMAHQLLQKISDCISAYLVKQVEAGADAIQIFDSWASALSEDDYREFALPYIKQNVAAVKAAYPEIPVIAFAKDMNTILSDIADCGADAVGLGWNIDIAKARKELNDRVCLQGNMDPTVLYGTPEKIKSEAAKVLKQFGQHNDHSGHV... | Function: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Catalytic Activity: 4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III
Sequence Mass (Da): 39104
Sequence Length: 351
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX b... |
A0M6C4 | MIKNDLLLKALKGESVERPPVWMMRQAGRYLPDFMKLKEKYDFFTRCRTPELATEITVMPIRQIGPDAAILFSDILVVPQAMNIEVEMKPGVGPWLPNPIDSPKKVEQVIVPDVNEELGYVFEAIKMTKQELNDEVPLIGFAGSPWTILCYCVQGQGSKTFDKAKRFCFMNPIAAHTLLQKITDTTIAYLKEKVKAGVDAVQLFDSWGGLLEPKDYQEFSWKYMQQIIEALKDEVPVIAYGKGCWFALDKMAKSGAAALGVDWTCEARNARYLSGGEITLQGNFDPARLYSKPIEIKYMVNDMIKAFGKDRYIANLGHGI... | Function: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Catalytic Activity: 4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III
Sequence Mass (Da): 38434
Sequence Length: 341
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX b... |
Q6KZ54 | MNSFISMIRNGYSDTIPVWFMRQAGRYLKEYNEKKGRMTIKEICMDPELIAGISYDPVRILNVDAAIIFSDITIPLEALGYKIEFLPGGPRIINGYIKNHDMKDIIYFEESNFKYKIYDAIKIFKEKYHFPLIGFSGGLITVLSYIIAGGPDSNLNLTKRSMLSDDKFNDYINIIKDMIIKYIRLQVRAGVDAIQIFDSWLGYLSPQTYENYIKGHIEEILSEINVPVIYFSTGTSSIIEKLSRLNVDYISVDWRLDMKLARSMVNKKGLQGNLDPLIAAYNLRYALKETSDIINAAGRSSYIFNLGHGVIPETPVENLK... | Function: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Catalytic Activity: 4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III
Sequence Mass (Da): 37932
Sequence Length: 331
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX b... |
A1VJ58 | MFAPLQNDTFLRACLRQATDHTPVWLMRQAGRYLPEYKATRAKAGSFMGLATNTDYATEVTLQPLERYPLDAAILFSDILTVPDAMGLGLSFALGEGPRFATPVRDEAAVNKLEVPDMNKLRYVFDAVTSIRKALGGRVPLIGFSGSPWTLACYMVEGSGSDDYRLVKTMLYQRPDLMHKMLAINADAVALYLNAQIEAGAQAVMIFDSWGGVLADAAFHTFSLAYTARVLSQLKREHKGVTIPRLVFTKGGGQWLESMKQLDCEVLGLDWTVNLAKARALVGENGPNAKALQGNLDPNVLFANPAQIEAEVAAVLNSFG... | Function: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Catalytic Activity: 4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III
Sequence Mass (Da): 40223
Sequence Length: 369
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX b... |
Q5RDK5 | MEANGLGPQGFPELKNDTFLRAAWGEETDYTPVWCMRQAGRYLPEFRETRAAQDFFSTCRSPEACCEPTLQPLRRFPLDAAIIFSDILVVPQALGMEVTMVPGKGPSFPEPLREEQDLECLRDPEVVASELDYVFQAITLTRQRLAGRVPLIGFAGAPWTLMTYMVEGGGSSTMAQAKRWLYQRPQASHQLLRILTDALVPYLVGQVAAGAQALQLFESHAGHLGPQLFSKFALPYIRDVAKQVKARLREAGLAPVPMIIFAKDGHFALEELAQAGYEVVGLDWTVAPKKARECVGKTVTLQGNLDPCALYASEEEIGQL... | Function: Catalyzes the sequential decarboxylation of the four acetate side chains of uroporphyrinogen to form coproporphyrinogen and participates in the fifth step in the heme biosynthetic pathway. Isomer I or isomer III of uroporphyrinogen may serve as substrate, but only coproporphyrinogen III can ultimately be conv... |
A5F3N0 | MTELKNDRYLRALLKQPVDYTPVWMMRQAGRYLPEYRATRAQAGDFMALCKNAELASEVTLQPLRRFPLDAAILFSDILTIPDAMGLGLRFAAGEGPVFERPITCKADVDKIGIPDPEGELQYVMNAVRQIRKDLQGEVPLIGFSGSPWTLATYMVEGGSSKAFTKIKKMMYSEPTVLHALLDKLADSVISYLNAQIKAGAQAVMVFDTWGGVLTPRDYQQFSLQYMHKIVDGLIRENEGRRVPVTLFTKNGGMWLEQIAATGCDAVGLDWTINIADAKARVGDKVALQGNMDPSILYAPAPRIREEVASILAGFGQGGT... | Function: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Catalytic Activity: 4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III
Sequence Mass (Da): 39048
Sequence Length: 355
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX b... |
Q8CWI5 | MQFFENDSYLRSALRKSVKRTPIWIMRQSGRYLKEYQSIKKQAKDFLSLCKTPDLSSKAALIPIKKFSLDAAIIFSDILILPYAMGMDVNFYENLGPSFLNPISSISDMKNLNVPDPEKNLKYVLDSIKIICKELDKKIPLIGFSGSPWTLACYMIEGKCNKIFSKIKKMIYQNSKELHFLLKKITNSIILYLNSQIIYGVNAIIIFDTWGGILTEEKYCEYSLHYMSLIIKNLFCKYKGNKIPVTIFTKNGGQWIKKIAKSGCDVIALDWSVDIEYARKQVNGKIAIQGNMDPFELYGSFSSIEEETNKILSKFGYNSG... | Function: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Catalytic Activity: 4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III
Sequence Mass (Da): 41359
Sequence Length: 360
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX b... |
B3CM33 | MESNKPAIVRIIKQNKPNEKVPIWLMRQAGRSLPEYRKAVEKTSNFMEICYSIDLVVELTLQPIKRFDMDAAIIFSDILIIADVLGCDVNFVRGVGPIIKPVKSSEELKNSQEFETKTFPILNAIRKVRSQLSEEKSLIGFAGGPWTVASYIIEGGSSKTFSKVLHFCSLELEEVIKKITEATIIYLIKQIEFGADVIQLFDSNAGILQGELFERYVIKPTKEIVSAIKNKFPDFPIIGFPRSAGNLYKDYYEKTGVSAVSIDYNVPIEWAKANLKIPLQGNLNPSLLAYNKAEAIEEAKRIIDCFRGLPFIFNLGHGVL... | Function: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Catalytic Activity: 4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III
Sequence Mass (Da): 37935
Sequence Length: 338
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX b... |
Q15SS1 | MFAAQYIGNKSFNVVEGHAIAPQAGEVRLDVGYVGICGTDMHIYHGVMDQRVSIPQTIGHEISGVVAQIGEGVEGFTVGEKVVVRPLDWCGECPTCEAGLTHICQNLKFMGIDTPGAFQSSWTVKARTLHKLPAGVDLKQGALVEPLSVACHDVRRSRLKAGEKAVILGGGPIGQLVAAVAKSVGAEVLVSEPNDSRREFADELGVKSVNPMDTDLAAYVDQWTGTKGADVVFEVSGVLPAIQSMTQIAGRRGRIVMVAIHSTAPPIDLFQFFWKELELLGARVYEAADFDWAIELIASGQIDLKPFISSVSPLADIGSA... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Involved in the degradation of 3,6-anhydro-L-galactose, which is the major monomeric sugar of red macroalgae. Catalyzes the third step of the pathway, the NAD(+)-dependent oxidation of 2-dehydro-3-deoxy-L-galactonate (L-KDGal) to 3-deoxy-D-glycero-2,5-hexodiulosonate... |
Q15SS0 | MLEKFSLEGKVALVTGCKRGIGKGIALGLAEAGADIIGVSASLALEGSDVENEVKALGRNFKGYQCDFSDRDALYAFIKEVKADFPKIDILVNNAGTILRAPAAEHGDDLWDKVIDVNLNSQFILSREIGKEMVARQSGKIIFTASLLTFQGGITVPGYAASKGAIGQLVMALSNEWAGKGVNVNAIAPGYIDTDNTQALREDSERSAAILGRIPQGRWGNPDDFKGPAVFLASDAASYVNGAILLVDGGWMGR | Function: Involved in the degradation of 3,6-anhydro-L-galactose, which is the major monomeric sugar of red macroalgae. Catalyzes the fourth step of the pathway, the reduction of 3-deoxy-D-glycero-2,5-hexodiulosonate (L-DDGal) to 2-dehydro-3-deoxy-D-gluconate (KDG).
Catalytic Activity: 2-dehydro-3-deoxy-D-gluconate + N... |
B2J6X9 | MSNVQASFEATEAEFRVEGYEKIEFSLVYVNGAFDISNREIADSYEKFGRCLTVIDANVNRLYGKQIKSYFRHYGIDLTVVPIVITEPTKTLATFEKIVDAFSDFGLIRKEPVLVVGGGLTTDVAGFACAAYRRKSNYIRVPTTLIGLIDAGVAIKVAVNHRKLKNRLGAYHAPLKVILDFSFLQTLPTAQVRNGMAELVKIAVVANSEVFELLYEYGEELLSTHFGYVNGTKELKAIAHKLNYEAIKTMLELETPNLHELDLDRVIAYGHTWSPTLELAPMIPLFHGHAVNIDMALSATIAARRGYITSGERDRILSLM... | Function: Catalyzes the conversion of sedoheptulose 7-phosphate to demethyl-4-deoxygadusol (DDG) . Involved in the synthesis of the mycosporine-like amino acid shinorine, a natural sunscreen compound that protects the cell against UV radiation .
Catalytic Activity: D-sedoheptulose 7-phosphate = (R)-demethyl-4-deoxygadu... |
Q3M6C3 | MSIVQAKFEAKETSFHVEGYEKIEYDLVYVDGIFEIQNSALADVYQGFGRCLAIVDANVSRLYGNQIQAYFQYYGIELRLFPITITEPDKTIQTFERVIDVFADFKLVRKEPVLVVGGGLITDVVGFACSTYRRSSNYIRIPTTLIGLIDASVAIKVAVNHRKLKNRLGAYHASRKVFLDFSLLRTLPTDQVRNGMAELVKIAVVAHQEVFELLEKYGEELLRTHFGNIDATPEIKEIAHRLTYKAIHKMLELEVPNLHELDLDRVIAYGHTWSPTLELAPRLPMFHGHAVNVDMAFSATIAARRGYITIAERDRILGLM... | Function: Catalyzes the conversion of sedoheptulose 7-phosphate to demethyl-4-deoxygadusol (DDG) . Involved in the synthesis of the mycosporine-like amino acid shinorine, a natural sunscreen compound that protects the cell against UV radiation (By similarity).
Catalytic Activity: D-sedoheptulose 7-phosphate = (R)-demet... |
Q8GPG4 | MLRTTRRTLMQGASLVGAGLFAAGRGWALNRLEPIGDTLAEEYPYRDWEDLYRNEFTWDYVGKAAHCINCLGNCAFDIYVKDGIVIREEQLAKYPQISPDIPDANPRGCQKGAIHSTSMYEADRLRYPMKRVGARGEGKWQRISWDQATEEIADKIIDIYEKYGPGKLMTHTGSGNMSMMRMAAPYRFASLVGGVQLDIFTDVGDLNTGAHLAYGNALESFTSDAWFGADYIMFLLFNPVATRIPDAHFLWEAKWNGARVVSVAPDYNPSSIHSDLWMPIKQGADPFLAMSMVNVIIEGKLYNEAFMKEQTDLPILVRSD... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Allows photoautotrophic growth on dimethyl sulfide (DMS) as the sole electron donor.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.
Catalytic Activity: dimethyl sulfide + 2 Fe(III)-[cytochrome c2]... |
Q8GPG1 | MPGFRFLLAATAAFLATSPALPLSADSLNAGNIRLVDPEETVPVIKIPDGIYLRTPNDPDDIIWARVPEFRVEMVMAPPVHPSVGLRYRDEYPEQDLVVQLARTSERFYVRLRWVDPTRDMSTLRDRFRDGAAIEFSESDDSVSYMMGTDAESPVNIWYWHPDGDRVESLAAGSPGSLTRLDRQPVTGASEYRTGHGPDDSQWIVVMSRPLASEGDHQVSFERDTIPVAFALWQGADAQRDGLKLVSLNWIFARMTPDAAPAPGN | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: May transfer electrons to the iron-sulfur centers of DdhB.
Sequence Mass (Da): 29499
Sequence Length: 265
Subcellular Location: Periplasm
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O46606 | MNYPGHGSPRSSERNGGRGGDGAAWELGSDTEPAFGGSVCRFDHLPVGEPGDDEVPLALLRGEPGLHLAPGAEDHNHHLALDPCLSDDNYDFSSAESGSSLRYYSEGESGGGGSSSSLHPPQQPLVPSNSGGGGAAGGGPGERKRTRPGGAAARHRYEVVTELGPEEVRWFYKEDKKTWKPFIGYDSLRIELAFRTLLQATGARARAQDPDGDHVCGPASPAGPASSSVEDEDEDRVCGFCPRIAGHGREMEELVNIERVCVRGGLYEVDVTQGECYPVYWNQSDKIPVMRGQWFIDGTWQPLEEEESNLIEQEHLSRFR... | Function: Phospholipase A1 (PLA1) that hydrolyzes ester bonds at the sn-1 position of glycerophospholipids producing a free fatty acid and a lysophospholipid . Prefers phosphatidate (1,2-diacyl-sn-glycero-3-phosphate, PA) as substrate in vitro, but can efficiently hydrolyze phosphatidylinositol (1,2-diacyl-sn-glycero-3... |
Q8NEL9 | MNYPGRGSPRSPEHNGRGGGGGAWELGSDARPAFGGGVCCFEHLPGGDPDDGDVPLALLRGEPGLHLAPGTDDHNHHLALDPCLSDENYDFSSAESGSSLRYYSEGESGGGGSSLSLHPPQQPPLVPTNSGGGGATGGSPGERKRTRLGGPAARHRYEVVTELGPEEVRWFYKEDKKTWKPFIGYDSLRIELAFRTLLQTTGARPQGGDRDGDHVCSPTGPASSSGEDDDEDRACGFCQSTTGHEPEMVELVNIEPVCVRGGLYEVDVTQGECYPVYWNQADKIPVMRGQWFIDGTWQPLEEEESNLIEQEHLNCFRGQQ... | Function: Phospholipase A1 (PLA1) that hydrolyzes ester bonds at the sn-1 position of glycerophospholipids producing a free fatty acid and a lysophospholipid . Prefers phosphatidate (1,2-diacyl-sn-glycero-3-phosphate, PA) as substrate in vitro, but can efficiently hydrolyze phosphatidylinositol (1,2-diacyl-sn-glycero-3... |
O94830 | MSSVQSQQEQLSQSDPSPSPNSCSSFELIDMDAGSLYEPVSPHWFYCKIIDSKETWIPFNSEDSQQLEEAYSSGKGCNGRVVPTDGGRYDVHLGERMRYAVYWDELASEVRRCTWFYKGDKDNKYVPYSESFSQVLEETYMLAVTLDEWKKKLESPNREIIILHNPKLMVHYQPVAGSDDWGSTPTEQGRPRTVKRGVENISVDIHCGEPLQIDHLVFVVHGIGPACDLRFRSIVQCVNDFRSVSLNLLQTHFKKAQENQQIGRVEFLPVNWHSPLHSTGVDVDLQRITLPSINRLRHFTNDTILDVFFYNSPTYCQTIV... | Function: Phospholipase that hydrolyzes preferentially phosphatidic acid, including 1,2-dioleoyl-sn-phosphatidic acid, and phosphatidylethanolamine. Specifically binds to phosphatidylinositol 3-phosphate (PI(3)P), phosphatidylinositol 4-phosphate (PI(4)P), phosphatidylinositol 5-phosphate (PI(5)P) and possibly phosphat... |
Q80Y98 | MSSGESHQEQLSQSDPSPSPNSCSSFELIDMDASSSYEPVSPHWFYCKVLDSKELWIPFNSEDSQQLEDAYGSGKDCNERIVPTDGGRYDVHLGERMRYAVYWDELPSEVRRCTWFYKGDKDNKYVPYSESFSQVLEDTYMLAVTLDEWKKKIESPNREIIVLHNPKLMVHYQPIAGSDEWGSTSTEQGRPRSVKRGVENIPVDIHCGEPLQIDHLVFVVHGIGPACDLRFRSIVQCVNDFRSVSLNLLQTHFKKAQENEQIGRVEFLPVNWHSPLHSTGVDIDLQRITLPSINRLRHFTNDTILDVFFYNSPTYCQTIV... | Function: Phospholipase that hydrolyzes preferentially phosphatidic acid, including 1,2-dioleoyl-sn-phosphatidic acid, and phosphatidylethanolamine. Specifically binds to phosphatidylinositol 3-phosphate (PI(3)P), phosphatidylinositol 4-phosphate (PI(4)P), phosphatidylinositol 5-phosphate (PI(5)P) and possibly phosphat... |
Q1EBV4 | MRITVMTAGEQIITLDVDSQETVENVKALLEVESNVPIQQQQLLYNGNEMGNSDKLSALGVKDDDLLMMMVSNASSGSATSAAGNDLGMNPDGSALNPAAFQQHIRGDSNLMGQLFQNDPELAQVISGSDLNKLQDVLRARHRQRSVLQRQKEEELALLYADPFDVEAQRKIEAAIRQKGIDENWEAALEHNPEGFARVIMLYVDMEVNGVPLKAFVDSGAQSTIISKSCAERCGLLRLMDQRYKGIAHGVGQTEILGRIHVAPIKIGNNFYPCSFVVLDSPNMEFLFGLDMLRKHQCTIDLKENVMTVGGGEVSVPFLQ... | Function: Receptor of ubiquitinated protein targeted to ubiquitin/proteasome-mediated proteolysis (UPP). Relatively weak affinity for both 'Lys-48'- and 'Lys-63'-linked ubiquitin chains with a slight preference for 'Lys-48-'linked chains of three or more ubiquitin units.
Sequence Mass (Da): 45359
Sequence Length: 414
S... |
Q754R2 | MNVTVSNEVTDELLGPFELSDDITLMDFMALIDFDENEQALWHNMRQLKSVDREKTLMQLGIVGESLVVVKAIKKKATEGSTTRASKASAKAAKAAAKAAAVARDTPAEQATTVSPVAQVPVAVSPAVTAAVPTQPTSPSGGPAAANDIITPEDEYIETFRKSLLNSPSLASNIPIPGVNQLIQDSQLFKQLIGPVLLHRRAQQQAANQMGTAQSEYVKLMSNPDDPSNQARISELINQQEIDEQLHKAMEYTPEVFASVNMLYINMEINGHPVKAFVDSGAQSTIMSTALAERTGLGRLVDKRFRGIARGVGKGEIIGR... | Function: Probable aspartic protease. May be involved in the regulation of exocytosis. Acts as a linker between the 19S proteasome and polyubiquitinated proteins via UBA domain interactions with ubiquitin for their subsequent degradation. Required for S-phase checkpoint control.
Sequence Mass (Da): 50975
Sequence Lengt... |
O51927 | MKKKIAVLLGGNSSERKISIKSGYAILQSLLRSGFNAYAIDTRDFPIMQLKKQGFDSAYIALHGTGGEDGSIQGILEYLNIPYTGSGIMSSAISLDKWRTKLLWKSLSLRVLPDIYLQKKDISKYTYSYILKKILKLKFPVVIKPNNAGSSIGITIVNHPDLLIDSINLAFNYSNNIIIEKFLKGTEYTVSILNKKVLPPIKIITKNNFYDYSSKYIESSTEYICPSGLNYQKEEELKKIVEIAWNSLGCKGCGRIDAILDNKDKFWLLEINTIPGMTHRSLVPMAAKSIGISFDELILKILKINK | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 34388
Sequence Length: 306
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.... |
Q9JSZ9 | MQNFGKVAVLMGGFSSEREISLDSGTAILNALKSKGIDAYAFDPKETPLSELKAQGFQTAFNILHGTYGEDGAVQGALELLGIPYTGSGVAASAIGMDKYRCKLIWQALGLPVPEFAVLHDDTDFDAVEEKLGLPMFVKPAAEGSSVGVVKVKGKGRLKSVYEELKHFQGEIIAERFIGGGEYSCPVLNGKGLPGIHIIPATEFYDYEAKYNRNDTIYQCPSEDLTEAEESLMRELAVRGAQAIGAEGCVRVDFLKDTDGKLYLLEINTLPGMTGHSLVPKSAAVMGVGFADLCIEILKTAHVG | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 32587
Sequence Length: 304
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.... |
Q82VS0 | MNTRDVGKVAVLLGGRSAEREISLRSGQAVLAALQRSRVNAHAFDPAGQPLENLLQQGFDRVFIALHGRYGEDGSVQGALELMELPYTGSGILASALAMDKWRTKMIWQAAGINTPDYVMLDASSRFRDVADRLGLPLIIKPAREGSTLGLNKVDNEQDFRSAYQAAAEYDSLVLAEQFIQGIELTAAILDDMPLPLVRIDVAEGLYDYQAKYFSESTRYTCPSGLSAALTTRIQEQALYAHRILGCTGWSRVDLILDENEQPFFLETNTSPGMTDHSLVPMAAKAAGISFDELVVQILELSCEH | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 33442
Sequence Length: 305
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.... |
Q2Y641 | MAGSHDFGKVAVLLGGRSAEREISLESGKAVLDALRSSGVDAHPFDPSEQHMDALLQQGYTRAHIALHGRYGEDGTVQGALELLGIPYTGSGVLASALAMDKWRTKLLWQSAGINTPRHILLDEQSDFDAVAKELGLPLIVKPSREGSTIGLSKVREAGEVAAAWHLAARHDAMVLAEQFIEGTELTASILGDVALPLVRIQVEGDLYDYQAKYLSDKTQYFCPSGVSEEQECLIRKQALQAHRLLGCEGWGRVDLILDKSGTPYFLEANTSPGMTTHSLVPMAAKAAGISFEELVLKILGLAHVG | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 32910
Sequence Length: 306
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.... |
Q3J792 | MIGRVDVKAWGKVVVLMGGYSAEREISLKSGTAVLQSLLRQGIEAHGIDVDKGVLTQLSKGQFTRAFIALHGRGGEDGVIQGVLETLNLPYTGSGVLGSALTMDKLRSKRLWRGMDLPTADFSVLTRDTNPALIAADLGLPLIVKPAREGSSLGMMKVESIEALQSAYREAVIFDTAVFAERWLPGAEYTAAILADRVLPLIRLETPRVFYDFEAKYHANTTRYFCPCGLSEKQEQDLQALALEAFQALGASGWGRVDLRCDEKAHPYLLEINTVPGMTDHSLVPMAAQAAGIEFDEMVLQILASSLERRMFQDGT | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 34489
Sequence Length: 316
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.... |
A6Q3Z7 | MQYAVVFGGKSYEHEISIVSTIAIKDIIPGAIFIFLDGNRDFYLIEKADLKSNYFSSGNYKKSPKLELKKGGFYQKSLLKEKKIPADVVINLVHGADGEDGKLASLLEFFEIDYIGPRIEGSVISYSKLLTKLYAKECGIEVLPYQLLRKQDKKIIDFEYPVIIKPNHLGSSIGVSVVYDSSELEYALDVAFEFDDEVLIEPFIEGIEEYNLAGAKGQTFHFSKIEAVKKEKLLDFEKKYLDFGRSGEVKDASLNETLRLHIRNAFEKIYDPLFSGAIIRIDFFVRDGKLYLNEINPVPGSLANYLFGDFRAVLEDVAKH... | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 38808
Sequence Length: 342
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.... |
A6NHG4 | MPFLELDTNLPANRVPAGLEKRLCAAAASILGKPADRVNVTVRPGLAMALSGSTEPCAQLSISSIGVVGTAEDNRSHSAHFFEFLTKELALGQDRFPTVLSTSPAAHGGPRCPGEIIEGKKSCLNEEALFIYFI | Function: May have lyase activity.
Sequence Mass (Da): 14195
Sequence Length: 134
Subcellular Location: Cytoplasm
EC: 4.1.1.-
|
Q54Q94 | MNKDKSKQKPQKKENNNNNNKNNNNNNNKTENNKTNKDFTKNKFDKDAKIDKVDNKKIFHNRSSQKRIAKLKKIELQKKPLTLKLNEIKSIEQRLIDEAPQRGTNPLANISSTTATTTTTTATKNDKEKEKEYKIDYPSATDFKDLPISQLTLKALTESKFLKLTDIQRASLPHTLCGRDILGAAKTGSGKTLSFILPILETLWRNRWGRDDGIGAIVLSPTRELAIQIFDVLKAVGKYHTFSAGLIIGGRNVQQEKDKINAMNILIATPGRLLQHMDETYGFDCSNLKILVLDEADRILDLGFSKCLNSIVENLPRERQ... | Function: Probable ATP-dependent RNA helicase which may be involved in ribosome biogenesis.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 100358
Sequence Length: 878
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydr... |
Q13206 | MGKTANSPGSGARPDPVRSFNRWKKKHSHRQNKKKQLRKQLKKPEWQVERESISRLMQNYEKINVNEITRFSDFPLSKKTLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYRLQWTSTDGLGVLIISPTRELAYQTFEVLRKVGKNHDFSAGLIIGGKDLKHEAERINNINILVCTPGRLLQHMDETVSFHATDLQMLVLDEADRILDMGFADTMNAVIENLPKKRQTLLFSATQTKSVKDLARLSLKNPEYVWVHEKAKYSTPATLEQNYIVCELQQKISVLYSFLRSHLKKKSIVFF... | Function: Putative ATP-dependent RNA helicase.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 100888
Sequence Length: 875
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
EC: 3.6.4.13
|
F1R345 | MESKSGRFPFPFQPYPIQESFMEALYTALDQRKVGIFESPTGTGKSLSLICGALTWLRDYEEQRKQEAARLLEGQKDSDVVKEKNSNSGPPEPDWVSEFVQKKAERDMVNKLKDEELKRKKREERLEMIRHNAQLRYAMKRKADEDDEAVKLLQLSREGAEPETHSPEEEGLIVAEYESDDEATPKSRLCDDDNDDDDDLEEEHVTKIYYCSRTHSQLAQFVHEVQKSPYGDAVRLVNLGSRQNLCINPEVVRLGNVQMMNERCLEMQKNKHEKRQKASDSESKRSRGLAKATCVFSRFENLMAMKDEVLVKVRDVEQLI... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: DNA-dependent ATPase and ATP-dependent DNA helicase that participates in various functions in genomic stability, including DNA replication, DNA repair and heterochromatin organization as well as in ribosomal RNA synthesis. Plays a role in DNA double-strand break (DSB) repai... |
Q96FC9 | MANETQKVGAIHFPFPFTPYSIQEDFMAELYRVLEAGKIGIFESPTGTGKSLSLICGALSWLRDFEQKKREEEARLLETGTGPLHDEKDESLCLSSSCEGAAGTPRPAGEPAWVTQFVQKKEERDLVDRLKAEQARRKQREERLQQLQHRVQLKYAAKRLRQEEEERENLLRLSREMLETGPEAERLEQLESGEEELVLAEYESDEEKKVASRVDEDEDDLEEEHITKIYYCSRTHSQLAQFVHEVKKSPFGKDVRLVSLGSRQNLCVNEDVKSLGSVQLINDRCVDMQRSRHEKKKGAEEEKPKRRRQEKQAACPFYNH... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: DNA-dependent ATPase and ATP-dependent DNA helicase that participates in various functions in genomic stability, including DNA replication, DNA repair and heterochromatin organization as well as in ribosomal RNA synthesis . Its double-stranded DNA helicase activity requires... |
Q6AXC6 | MADENQEIGGIHFPFPFPPYPIQKDFMAELYKVLEGGKIGIFESPTGTGKSLSLICGALSWLRDFEKKKLQAEALLLAPGSGPPSSEKNSLLTSSSCQEPTDTPRPAGEPDWVTEFVQKKEERDLVERLREEQVRRRKREERLKEVCQDGRLRFAAKRTKHEEEETEALLRLSREMLDAGTGPEQLEQLECGEEHLVLAEYESDEERRGSRVDEAEDDLEEEHITKIYYCSRTHSQLAQFVREVLKSPFGKETRLVSLGSRQTLCVNEDVKNLGSVQLMNDRCVDMQRSKREKNGTGEDKPKRKRQKIQTSCPFYNHEQM... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: DNA-dependent ATPase and ATP-dependent DNA helicase that participates in various functions in genomic stability, including DNA replication, DNA repair and heterochromatin organization as well as in ribosomal RNA synthesis. Its double-stranded DNA helicase activity requires ... |
Q54CE0 | MSYNSSNSGSGRYDDNRSGNSSYSSTSRGGSSYGNRSGSDRDYNRDGGSYNRDSSRDYNSSSGSGSGNGSSSYNKYPSSSSSSSSSSSTSSYGPSKGKDFQDSWGSSSTGTTNGYNGSSNGYNSSSNGYNSSNSSSSYGASNNGYNNSSGSSSSGSSGSSNGGSYNNSGSSNSNGYSKPTSNYSYSNGYTGPTTNYSSYSNGYSTPPTSTSTSSSSTTTTTTTTPSTSYNGGSTSYGYSTSGSSNGYGGYSQPPIPSYDPSSVSSYGAVTPASSSYNASVPGSSYGNSTYRSSGYGNQSYATTNSYGSSSYGSSGFYGNA... | Function: Probable ATP-dependent RNA helicase which may be involved nonsense-mediated mRNA decay and ribosome biogenesis through rRNA processing.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 84021
Sequence Length: 785
Domain: The Q motif is unique to and characteristic of the DEAD box fami... |
P19109 | MLKLVQYIAPRVGGATPRPTACGWGNLLLISPRSGASSEKCITQRRHFLFSSASSSGTFASSSSLCTEQRQQFHGSRRNRETILFPSTYSSLQAQSQRAFRDSSKPDSDDYVDSIPKAEQRTRTRKSLFNDPDERTEEIKIEGVMAPHDRDFGHSGRGGRGGDRGGDDRRGGGGGGNRFGGGGGGGDYHGIRNGRVEKRRDDRGGGNRFGGGGGFGDRRGGGGGGSQDLPMRPVDFSNLAPFKKNFYQEHPNVANRSPYEVQRYREEQEITVRGQVPNPIQDFSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSN... | Function: As an RNA helicase, unwinds RNA and alters RNA structures through ATP binding and hydrolysis. Involved in multiple cellular processes, including pre-mRNA splicing, alternative splicing, rRNA processing and miRNA processing, as well as transcription regulation (By similarity) . Plays a role in innate immunity.... |
Q23116 | MACKNPKKFFPIRKSPVLRDGAFKGKLVLVTGGGTGIGKAIATTFAHLRATVVIAARRMEKLEQTARDITKITGGTCEPFQMDIKDPGMVSDAFDKIDMKFGKVPEILVNNAAGNFIMATELLSSNAYGTIIDIVLKGTFNVTTELGKRCIQNKTGASITSITAGYARAGAPFIVPSAVSKAGVETMTKSLATEWSKYGLRFNAVSPGPIPTKGAWGRLNSGEMGDIAEKMKFLNPEGRVGSPEEVANLVAFISSDHMSFLNGAIIDLDGGQQHFNHGSHMGDFLHSWDHKNWEDAENLIRGRTGKEKA | Function: Auxiliary enzyme of beta-oxidation. It participates in the metabolism of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA.
Catalytic Activity: a (2E,4E)-dienoyl-CoA + H(+) + NAD... |
P18170 | MRLFSLLPLLALLVVQAAGQSEVTSDDPATDAGSTTNSTTDTKPRIPSQDEILGQMPSINPIRTGNPQMDAFYMMFPALGSLLKWGSLFPAYSILGAIPDNLQPTAAASKVVLVLADDATAKTRVARQNPPPNPLGQLMNWPALPQDFQLPSMDLGPQVGSFLAQLPAMPTVPGLLGAAAPVPAPAPAPAAAPPPAPAPAADPPAAPVPDAPQPAILGQAALQNAFTFFNPANFDASSLLGQSVPTFAPPNLDFVAQMQRQFFPGMTPAQPAAAGTDAQASDISEVRVRPEDPYSQEAQMKIKSALEMEQERQQQAQVKD... | Function: Required for proper assembly of the eggshell.
PTM: Proteolytic cleavage of isoform FC106 generates 2 further products, S80 and S60.
Sequence Mass (Da): 108371
Sequence Length: 950
Subcellular Location: Secreted
|
Q8NJQ3 | MTITGQINSETLNNGVPIFAPPYRWSKHWPRFTDVNCITIRYRTDGSSIRQYIPDNLQIEETPIVTIMLLDFGFSVIGPYHELIHCVEVTYEGKKYNYSFLLILDNEEACIGGRELLGNPKVLGTIEFDRQNRPPTAFIHGRVLRPSNTVIADIHFKPLCLVLDAGESKTPITGLNLRLIPSLIPGAPPSVREYTNVDFTLQGGEVWEGVGSLNFPSNSEFEPLHKFPVLEYLSATYHRGAWVEQRLLNVYSF | Function: Decarboxylase; part of the Tox1B locus, one of the 2 loci that mediate the biosynthesis of T-toxin, a family of linear polyketides 37 to 45 carbons in length, of which the major component is 41 carbons, and which leads to high virulence to maize . One of the PKSs (PKS1 or PKS2) could synthesize a precursor, u... |
Q6QGD6 | MIDYSGLRTIFGEKLPESHIFFATVAAHKYVPSYAFLRRELGLSSAHTNRKVWKKFVEAYGKAIPPAPPAPPLTLSKDLTASMSVEEGAALTLSVTATGGTGPYTYAWTKDGSPIPDASGATYTKPTAAAEDAGSYKVTVTDSKQVSKDSTTCAVTVNPTVPGG | Function: Decoration protein that binds asymmetrically to the center of each capsid protein hexamer after capsid expansion. Stabilizes the capsid and protects from DNA release.
Sequence Mass (Da): 17247
Sequence Length: 164
Domain: The N-terminus binds to the capsid proteins with high affinity and high cooperativity wh... |
Q9LTV6 | MDSPFKPDVVRGQVALITGGGSGIGFEISSQFGKHGASIAIMGRRKQVLDDAVSALRSLGIQAIGLEGDVRKQEDARRVVEATFQHFGKLDILVNAAAGNFLAAAEDLSPNGFRTVLDIDAVGTFNMCHAALKYLKKGAPGRDSSSGGGSIINISATLHYTASWYQIHVSAAKAAVDATTRNLALEWGTDYDIRVNGIAPGPIGGTPGMSKLVPEEIENKTREYMPLYKVGEKWDIAMAALYLSCDSGKYVSGLTMVVDGGLWLSKPRHLPKEAVKQLSRAVEKRSRAKPVGLPTSKL | Function: Auxiliary enzyme of beta-oxidation. Participates in the degradation of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in peroxisome. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA (By similarity).
Catalytic Activity: a (2E,... |
Q8PCN7 | MIREIIRMGDKRLLRVAPPVTNLGSDELHALVADMFETMDAARGVGLAAPQIAVDLQLMVFGFEASERYPEAPAVPRTALANVQIEPLSDEMENGWEGCLSIPGLRAVIPRHRVIRYSGFAPDGTPIEREAEGFHARVVQHEYDHLVGRLYPSRIENFDTFGFEDVLSYDL | 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.
Catalytic Activity: H2O... |
P35732 | MSTQFRKSNHNSHSSKKLNPALKSKIDTLTELFPDWTSDDLIDIVQEYDDLETIIDKITSGAVTRWDEVKKPAKKEKYEKKEQQHSYVPQQHLPNPEDDITYKSSNNSNSFTSTKHNSSNNYTQARNKKKVQTPRAHTTGKHVNLDKGKHVPSKPVSNTTSWAAAVSVDTKHDVPQDSNDNNNEELEAQGQQAQEKNQEKEQEEQQQQEGHNNKEEHKQIEQPSLSSKKTTSRTSASQPKKMSWAAIATPKPKAVKKTESPLENVAELKKEISDIKKDDQKSEASEEKVNEQETSAQEQEEETAEPSEENEDRVPEVDGE... | Function: Recruits the ubiquitination machinery to RNA polymerase II for polyubiquitination, removal and degradation, when the transcription-coupled repair (TCR) factor RAD26 fails to efficiently displace stalled RNA polymerase II . Also involved in telomere length regulation . Binds DNA .
PTM: Ubiquitinated at Lys-281... |
C5E4K0 | MSAQSRKSNSHNGKNSRVNPEIKFKLETLTELFPDWTNDDLIDLVHEYDDLETIIDKITSGAVTRWDEVKKPSKKERLEKRLEQQQQLQKEQQQHQLQQQHYHAQDLDGHHGGSSSHHHTKAGQGSGSRYSRDNNGTHSSSGGSNAKSKKQQQQQQQQQNGKPSLPSDNARAAISRGKPASGGGSWAAVASSDSKKHQQEEEEEEDQQQQRPESSPEEPSATTVQASETKTDGVEASASATSTAQSSTHATATASTGNAAHNEKPKKMSWAAIAAPKPKVVQKKQSSLNNVGGLKKEINEVAKETETPAAGQAQREPVSE... | Function: Recruits the ubiquitination machinery to RNA polymerase II for polyubiquitination, removal and degradation, when the transcription-coupled repair (TCR) factor RAD26 fails to efficiently displace stalled RNA polymerase II. Also involved in telomere length regulation. Binds DNA.
PTM: Ubiquitinated.
Sequence Mas... |
Q9H4E7 | MALRKELLKSIWYAFTALDVEKSGKVSKSQLKVLSHNLYTVLHIPHDPVALEEHFRDDDDGPVSSQGYMPYLNKYILDKVEEGAFVKEHFDELCWTLTAKKNYRADSNGNSMLSNQDAFRLWCLFNFLSEDKYPLIMVPDEVEYLLKKVLSSMSLEVSLGELEELLAQEAQVAQTTGGLSVWQFLELFNSGRCLRGVGRDTLSMAIHEVYQELIQDVLKQGYLWKRGHLRRNWAERWFQLQPSCLCYFGSEECKEKRGIIPLDAHCCVEVLPDRDGKRCMFCVKTANRTYEMSASDTRQRQEWTAAIQMAIRLQAEGKTS... | Function: Phosphatidylinositol 3,4,5-trisphosphate-dependent guanine nucleotide exchange factor (GEF) which plays a role in the activation of Rho GTPases RAC1, RhoA and CDC42 . Can regulate cell morphology in cooperation with activated RAC1 (By similarity). Involved in immune homeostasis by ensuring proper trafficking ... |
P80571 | GFGCPNNYQCHRHCKSIPGRCGGYCGGWHRLRCTCYRCGGRREDVEDIFDIFDNEAADRF | Function: Active against both Gram-positive and Gram-negative bacteria but is not cytotoxic towards human erythrocytes or protozoa .
PTM: The hydroxylation of the Trp-28 is not important for the antibacterial activity.
Sequence Mass (Da): 6920
Sequence Length: 60
Subcellular Location: Secreted
|
Q88VB2 | MIKMRDIIREGNHTLRAEAKQVKFPLSEADQKLANDMMEYLENSQDPELAKKYGLRAGVGLAAPQVDVSEQMAAVLVPSENEDDEPVFKDVIINPVIISHSVQPGALTEGEGCLSVDRDIAGYVIRHDRITLRYYNMAGEEKKIRLKNYPAIVCQHEIDHLHGILFYDHINGDNPFAADDDLVLIS | 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.
Catalytic Activity: H2O... |
Q72S74 | MSVRKILRMGDPILRKISEPVTEDEIQTKEFKKLIRDMFDTMRHAEGVGLAAPQIGILKQIVVVGSEDNERYPGTPDVPERIILNPVITPLTKDTSGFWEGCLSVPGMRGYVERPNQIRMQWMDEKGNQFDETIDGYKAIVYQHECDHLQGILYVDRLKDTKLFGFNETLDSSHNVLD | 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.
Catalytic Activity: H2O... |
Q0AXL3 | MSVYQVITVPNDILRGKALPVKEINAGVLRVLDNMRDTMYAADGVGLAAPQIGIPKRMIVVDIGENLLELINPEILKQEGNQLGSEGCLSVPGIVGRVNRAKKVLVKGLDRNGQELNFAAVDLLAKVLQHEIDHLEGILFIDKAIETRIEKL | 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.
Catalytic Activity: H2O... |
P96113 | MYRIRVFGDPVLRKRAKPVTKFDENLKKTIERMIETMYHYDGVGLAAPQVGISQRFFVMDVGNGPVAVINPEILEIDPETEVAEEGCLSFPEIFVEIERSKRIKVKYQNTRGEYVEEELEGYAARVFQHEFDHLNGVLIIDRISPAKRLLLRKKLMDIARTVKR | 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 (By similarity).
Catalyt... |
B0KA11 | MAIRYVRKIGDEVLRKKAKPVTEINSHILTILEDMAQTMYLNDGVGLAANQIGVLRRLVVIDVGEGLLELINPEIVYEEGEQVGAEGCLSIPGVVGEVKRPKKVKVKYLDREGKEREIEGEDLLARALCHEIDHLNGVLFIDKAIRFLDEEEKEQVKEV | 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.
Catalytic Activity: H2O... |
B9L0C1 | MAVRTIITEGDPRLRQKAIRIRVVDEEVRQLARDLWDTVRAARGLGLAAPQIGVLRRIIVVAIPPDYVEEGDPGVELTLINPEIVRASGRQVGLEGCLSIPGWYGEVPRSMHVTVKALDLDGREVRVKGSGLLARVLQHEIDHLEGILFVDRIEDRSTLRYIPDEEEETAEAATGT | 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.
Catalytic Activity: H2O... |
Q72H33 | MVYPIRLYGDPVLRRKARPVEDFSGIKRLAEDMLETMFEAKGVGLAAPQIGLSQRLFVAVEYADEPEGEEERPLRELVRRVYVVANPVITYREGLVEGTEGCLSLPGLYSEEVPRAERIRVEYQDEEGRGRVLELEGYMARVFQHEIDHLDGILFFERLPKPKREAFLEANRAELVRFQKEARALLKELSQG | 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.
Catalytic Activity: H2O... |
B5YIL7 | MAILEIKKYPDEVLKKKAETISEINGDLQKLIDNMIETMYNANGIGLAAPQVGVLKRLIVVDTSPREQNQSLIVLINPEITDSEGEILSEEGCLSLPGFTTRLKRKERVIVKGLDRNGKEIEIEATGLLARALQHEIDHLDGILLIDKISPLKRELFRKKFKTKK | 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.
Catalytic Activity: H2O... |
Q0KBD2 | MNVLITGGAGFLGLQLARLLLQRGTLNLDGQPVAIKRLTLLDVVAPQGLDDARVRVVTGDLSDPAVLRQAIDTDTGAVFHLAAVVSGQAEADFDLGMRVNLDASRALLETCRELGHQPRVLFTSSVAVYGGQLPPVVQDDTALNPQSSYGVQKAIGELLLSDYSRRGFVDGRVLRLPTISVRPGKPNAAASSFASGIIREPLSGVAANCPVAPETPLWLLSPRAAVAALVNGIELAGERLGNRRVVNLPGLSVTAAGMIEALRRVAGNAVADRVTWEREARVENIVGTWPAAWNAERALALGFQSDASFDEVIRAYMEDA... | Function: Catalyzes oxidation of D-erythronate to 2-oxo-tetronate. Can use either NAD(+) or NADP(+) as cosubstrate, with a preference for NAD(+).
Catalytic Activity: D-erythronate + NAD(+) = 2-dehydro-D-erythronate + H(+) + NADH
Sequence Mass (Da): 34270
Sequence Length: 324
EC: 1.1.1.410
|
P44094 | MKVVITGGQGFLGQRLAKTLLAQNNVHIDDLILIDVVKPIAPNNDPRVRCYEMNLRYPTGLDELITEETDAIFHLAAIVSSHAEQDPDLGYETNFLATRNILEICRKNNPKVRFIFSSSLAIFGGELPETILDSTAFTPQSTYGTQKAMCELLINDYSRKGFVDGIVVRLPTICIRPGKPNKAASSFVSSIMREPLHGEDAVCPVSEELRLWLSSPNTVVANFIHALQLPSLPLRSWHTINLPGFSVTVKQMLSDLTQVKGEAILEHIKFEFDESINNIVASWPSRIDNTQALALGFKVDSNFQNVIQQFIEYDM | Function: Catalyzes oxidation of D-erythronate to 2-oxo-tetronate. Can use either NAD(+) or NADP(+) as cosubstrate, with a preference for NAD(+).
Catalytic Activity: D-erythronate + NAD(+) = 2-dehydro-D-erythronate + H(+) + NADH
Sequence Mass (Da): 35145
Sequence Length: 315
EC: 1.1.1.410
|
P50617 | MLDGPLFSEGPDSPRELQDEESGSCLWVQKSKLLVIEVKTISCHYSRRAASRQSMDIQASYWARGPQNRTCRLRPGSPEPPPRRPWASRVLQEATNWRAGPPAEVRAREQEKRKAASQEREAKETERKRRKAGGARRSPLGQPRPELRNALRAAQPTGFPVFSRPERFGQVGRAPRPSALPQGDPGVAWAGPWGGRRPGPPSYEAHLLLRGAAGTAPRRRWDRPPPYVAPPSYEGPHRTLGTKRGPELSRAPTSSAPVPATTRTEGGRTKKRLDPRIYRDVLGAWGLRQGRGLLGGAPGCAAARARPESCKGAVEKSSGL... | Function: Promotes apoptosis of kidney glomerular podocytes. Podocytes are highly specialized cells essential to the ultrafiltration of blood, resulting in the extraction of urine and the retention of protein.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 76004
Sequence Length: 707
Subcellular Loca... |
B0TBI9 | MSNVVIIADDLTGANATGVLLARKGYKTATFLQLPQDPLENGNRFDVISITTDSRAVAPEEAYRRVAEAARAMLGNKPGLFTKRIDSTLRGNLGPEIDAMLDVLGPDSLAVVVAAFPTSGRITVGGYLLVHSIPLEQTDVARDPKTPVHQTLVADIVAAQSKHSVGFIPLATVLQGSTAVMEALGAQKEAGKRIVVMDAATQKDLDTIAHGAYLSGLSVVAVDPGPFTEALAAYVLPKPKQGRGKKVLMVVGSVTALTRQQLKAVENAYSTCFTTVDVHALIDPWRNAEEIERVSGEVLDHLDDHQVLGVRTVEEAGQVL... | Function: Catalyzes the ATP-dependent phosphorylation of D-erythronate to D-erythronate 4-phosphate. Can also phosphorylate D-threonate and 4-hydroxy-L-threonine, with lower efficiency.
Catalytic Activity: ATP + D-erythronate = 4-phospho-D-erythronate + ADP + H(+)
Sequence Mass (Da): 46168
Sequence Length: 439
EC: 2.7.... |
Q892U4 | MEIQKFIDHTILKPEATEEQVKKLCKEARDYKFASVCVNPYYTSLVSKELQGTDVKTCVVIGFPLGANTKEVKAFETKQAIENGAKEVDMVINIGALKDKKYDVVKEDIEAVVNEAKGKALVKVIIETCLLTDEEKVKACEISKEVGADFVKTSTGFSTGGAKKEDVKLMRETVGENIGVKASGGIRDYKTSLEMIEAGANRIGASAGIKIVEESK | Function: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Catalytic Activity: 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate
Sequence Mass (Da): 23516
Sequence Length: 216
Pathway: Carbohydrate degradation;... |
P0CH94 | MSSLNNEEWDLLISGKKATLQYPIPLLCYPAPEVVSIAQIIDHTQLSLSATGSQIDVLCAEAKEYGFATVCVRPDYVSRAVQYLQGTQVGVTCVIGFHEGTYSTDQKVSEAKRAMQNGASELDMVMNYPWLSEKRYTDVFQDIRAVRLAAKDAILKVILETSQLTADEIIAGCVLSSLAGADYVKTSTGFNGPGASIENVSLMSAVCDSLQSETRVKASGGIRTIEDCVKMVRAGAERLGASAGVKIVNETRLGNRQVDEPMEPTNY | Function: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Catalytic Activity: 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate
Sequence Mass (Da): 28872
Sequence Length: 267
Pathway: Carbohydrate degradation;... |
Q8FSJ0 | MTITRAEMASILDYTLLGPEVTTADLQALIDDALTLGVPTICIPPSMMNATKRAQDAGLRIATVAGFPHGKSAPLVKAAEARLAVQYGASEVDVVLDIAAVKAADDNALLAEMVAIREALASPVTLKFIVESAVVDDVALEVATHAARAAGADFIKTSTGFHPAGGATVEAVRVLAGAAQGQIGVKASGGIRTWEQAVAMVEAGATRIGTSNARAILEGAPA | Function: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Catalytic Activity: 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate
Sequence Mass (Da): 22539
Sequence Length: 222
Pathway: Carbohydrate degradation;... |
Q9RV25 | MSLASYIDHTLLKATATLADIRTLCEEAREHSFYAVCINPVFIPHARAWLEGSDVKVATVCGFPLGAISSEQKALEARLSAETGADEIDMVIHIGSALAGDWDAVEADVRAVRRAVPEQVLKVIIETCYLTDEQKRLATEVAVQGGADFVKTSTGFGTGGATVDDVRLMAEVIGGRAGLKAAGGVRTPADAQAMIEAGATRLGTSGGVGLVSGGENGAGY | Function: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Catalytic Activity: 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate
Sequence Mass (Da): 22792
Sequence Length: 220
Pathway: Carbohydrate degradation;... |
Q24SU9 | MRTMNLAGMIDHTFLKPEATEKDIVNLCHEAKQHKFATVCINPAYICTAAKLLHGSGVGVATVIGFPLGATMTEIKVQEIFAAKAHGAREVDIVINIGWAKSGNWEAVAKDITRAVEAAHCCGVTIKVIIETSLLTEEEKQKAAEIVKASGADYIKTSTGFAGGGATVEDVRNLKAWVGQSVKVKASGGIRSRETALQMVEAGADRLGTSSGVQIITV | Function: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Catalytic Activity: 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate
Sequence Mass (Da): 23020
Sequence Length: 218
Pathway: Carbohydrate degradation;... |
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