ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q1I2K4 | MKDLHWHGHATSRLARVEMNGHRPCTIWFTGLSGSGKSTIANALDGWLHRRGCHTYVLDGDNVRQGLNKDLGFSEQDRVENIRRVGEVAKLFNDAGLIVSCAFISPYEKDRHLVRQLLNEDEYVEVFLSTSLADCERRDPKGLYRKARAGELANFTGIDSPYEPPVRPNLAFDTSTHTVNEVVGAIFDYLVAKGIVRQHGAVGRASVG | Function: Catalyzes the synthesis of activated sulfate.
Catalytic Activity: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)
Sequence Mass (Da): 23147
Sequence Length: 208
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
EC: 2.7.1.25
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Q7UQW3 | MSQSNSDDSASSSTQQAGDGQDDVQQNIVWHAHTVSREDRESKLGQRGVVVWFTGLSGCGKSTIANELDRLLIDRGATCTLLDGDNVRHGLCAPPSVLKEEHGEDFAGRFGLGFGPTDREENIRRIGAVTELFASAGVIVLAAFVSPYQRDRDRVRNTIESSGRAGDFLEVFVDTPLEICKQRDPKGLYQKAIAGEIKNFTGISDPYDAPPSPEIHLKWREGQTPHDQASEIIREMEKRGVLGPAKG | Function: Catalyzes the synthesis of activated sulfate.
Catalytic Activity: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)
Sequence Mass (Da): 26990
Sequence Length: 247
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
EC: 2.7.1.25
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P25924 | MDHLPIFCQLRDRDCLIVGGGDVAERKARLLLEAGARLTVNALTFIPQFTVWANEGMLTLVEGPFDETLLDSCWLAIAATDDDTVNQRVSDAAESRRIFCNVVDAPKAASFIMPSIIDRSPLMVAVSSGGTSPVLARLLREKLESLLPQHLGQVARYAGQLRARVKKQFATMGERRRFWEKFFVNDRLAQSLANADEKAVNATTERLFSEPLDHRGEVVLVGAGPGDAGLLTLKGLQQIQQADIVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKRVVRLKGGDPFIFGRGGEELETLCHA... | Function: Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlo... |
B0SF75 | MAETKKETLAEKVKRLSRGLRGSLVDSLKDEHTGSLRSDDQLLLKFHGMYQQDDRDRRDERALKKLERLYSFMIRLRIPGGMIGPVHWEALHNVAGENSTGTIKITTRQTVQLHGILKSKIKPTIKAFDSVFLDSIAACGDVNRNVTCTSNPAASPLHKEVFGYAGEISRSLLPKTRAYYEIWLDENLLAEKEEPEDPLYKDVYLPRKFKIAIAIPPYNDVDLFTNDIGLIAIIENGQLLGFNVAVGGGLGTTHGNPDTYPRVGTVFGFIPKKDILRVVYEIVTVQRDFGNREDRKLSRLKYTLDRLGVEFYKREVEKRA... | Cofactor: Binds 1 siroheme per subunit.
Function: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate.
Catalytic Activity: 3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NA... |
B8IRY2 | MDDHKTASPPRERSYETPPAERPITDAEAARAAALSANEHIKIASGYLRGTLADGLLKHATGAISDDDGQLVKFHGMYLQDDRDLRAERTKKKLEKAYSFMIRLRIAGGVVSPKQWLALDEIARTYANGTLRATTRQTFQYHGVIKSNLKRTMQAIDAVLLDTIAACGDVNRNVMAATNPAQTGAHKAAYQLAKTISDTLLPKTNAWREIWLDGERVVGGEDEAVEPIYGKTYLPRKFKIVVAVPPSNEVDIFAHDLGFIAILDKKNKLKGWNVTVGGGMGMTHGETDTFPRTADVMAFCEPEDALKVAEAVMTVQRDWG... | Cofactor: Binds 1 siroheme per subunit.
Function: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate.
Catalytic Activity: 3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NA... |
Q93244 | MADRNSIGENAAALIGNTPMVYINKLTKGLPGTVAVKIEYMNPAGSVKDRIGAAMLAAAEKDGTVIPGVTTLIEPTSGNTGIALAFVAAAKGYRCIVTMPASMSGERRTLLKAYGSEVVLTDPAKGMKGAIDMANQLKENIPGSIILAQFDNPNNPLVHYQTTGPEIWRQTKGTVDAVVFGVGTGGTITGVGRYLQEQNPGVRVFAVEPEESAILSGRPAGPHKIQGIGAGFAPAVLDTKIYEDVIRIHSDEAIVMAQRLSYEEGLLGGISSGANVAAALQLAARPEMAGKLIVTCLPSCGERYMTSPLYTDIRESAMAL... | Function: Catalyzes the formation of cysteine and acetate from O-acetylserine and hydrogen sulfide . By metabolizing hydrogen sulfide produced by cysl-2-mediated cyanide assimilation, mediates resistance to P.aeruginosa infection . Mediates survival in high levels of hydrogen sulfide . By sequestering egl-9, which in t... |
Q9XEA6 | MGETIAKDVTELIGNTPLVYLNRVTDGCVGRVAAKLESMEPCSSVKDRIGYSMITDAEEKGLITPGKSVLIEPTSGNTGIGLAFMAAAKGYRLVLTMPASMSMERRIILKAFGAELILTDPLLGMKGAVQKAEELAAKTNNSFILQQFENPANPKIHYETTGPEIWKGTGGKVDGLVSGIGTGGTITGAGRYLREQNPDIKIYGVEPVESAVLSGGKPGPHKIQGIGAGFVPGVLDVDLINETVQVSSDEAIEMAKALALKEGLLVGISSGAAAAAAVRLAQRPENEGKLFVVVFPSFGERYLSSVLFQSIKKEAENMVV... | Catalytic Activity: hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine
Sequence Mass (Da): 33838
Sequence Length: 321
Pathway: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 2/2.
Subcellular Location: Cytoplasm
EC: 2.5.1.47
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O45679 | MSRELMVETGGELIGNTPLLKLNKIGKDLGASIAVKVEYMNPACSVKDRIAFNMIDTAEKAGLITPGKTVLIEPTSGNMGIALAYCGKLRGYKVILTMPASMSIERRCLLKAYGAEVILTDPATAVKGAVQRAEELRDVIPNAYILNQFGNPANPEAHYKTTGPEIWRQTQGKVDIVCFGVGSGGTCTGVGRFLKEKNPSVQVFPVEPFESSVINGLPHSPHKIQGMGTGMIPDILDLTLFSEALRVHSDDAIAMAKKLADEESILGGISSGANVCAAVQLAKRPENKGKLIVTTVNSFGERYLSTALYAELRDNAANMK... | Function: Primarily catalyzes the formation of cyanoalanine and hydrogen sulfide from cysteine and hydrogen cyanide. Can also catalyze, although less efficiently, the formation of cyanoalanine and hydrogen sulfide from either S-sulfocysteine or O-acetylserine and hydrogen cyanide and the formation of cysteine from eith... |
Q79FV4 | MRSRQTRDRYRLLPEGYQVTPGRNRHPGTMVGNTPVLWIPELSGTSDPDRGFWAKLEGFNPGGMKDRPALYMVECARARGDIAPGAAIVESTGGTLGLGLALAGKVYRHPVTLVTDPGLEPIIARMLTAYGAGVDMVTQPHPVGGWQQARKDRVAQLMAEYPGAWNPNQYGNPDNVGAYRSLALELVAQLGRIDVLVCSVGTGGHSAGVARVLREFNPDMRLIGVDTIGSTIFGQPASNRLMRGLGSSIYPRNVDYRAFDEVHWVAPPEAVWACRSLAATHYASGGWSVGAVALVAGWAARNLPADTTIAAVFPDGPQRY... | Function: Catalyzes the synthesis of S-sulfocysteine, utilizing O-phosphoserine (OPS) and thiosulfate as substrates. To a lesser extent, can also use sulfide as donor substrate, producing L-cysteine. CysK2 thus provides a third metabolic route to cysteine, either directly using sulfide as donor or indirectly via S-sulf... |
Q9XEA8 | MAESGQSIASDVTALIGNTPLVYLNKVVDGCEAQIAAKLEIMEPCSSVKDRIGYSMITDAEEKGLITPGKSVLIEPTSGNTGIGLAFMAAAKGYKLILTMPASMSMERRIILKAFGAELVLTDPLLGMKGAIQKADELAAKMPNSYILQQFENPANPKIHYETTGPEIWKATAGKVDILVSGIGTGGTVTGTGKYLKEQNPEIKIYGVEPTESAILSGGRPGPHKIQGIGAGFVPGVLDVNLLDEVVQVSSDEAISMAKQLALKEGLLVGISSGAAAVAAIRVAQRPENKGKLVVVVFPSFGERYLSSVLFESIKREAEN... | Catalytic Activity: hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine
Sequence Mass (Da): 34307
Sequence Length: 325
Pathway: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 2/2.
Subcellular Location: Cytoplasm
EC: 2.5.1.47
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O01592 | MSRELMVQDSGDTIGNTPLVLLRNISKGLDARIAVKVEYLNPSCSVKDRIAKSMVDEAEKAGTIVPGKTVLVEGTSGNLGIALAHIGKIRGYKVILVMPATMSVERRAMLRAYGAEVILSDPAEGHPGVIKKVEMLVDKLPNAHCLDQFSNPANPAAHYRTTGPEIWRQTEGKVDIVCFGVGSSGTVTGVGRYLREQNPNIEIYPVEPYESSVLSGLPRGPHKIQGIGAGIVPGNVDRSLFTEILRIKSDDAMQMARRLADEEAILGGISSGANVVAAVELASRPENKGKLIVTTVNSFAERYFTTELYSDVLNEVSQLT... | Function: Primarily catalyzes the formation of cysteine and acetate from O-acetylserine and hydrogen sulfide. Can also catalyze the formation of cysteine and acetate from S-sulfocysteine and hydrogen sulfide and the formation of cyanoalanine and hydrogen sulfide from either S-sulfocysteine or O-acetylserine and hydroge... |
O22682 | MAFASPSLRLLPQSPLGRITSKLHRFSTAKLSLFSFHHDSSSSLAVRTPVSSFVVGAISGKSSTGTKSKSKTKRKPPPPPPVTTVAEEQHIAESETVNIAEDVTQLIGSTPMVYLNRVTDGCLADIAAKLESMEPCRSVKDRIGLSMINEAENSGAITPRKTVLVEPTTGNTGLGIAFVAAAKGYKLIVTMPASINIERRMLLRALGAEIVLTNPEKGLKGAVDKAKEIVLKTKNAYMFQQFDNTANTKIHFETTGPEIWEDTMGNVDIFVAGIGTGGTVTGTGGFLKMMNKDIKVVGVEPSERSVISGDNPGYLPGILD... | Function: S-sulfocysteine synthase that plays an important role in chloroplast function and is essential for light-dependent redox regulation and photosynthetic performance within the chloroplast . Probably unable to interact with SAT and to form the decameric Cys synthase complex (CSC) required for O-acetylserine (thi... |
Q5BD67 | MPDHSHIYIGSAFVAGVVLTIAFKDLFYPEIEERIRDYRARHSSKSYQNASVDSLAVRHGPPAIVDGIEGCIGNTPLLRIKSLSEATGCEILAKAEFLNGAGQSSKDRVALSMIELAEERGLMTPHSGDTIYEGTSGSTGISLATLARAKGYLAHICMPSDQAIEKSNLLLKLGAIVDRVPPAPIVEKDNFVNRARALAQAHTNSTASESSVGTASQRGRGYFADQFENEANWRAHYNGTGPEIYAQCNGSLDAFVAGAGTGGTISGVALYLKPRIPNMTVVVADPQGSGLYNRVRYGVMFDTKEKEGTRRRRQVDTIVE... | Function: Putative cysteine synthase that catalyzes the conversion of O-acetyl-L-serine (OAS) into cysteine, the last step in the cysteine biosynthesis pathway. However, in contrast to cysteine synthase cysB, this CS-like protein seems not to function in cysteine biosynthesis.
Catalytic Activity: hydrogen sulfide + O-a... |
Q7SHQ1 | MSISDHPRVYGTVALTAAFAAGILVTLGFKDCYPELENRYQRRRNRNLSRSNGDYGVVVPTANRVHRESLIFGPVRLEDHEEVTSNINSSFDWVEGIEGCIGNTPLVMIRSLSEATGCVILAKAELLNGAGGSPKDRVALNMIQDAEERGLLVPGRGDTIYEGTVGSTGISLATLARAKGYKCHICMPNDMAIEKSQLLHHLGATVERVDPAPITSPDHFVNLARRRAREHEAVHADGSVGFFADQFESTANYQAHVKTTGPEIYRQTGGQLDAFVAGAGTGGTIAGVAKYLKEEKNLWETRVVLADPQGSGLFNKIRHG... | Function: Putative cysteine synthase that catalyzes the conversion of O-acetyl-L-serine (OAS) into cysteine, the last step in the cysteine biosynthesis pathway. However, in contrast to cysteine synthase cys-17, this CS-like protein may not function in cysteine biosynthesis.
Catalytic Activity: hydrogen sulfide + O-acet... |
P87131 | MAKKYQDLASGIAMGAVFMYLLRRLYESLRVKSSADSLEEDIVNGVEGLIGNTKMVRIKSLSQATGCDILAKAEFLNPGNSPKDRVALQMIRTAEENGDLVPYQSNAVYEGTAGSTGISIAMLCCSLGYDSRIYMPSDQSKEKSDILELLGAHVQRVTPAPIVDPNHFVNTARRNAANHTVDESIPGKGYFANQFENPANWQAHFNSTGPEIWRQCAGKLDAFIAGSGTGGTIAGISRYLKSKDPSITVCLADPPGSGLYHKVLHGVMFDLAEREGTRRRHQVDTIVEGVGINRMTRNFSIAEPLIDMAYRVTDEQAVAM... | Function: Putative cysteine synthase that catalyzes the conversion of O-acetyl-L-serine (OAS) into cysteine, the last step in the cysteine biosynthesis pathway. However, in contrast to cysteine synthase cys11, this CS-like protein seems not to function in cysteine biosynthesis, at least under normal growth conditions, ... |
P47999 | MAATSSSAFLLNPLTSRHRPFKYSPELSSLSLSSRKAAAFDVSSAAFTLKRQSRSDVVCKAVSIKPEAGVEGLNIADNAAQLIGKTPMVYLNNVVKGCVASVAAKLEIMEPCCSVKDRIGYSMITDAEEKGLITPGKSVLVESTSGNTGIGLAFIAASKGYKLILTMPASMSLERRVLLRAFGAELVLTEPAKGMTGAIQKAEEILKKTPNSYMLQQFDNPANPKIHYETTGPEIWEDTRGKIDILVAGIGTGGTITGVGRFIKERKPELKVIGVEPTESAILSGGKPGPHKIQGIGAGFVPKNLDLAIVDEYIAISSEE... | Function: Acts as a major cysteine synthase.
Catalytic Activity: hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine
Sequence Mass (Da): 41656
Sequence Length: 392
Pathway: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 2/2.
Subcellular Location: Plastid
EC: 2.5.1.47
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P32260 | MASLVNNAYAALRTSKLELREVKNLANFRVGPPSSLSCNNFKKVSSSPITCKAVSLSPPSTIEGLNIAEDVSQLIGKTPMVYLNNVSKGSVANIAAKLESMEPCCSVKDRIGYSMIDDAEQKGVITPGKTTLVEPTSGNTGIGLAFIAAARGYKITLTMPASMSMERRVILKAFGAELVLTDPAKGMKGAVEKAEEILKKTPDSYMLQQFDNPANPKIHYETTGPEIWEDTKGKVDIFVAGIGTGGTISGVGRYLKERNPGVQVIGIEPTESNILSGGKPGPHKIQGLGAGFVPSNLDLGVMDEVIEVSSEEAVEMAKQL... | Catalytic Activity: hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine
Sequence Mass (Da): 40637
Sequence Length: 383
Pathway: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 2/2.
Subcellular Location: Plastid
EC: 2.5.1.47
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P37887 | MVRVANSITELIGNTPIVKLNRLADENSADVYLKLEYMNPGSSVKDRIGLAMIEAAEKEGKLKAGNTIIEPTSGNTGIGLAMVAAAKGLKAILVMPDTMSMERRNLLRAYGAELVLTPGAEGMKGAIKKAEELAEKHGYFVPQQFNNPSNPEIHRQTTGKEIVEQFGDDQLDAFVAGIGTGGTITGAGEVLKEAYPSIKIYAVEPSDSPVLSGGKPGPHKIQGIGAGFVPDILNTEVYDEIFPVKNEEAFEYARRAAREEGILGGISSGAAIYAALQVAKKLGKGKKVLAIIPSNGERYLSTPLYQFD | Function: Catalyzes the conversion of O-acetylserine to cysteine. Also acts as a sensor of cysteine availability in the signal transduction pathway modulating CymR activity. When cysteine is present, the pool of O-acetylserine (OAS) is low, which leads to the formation of a CymR-CysK complex and transcriptional repress... |
C4LAG3 | MNSTIAEAIKEEGIENYLKNQQHKSLLRFLTCGSVDDGKSTLIGRLLHDSRQVYEDQLKTLHSDSQKIGTTGEKLDFALLVDGLQAEREQGITIDVAYRYFSTPKRKFIIADTPGHEQYTRNMATGASTCDLAIILIDARRGVLEQTRRHSFIASLLGIRQFIVAVNKMDLVNFDEKVFDSIKKEYLEFASGLPKTDIRVVPISALDGENLVVNSELTPWYQGEPLLTMLENAEVGTRDLDLPFRMPVQLVSRPNLDFRGYMGTVAAGVVKPGDVVKVLPSGKESKVKRIVTFDGDLDYALPGEAVTITLEDEIDISRGD... | Function: With CysD forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP... |
Q9KP20 | MNNAVKEQLAELGIEGYLNQHQHKSLLRFLTCGSVDDGKSTLIGRLLHDSKQIYEDQLAAVHNDSQRVGTTGSRPDLALLVDGLQAEREQGITIDVAYRYFSTQKRKFIIADTPGHEQYTRNMATGASTCDLAVILIDARKGVLDQTRRHSFISNLLGLKHFIVAVNKMDLVDYSQDRFEQIRAEYLEFSKHLQGETEIQIIPLSALEGDNVVEKSRLMDWYQGPSLLELLEYVDIDRDKSSGAFRFPVQYVNRPNLDFRGFAGTIASGVVKVGDKIKALPSGKTSTVTRIVTFDGDLPQAQAGLAVTLTLADEIDISRG... | Function: With CysD forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP... |
Q9YBL2 | MALADISGYLDVLDSVRGFSYLENAREVLRSGEARCLGNPRSEPEYVKALYVIGASRIPVGDGCSHTLEELGVFDISVPGEMVFPSPLDFFERGKPTPLVRSRLQLPNGVRVWLKLEWYNPFSLSVKDRPAVEIISRLSRRVEKGSLVADATSSNFGVALSAVARLYGYRARVYLPGAAEEFGKLLPRLLGAQVIVDPEAPSTVHLLPRVMKDSKNEGFVHVNQFYNDANFEAHMRGTAREIFVQSRRGGLALRGVAGSLGTSGHMSAAAFYLQSVDPSIRAVLVQPAQGDSIPGIRRVETGMLWINMLDISYTLAEVTL... | Function: Cysteine synthase that can also catalyze the synthesis of S-sulfo-L-cysteine from thiosulfate and O(3)-acetyl-L-serine, as well as the sulfhydrylation of L-serine by sulfide.
Catalytic Activity: hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine
Sequence Mass (Da): 41981
Sequence Length: 389
Pathway:... |
P0A647 | MNVTVSIPTILRPHTGGQKSVSASGDTLGAVISDLEANYSGISERLMDPSSPGKLHRFVNIYVNDEDVRFSGGLATAIADGDSVTILPAVAGG | Function: In its thiocarboxylated form (CysO-COSH), is the sulfur donor in the CysM-dependent cysteine biosynthetic pathway.
PTM: Thiocarboxylated by MoeZ.
Sequence Mass (Da): 9557
Sequence Length: 93
Pathway: Amino-acid biosynthesis; L-cysteine biosynthesis.
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P04988 | MKVILLFVLAVFTVFVSSRGIPLEEQSQFLEFQDKFNKKYSHEEYLERFEIFKSNLGKIEELNLIAINHKADTKFGVNKFADLSSDEFKNYYLNNKEAIFTDDLPVADYLDDEFINSIPTAFDWRTRGAVTPVKNQGQCGSCWSFSTTGNVEGQHFISQNKLVSLSEQNLVDCDHECMEYEGEQACDEGCNGGLQPNAYNYIIKNGGIQTESSYPYTAETGTQCNFNSANIGAKISNFTMIPKNETVMAGYIVSTGPLAIAADAVEWQFYIGGVFDIPCNPNSLDHGILIVGYSAKNTIFRKNMPYWIVKNSWGADWGEQ... | Function: Cysteine proteinases 1 and 2 are believed to participate in the breakdown of protein during differentiation of Dictyostelium as a response to starvation.
PTM: Phosphoglycosylated, contains GlcNAc-alpha-1-P-Ser residues.
Sequence Mass (Da): 38510
Sequence Length: 343
Subcellular Location: Lysosome
EC: 3.4.22.-... |
P01036 | MARPLCTLLLLMATLAGALASSSKEENRIIPGGIYDADLNDEWVQRALHFAISEYNKATEDEYYRRPLQVLRAREQTFGGVNYFFDVEVGRTICTKSQPNLDTCAFHEQPELQKKQLCSFEIYEVPWEDRMSLVNSRCQEA | Function: This protein strongly inhibits papain and ficin, partially inhibits stem bromelain and bovine cathepsin C, but does not inhibit porcine cathepsin B or clostripain. Papain is inhibited non-competitively.
PTM: Phosphorylated at both its N- and C-terminal regions.
Sequence Mass (Da): 16214
Sequence Length: 141
S... |
P35481 | MYLKVIVLFLAVTLVVESTGIPGGLVDADINDKDVQKALRFAVDHYNGQSNDAFVRKVSKVIKVQQQVAAGMKYIFTVKMEVASCKKGGVKTMCAVPKNPSIEQVIQCKITVWSQPWLNSLKVTENTCM | Function: Cysteine proteinase inhibitor.
PTM: Proteolytically processed to produce two chains linked by a disulfide bridge.
Sequence Mass (Da): 14236
Sequence Length: 129
Subcellular Location: Secreted
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Q8L493 | MAGLSLEFTVNTWNLRSLSQVPCPLRHGFRFPRRLTRRRTILMCSDSSSQSWNVPVLSSYEVGERLKLARGGQQFLAMYSSVVDGITTDPAAMVLPLDDHMVHRGHGVFDTALIINGYLYELDQHLDRILRSASMAKIPLPFDRETIKRILIQTVSVSGCRDGSLRYWLSAGPGDFLLSPSQCLKPTLYAIVIKTNFAINPIGVKVVTSSIPIKPPEFATVKSVNYLPNVLSQMEAEAKGAYAGIWVCKDGFIAEGPNMNVAFVVNGGKELVMPRFDNVLSGCTAKRTLTLAEQLVSKGILKTVKVMDVTVEDGKKADEM... | Function: Amino acid aminotransferase showing activity for D-Asp and D-Ala as amino donors with 2-oxoglutarate as an amino acceptor. Can also use D-Met, D-Tyr, D-Phe, D-Gln, D-Trp and D-Asn as substrates, but no activity with L-Asp, L-Ala, L-Leu, L-Ile or L-Val. Catalyzes also the reverse reaction where an amino group ... |
O07597 | MKVLVNGRLIGRSEASIDLEDRGYQFGDGIYEVIRVYKGVLFGLREHAERFFRSAAEIGISLPFSIEDLEWDLQKLVQENAVSEGAVYIQTTRGVAPRKHQYEAGLEPQTTAYTFTVKKPEQEQAYGVAAITDEDLRWLRCDIKSLNLLYNVMTKQRAYEAGAFEAILLRDGVVTEGTSSNVYAVINGTVRTHPANRLILNGITRMNILGLIEKNGIKLDETPVSEEELKQAEEIFISSTTAEIIPVVTLDGQSIGSGKPGPVTKQLQAAFQESIQQAASIS | Function: Acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate cofactor to form pyridoxamine and an alpha-keto acid in the first half-reaction. The second half-reaction is th... |
P19938 | MGYTLWNDQIVKDEEVKIDKEDRGYQFGDGVYEVVKVYNGEMFTVNEHIDRLYASAEKIRITIPYTKDKFHQLLHELVEKNELNTGHIYFQVTRGTSPRAHQFPENTVKPVIIGYTKENPRPLENLEKGVKATFVEDIRWLRCDIKSLNLLGAVLAKQEAHEKGCYEAILHRNNTVTEGSSSNVFGIKDGILYTHPANNMILKGITRDVVIACANEINMPVKEIPFTTHEALKMDELFVTSTTSEITPVIEIDGKLIRDGKVGEWTRKLQKQFETKIPKPLHI | Function: Acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate cofactor to form pyridoxamine and an alpha-keto acid in the first half-reaction. The second-half reaction is th... |
P0DJL9 | MKVLVNNHLVEREDATVDIEDRGYQFGDGVYEVVRLYNGKFFTYNEHIDRLYASAAKIDLVIPYSKEELRELLEKLVAENNINTGNVYLQVTRGVQNPRNHVIPDDFPLEGVLTAAAREVPRNERQFVEGGTAITEEDVRWLRCDIKSLNLLGNILAKNKAHQQNALEAILHRGEQVTECSASNVSIIKDGVLWTHAADNLILNGITRQVIIDVAKKNGIPVKEADFTLTDLREADEVFISSTTIEITPITHIDGVQVADGKRGPITAQLHQYFVEEITRACGELVFAK | Function: Acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate cofactor to form pyridoxamine and an alpha-keto acid in the first half-reaction. The second half-reaction is th... |
P54693 | MAYSLWNDQIVEEGSITISPEDRGYQFGDGIYEVIKVYNGHMFTAQEHIDRFYASAEKIRLVIPYTKDVLHKLLHDLIEKNNLNTGHVYFQITRGTTSRNHIFPDASVPAVLTGNVKTGERSIENFEKGVKATLVEDVRWLRCDIKSLNLLGAVLAKQEASEKGCYEAILHRGDIITECSSANVYGIKDGKLYTHPANNYILNGITRQVILKCAAEINLPVIEEPMTKGDLLTMDEIIVSSVSSEVTPVIDVDGQQIGAGVPGEWTRKLQKAFEAKLPISINA | Function: Acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate cofactor to form pyridoxamine and an alpha-keto acid in the first half-reaction. The second half-reaction is th... |
P63511 | MEKIFLNGEFVSPSEAKVSYNDRGYVFGDGIYEYIRVYNGKLFTVTEHYERFLRSANEIGLDLNYSVEELIELSRKLVDMNQIETGAIYIQATRGVAERNHSFPTPEVEPAIVAYTKSYDRPYDHLENGVNGVTVEDIRWLRCDIKSLNLLGNVLAKEYAVKYNAVEAIQHRGETVTEGSSSNAYAIKDGVIYTHPINNYILNGITRIVIKKIAEDYNIPFKEETFTVDFLKNADEVIVSSTSAEVTPVIKLDGEPINDGKVGPITRQLQEGFEKYIESHSI | Function: Acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate cofactor to form pyridoxamine and an alpha-keto acid in the first half-reaction. The second half-reaction is th... |
B7JB00 | MPTPATIKSYQDIKANIEGACQRIAPLWPLKHFVAVNPYVGLRDQPFWRADQTLRKITGKGLTMPRPYYEEQIANGRIIQEDLDEALKQMHSNWSVTQLKQVMKQRSASRNVPFPVFADAMFADDRRDWPGFVVERISQYCAAYFDEGQATWSMPWRDDPMYQAWLKFMHFDKSPRMVGLRGIGEAAAALPAAAETAIALALKELSVPFDLIDDYLFAALLSIGGWAGWARYLRWQAELKGETDQSLRDLLAIRVCWDAILHKTCADIAVRKQWHLMLHTQQNRAIEKPSEHVDAILQTALEIGYQRSLIKSLKEASRPS... | Function: Part of an energy-coupled inorganic carbon pump.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 92277
Sequence Length: 825
Subcellular Location: Cell inner membrane
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O67026 | MELGRKLYIRSLVNVAGEPLSYFWPMRNFVYHNPLHELEGEHFSKAIKEGEEIFKGRAFLRRKDYIDFLNKGLIKEEKLLNSLKENVNLEGAPLTYEDLLRLIKDEKLKVYENTYLIREADTDLVEKLKGFFSENPKEVMENLFSEFGKKYTIADFVDLFFGESVNRTVNELLIKLSLDFLDEGQSVVEMPRRKEGFFRAFRELAKYNLRFIIRGGRELGELMESFEEPEEAIDNILKSYGIPEELWERYITLELAKLKGIAGYIKWRSHNKHYYFQRVYPSDLVEFLAVRLILEKGILEHRKKVYPFEPTYENFKRFFE... | Function: Part of an energy-coupled inorganic carbon pump.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 118201
Sequence Length: 1007
Subcellular Location: Cell inner membrane
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C1DDM9 | MPMASGDESMSARSENPVQSARFDEATVLHELEHYLPKQAPLKDFVHHNTLHAFQDSKFHDAARNASGIFGYNLSLKLDKYRDLYHRGEITPAVLDWVVRRHKGDQSDLWKTKVVAGSFAPPPLPRIGAVRANWKKNLRIDLDSLVHPLLFRILCSYLDQGISMWTFPSGGEGFLCAIRELERHSFTSFFRRERARRLLLEQDCSIAGLLKLLVRDEALFERYLFDQQFAHPGWSGMVTVIEAQPDTLIDSRRIGLRELIVFELLLEIDALDEHFDEQWSPLEAELGGEPLDILAEVPRTELHDALAIWQEALEWSFYDP... | Function: Part of an energy-coupled inorganic carbon pump.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 95230
Sequence Length: 845
Subcellular Location: Cell inner membrane
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A7GMS5 | MSVSSVVTKESFKKKDVNMNIQEKDINDFVQSASRVIAPLWPISTFAARHPWVGLEKQSFEQVADWLKEIRDVDIYPSASMIHSAKRRGEIDESFLYAGLHRWLDSQSFHIPREKVERYCQAALKLDKLPSHLLLSKELNTLAAEINNVNTESTEDFSMQPISSLIENQDSERLANILDYHVIKWCKLYLDNFQSSWAMPNREKGFYHAWHHLIKYDPALSKQQRKALKDWPQDANAALVRALSELKIPKSKIQTYLEGHLLSLPGWAGIILWRSKQSIREHALLTEYLAVRISMEWAIVNPYLSLVNHRLKKKVSIVPL... | Function: Part of an energy-coupled inorganic carbon pump.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 99846
Sequence Length: 874
Subcellular Location: Cell membrane
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A2XSY1 | MPRATSDAKLLIQSLGKAYAATPTNLKIIDLYVVFAVATALIQVVYMGIVGSFPFNSFLSGVLSCIGTAVLAVCLRIQVNKDNKEFKDLPPERAFADFVLCNLVLHLVIMNFLG | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in ... |
Q9ZRA3 | MAKTSSTTKDAQDLFHAIWSAYSATPTNLKIIDLYVVFAVFTALLQDVYMALVGPFPFNSFLSGVLSCVGTAVLAVCLRIQVNKENKEFKDLGPERAFADFVLCNLVLHLVIMNFLG | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in ... |
O65085 | MGTSTAKEAHALIASLRSAYSATPTKLKIIDLYVVYAILTAVVQVVYMAIVGSFPFNAFLSGVLSCTGTAVLAVCLRMQVNKENREFKDLPPERAFADFVLCNLVLHLVIMNFLG | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in ... |
Q29036 | MSASVLSVISRFLEEYLSSTPQRLKLLDAYLLYILLTGALQFGYCLLVGTFPFNSFLSGFISCVGSFILAVCLRIQINPQNKADFQGISPERAFADFLFASTILHLVVMNFVG | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in ... |
Q8PUQ3 | MADIIIKNAYVLTMDPDAGDIKKGTVVIEDGKITEIGVKTKESADTVIDAKGSVVMPGLVNTHTHAAMTLFRGYADDLQLAEWLEKHIWPAEAQLTAEDVYRGSLLACLEMIRSGTTSFADMYFFMDETAKAVEASGLRASLSHGLIELWNEEKGENDLKEGKRFVRAWQGAAKGRIKTMYGPHAPNTCSDEFLAKVKEAARQDGAGLHIHVLETEAELLAMKERYGKCSVHMLDDIGFFGPDVLAAHCVWLSDGDIEVLREKGVNVSHNPISNMKLASGTAPVYKMLERGVNVSLGTDGCASNNNLDLFEEMKTAALLH... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-methylthioadenosine, to produce the inosine analogs. Can also deaminate adenosine. The preferred substrate for this enzyme is 5'-deoxyadenosine... |
O27549 | MDNESILITGPEILDAGGIRRGSVLIEDNRIADVSNTLSPGDADTVIDGTGKLLIPGLVNTHTHLSMTLFRGIADDLPLDRWLNDHIWPAEARLNGDYCYAGALLGCIEMIRSGTTSFNDMYFYMDHVARAVEEAGLRCVISHGMIDLGDTEKMTAELRESRRIIKECHGMADDRIRVALGPHSPYTCSEELLKETAALADKNDLMIHIHVSETENEVSEVSRSHGMTPVEYLDEVGVLGPRTVAAHCVWLKDWEIDVLAERDVKVSHNPSSNMKLASGVSPVARLLQRGVNVSLGTDGAASNNNLDMFQEMKTASLLQK... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-methylthioadenosine, to produce the inosine analogs. Can also deaminate adenosine. The preferred substrate for this enzyme is 5'-deoxyadenosine... |
A0B7V2 | MLIRSASIIRNGSLLKNIDILIEGNRISEVGRDLRPNDDEIIDARNMLAVPGLVNSHTHLAMTLLRGYADDMELIPWLQEKIWPLEARLKPSDVRAGVKLGCLELIRFGVTCYNDMYYFMDETAAATREMGIRGVLSGVLFDMRPEFINDVEPFIKKWRDDDLIKPAVGPHAVYTCSEETLLRAKDIAERYDVKIHIHLSETRDEVDTFVNQRHMSPVEYLENLGFLSERVVAAHCVWLTPRDIRILAERHVNVAHCPISNLKLASGIAPVATLIEHGVNVCLGTDGASSNNNLDIFEEMKVAAVVQKCSVGRSAILPAD... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-methylthioadenosine, to produce the inosine analogs. Can also deaminate adenosine. The preferred substrate for this enzyme is 5'-deoxyadenosine... |
A0A369NIV7 | MGNLTMSRRTFVKTAAITGAAAAAFGASTHTALAEETYSSVSGNDTVAVKTCCRGCGKMECGVKVIVQNGRAIRVEGDEGAFQSMGNCCTKSQSSIQAAYHPDRLHYPMKRTNPKGEEPGWQRISWDEAMQSIVDNFMDIKAKHGGEAIACQVGTSRIWCMHSESILKNMLETPNNVEAWQICKGPRHFATTMVSQFAMSWMETITRPKVYVQWGGASELSNYDDSCRTTVDVASRADVHISVDPRMANMGKEADYWQHLRPGTDGALALAWTNVIIEKKLYDELYVKKWTNAPFLVCEDMEPSGFPTVRTDGSYWDVKT... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Involved in drug metabolism, as part of an interspecies gut bacterial pathway for Levodopa (L-dopa) metabolism, acting on dopamine produced by Enterecoccus L-dopa decarboxylase. Removes the para hydroxyl group of dopamine to produce m-tyramine (3-tyramine). It is possible t... |
Q08IT1 | MWKQKGAQGNDPYLYSTNNFVGRQYWEFQPDAGTPEEREEVEKARKDYVNNKKLHGIHPCSDMLMRRQLIKESGIDLLSIPPLRLDENEQVNYDAVTTAVKKALRLNRAIQAHDGHWPAENAGSLLYTPPLIIALYISGTIDTILTKQHKKELIRFVYNHQNEDGGWGSYIEGHSTMIGSVLSYVMLRLLGEGLAESDDGNGAVERGRKWILDHGGAAGIPSWGKTYLAVLGVYEWEGCNPLPPEFWLFPSSFPFHPAKMWIYCRCTYMPMSYLYGKRYHGPITDLVLSLRQEIYNIPYEQIKWNQQRHNCCKEDLYYPH... | Function: Component of the dammarane-type triterpene saponins (e.g. ginsenosides or panaxosides) biosynthetic pathway . Oxydosqualene cyclase that produces specifically the 20S isomer of the triterpene dammarenediol II .
Catalytic Activity: dammarenediol-II = (S)-2,3-epoxysqualene + H2O
Location Topology: Single-pass m... |
B7PLT0 | MKLFLISAALVVLGLAAVADAIGCSDPSPFQGRWVIGVDKKECVALVKEKCGNLRDYTTGRWVRGQHVKSNCGSIPKFTAIATFLKPGNKYLGHAAIFESCASDGIWVYDQWNAKPVERRKIRYGNTGKPNYNGDNFYTIEL | Function: Tick gut and saliva antibacterial peptide that directly antagonizes host skin commensals which enter the ticks during feeding . Acts as a cell wall hydrolase that cleaves the bond between gamma-D-glutamate-meso-diaminopimelate of a peptide stem and D-alanine of another peptide stem in peptidoglycans . In vitr... |
P20792 | MRIRHVVFCLLALVYGAETSDDDLDERTNIFIRDKLIPALKLAEVTKVNFTRLHLCHCSREVGCNARTTGWVPGIEFLNETDRSFYENTCYTDGSCYQSARPSPEISHFGCMDEKSVTDETEFHDTAAKVCTNNTKDPHATVWICCDKGNFCANETIIHLAPGPQQSSTWLILTILALLTFIVLLGIAIFLTRKSWEAKFDWYIRFKPKPGDPLRETENNVPMVTMGDGAGSSVPEVAPIEQQGSTMSTSAGNSFPPGIMPNNMKDMLDVLEETSGSGMGPTTLHKLTIGGQIRLTGRVGSGRFGNVSRGDYRGEAVAVK... | Function: Probably involved in a TGF-beta pathway . May be a receptor for TGF-beta-like ligand daf-7 . Controls the decision of whether or not larvae enter a developmentally arrested state, known as dauer, in response to environmental conditions . Involved in regulating entry into quiescence triggered by satiety . Invo... |
Q61475 | MIRGRAPRTRPSPPPPLLPLLSLSLLLLSPTVRGDCGPPPDIPNARPILGRHSKFAEQSKVAYSCNNGFKQVPDKSNIVVCLENGQWSSHETFCEKSCVAPERLSFASLKKEYLNMNFFPVGTIVEYECRPGFRKQPPLPGKATCLEDLVWSPVAQFCKKKSCPNPKDLDNGHINIPTGILFGSEINFSCNPGYRLVGVSSTFCSVTGNTVDWDDEFPVCTEIHCPEPPKINNGIMRGESDSYTYSQVVTYSCDKGFILVGNASIYCTVSKSDVGQWSSPPPRCIEKSKVPTKKPTINVPSTGTPSTPQKPTTESVPNPG... | Function: This protein recognizes C4b and C3b fragments that condense with cell-surface hydroxyl or amino groups when nascent C4b and C3b are locally generated during C4 and c3 activation. Interaction of daf with cell-associated C4b and C3b polypeptides interferes with their ability to catalyze the conversion of C2 and... |
Q61476 | MVSSTWGYDPRAGAGDLVITTTAAGAVTIAVLLFQTVCGDCGPPPDIPNARPILGRHSKFAEQSKVAYSCNNGFKQVPDKSNIVVCLENGQWSSHETFCEKSCDTPERLSFASLKKEYFNMNFFPVGTIVEYECRPGFRKQPSLSGKSTCLEDLVWSPVAQFCKKKSCPNPKDLDNGHINIPTGILFGSEINFSCNPGYRLVGITSILCTIIGNTVDWDDEFPVCTEIFCPDPPKINNGIMRGESDSYKYSQVVIYSCDKGFILFGNSTIYCTVSKSDVGQWSSPPPQCIEESKVPIKKPVVNVPSTGIPSTPQKPTTES... | Function: This protein recognizes C4b and C3b fragments that condense with cell-surface hydroxyl or amino groups when nascent C4b and C3b are locally generated during C4 and c3 activation. Interaction of daf with cell-associated C4b and C3b polypeptides interferes with their ability to catalyze the conversion of C2 and... |
Q0ID68 | MVKVNGNYLKLKAGYLFPEIGRRVKAFSSANPEAQLIRLGIGDVTEPLPQACRDAMKSAIDEMGTAEGFHGYGPEQGYAWLREAIARDDFQARGCEISAEEIFVSDGSKCDSSNILDILGSGNRIAVTDPVYPVYVDSNVMAGRTGESGDDGRYGGLTYLPISADNGFAAQIPSEPVDLIYLCYPNNPTGAVATKAQLKKWVDYARANKALILFDAAYEAFIQDPELPHSIYEIEGARDCAIEFRSFSKNAGFTGTRCALTVVPKGLKGKADDGSEVELWGLWNRRQSTKFNGVSYIIQRGAEAVYSDAGKQEVKALVSF... | Function: Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)-2,3,4,5-tetrahydrodipicolin... |
Q55828 | MASINDNYLKLKAGYLFPEIARRVNAFTTANPNAQVIKLGIGDVTEPLPLACRQAMAKAIDDMGDRQTFKGYGPEQGYAWLREKIAQHDFQARGCEVNAEEIFISDGSKCDTGNILDIFGKDNTIAVTDPVYPVYVDTNVMAGHTGDANEKGEYGGLVYLPISAENDFVAAIPSKKVDLIYLCFPNNPTGATATKAYLKQWVDYALAHGSIIFFDAAYEAFITDPTLPHSIYEIEGARDCAIEFRSFSKNAGFTGTRCALTVVPKTLTAKAADGSDVELWKLWNRRQSTKFNGVSYIIQRGAEAVYSPEGQAQVQELIAF... | Function: Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)-2,3,4,5-tetrahydrodipicolin... |
A3DE17 | MRKPIFTGAGVAIITPFTENGVNYDKLGELIEFQIREGIDSIIICGTTGEASTMPDEEHKAVIKYTVEKVNKRVPVIAGTGSNDTIHAVELSKYAEEVGADAILSVTPYYNKTTQKGLYEHFKLIAESIKIPVVLYNVPGRTGLNIEPKTVKQLAEIENIVAIKECNINQVGEIISICPPDFTVYSGNDDMVVPLLALGGKGVISVMANIIPKKTHELVATFLDGNVEESRKIQLSLLNLIKALFIEVSPIPVKAAMNLMGMEVGKCRLPLTDMTEKNFEILKQTLKDYGLI | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 31975
Sequence Length: 292
Pathway: Ami... |
A9NGC2 | MKKFTGSGVALVTPFKGSKINYPVLQKLLDFHIENETDFLVILGTTAESPTLTSSEKKEVISFVVNYINKRIPIMVGTGSNDTKQTISFSRTAQRLGADALLIVTPYYNKPTQNGLLAHYKAVAKSINLPIMLYNVPSRTGVNLEVDTVKRLSKVKNIIGIKEASGNLEQVKSIIDQTHEDFIVLSGNDDQVYDVLSLGGHGVISVTANIIPLSTSLLIQNFRAGIDNKEAFIKFNKLHDMMFVESNPIPVKRALEHLGFEVGKPRLPLTKLGAKHNRMLLKVLRDYKLVDND | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 32475
Sequence Length: 293
Pathway: Ami... |
A0LV15 | MTTSLRPAPFGRVLTAMVTPFTADGALDLDGAARLATYLVDHGNDGLVISGTTGESPTTTDDEKERLLRAVLDAVGDRATVVAGVGTNDTRHTIELAQRAEKAGAHGLLVVTPYYSKPPQAGLLAHFRQVADATGLPVMLYDIPGRTGTAIEPETMVRLAEHERIVAVKDAKGDFEASSWVLARTDLAYYSGDDKNTLPLLAIGAVGVVGVPTHVFGTQTGAMIAAYLRGDVDGALALHRQLLPVFTGFFRTQGVILAKAALRLAGLPGGPVRPPLVDATAEQVARLREDMAAAGFTEFAEGAEERRG | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 32423
Sequence Length: 308
Pathway: Ami... |
C1F658 | MDLSGCGTALITPFRADESIDEPALRALVDWQIASGIDWLVACGTTAETPTLTHDEWLRVIRIIAEQAAGRVPVWAGCTHNATRQAVENARQAAQIPGVTAILVANPYYNKPTQQGLYEHFLAVARAVELPVVLYNIPSRTGCNLEPETVLRLVGAAPNIAAIKESSSNLPQIGELLTRAPESFRVYSGDDNMALGTIALGGAGLVSVASNEIPREMAEMVRAAVQNDWALARQLHRKYFPLLQANFLETSPGPVKAVLAMMGRIEERYRLPMTPVSSATRARLERLAGELGLLVETPVPQR | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 32754
Sequence Length: 302
Pathway: Ami... |
B9MER6 | MTSPSAPLTGSIVALVTPMHDDGSVDYPALRKLIDWHIAEGTDCIGVVGTTGESPTVNVEEHCEIIRVSVEQAAKRVPIMAGCGANSTAEAIELARFAKKVGADSQLQVVPYYNKPTQEGQYRHFKAIAEAVGDLPMVLYNVPGRSVADMQHETVLRLTQVPGIVGIKEATGNIERAQWLIRDVPKGFAVYSGDDPTAVALMLCGGQGNISVTANVAPRLMHELCVAALAGDTRRAMEIQFRLMPVHKQLFVEANPIPVKWAVQRMGLCGGALRLPMTPLSQGNEAVVEAALRAAGLL | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 31854
Sequence Length: 298
Pathway: Ami... |
Q5FKQ9 | MATLIDADLLTAIVTPFDENNKIDFSSLEKLVNYLIGQGCNGFVVGGTTGETPTLTHDEKIDLYKHFSQFVNKRVPIIAGTGSNNTAETIAFTNEVAQIEGIDYALIVVPPYNKPNQRSMVAHFSAINDATKIPFLIYNIPGRTGVKMEKETIVQLSRLDNIKGIKQCASLEEMEYIIENKDPDFQVFTGEDTQALTARLLGANGVISVASHIYANQMRRMYDSLYEGNYPLAAKIQRWLTPRMQALFMYPSPAPVKAVLNAQGLNVGGCRLPLVELNDEEKITLAQRLGLDDNALMQKLPLDLGKELEDD | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 34442
Sequence Length: 311
Pathway: Ami... |
Q9CF61 | MSAKETIEKLQNARIITALVTPFKENGQINFGAFPKLIEDLLANHTEGLILAGTTAESPTLTHDEELAIFAAVNKIVDGRIPLIAGVGTNDTRDSVEFVKEVAELGYIDAGLAVTPYYNKPSQEGIYQHFKAIATASDLPIILYNIPGRVVTEIQVETILRLAELENVIAIKECTNTDNLAYLIEKLPKDFLVYTGEDGLAFHTKALGGQGVISVASHILGQEFFEMFAEIDQGSIQKAAAIQRKILPKINALFSVTSPAPIKTVLNAKGYEVGGLRLPLVACTTEESKIILEKIGN | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 32190
Sequence Length: 297
Pathway: Ami... |
Q1MPX7 | MGQIQFQGAITALVTPFKKGEIDLECYREIIEWQIEQGINGLVSCGTTGESATLTYEEYKLLIKACVEQTKSRVPVIAGAGSNDTAKAIQLTKIAKELGADGVLHVTPYYNKPTQEGLFQHFKTIASQESIPILLYNVPGRTGCNLLPETVARIVQDIPEVVGIKDATGNLEQFSEIIEFCPIGFQVLTGDDFTILPSMILGGCGVISVISNIVPAMVVELCSLIEKNKLEEARQIHYNLAPLCRLMFVETNPIPVKTALSLMEKLELEFRLPLTELSPINFTKLESTLKNIGIISK | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 32599
Sequence Length: 297
Pathway: Ami... |
Q5ZT51 | MFSGSIVALVTPMRNDSVDVHHLRELVEFHIAKGTHALVAAGTTGEAGTLSHSEKLLVIKTVIEQAKERVPVIAGTAMNATKDCIELTQQAMEYGAHAALIMTPAYIKPTQEGLYLHYSHIAQSVAIPIILYNVPGRTACDMLPETVARLAKISNIIGIKEATGQMTRLQQILRLCEGSIDVYSGDDLTAAQWLLAGAKGVISVTANVAAKLMAKMCDLAMDDDQAGCLRIQEQLMPLHELLFVESNPIPVKWAMNKMGLIGGELRLPMTELSEKHHQALEKVLKNLELI | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 31551
Sequence Length: 290
Pathway: Ami... |
Q72U22 | MIAKSGSNQESNPMFQGVYTAIITPFKNDKIDYDSYFKLLEKQIKAGVSGVVPCGTTGESPTLSHSEHAELIRETVKAVQGKIQVVAGTGSNSTKEAIELTEAACKDGVDGILSVNPYYNKPTQEGLFQHFKSIAEHSTVPVMLYNIPGRTSVNLLPETVLRLSEVKQIRSMKEATGDLGQMGKLISLVGNKMTVLSGDDNLTLPLLAIGGVGVVSVISNLFPKALVQLVESFQQGKISEAKKIHYDFIEVFALAFMETNPIPIKAAMCWFGHCGPEIRLPLTPLSQNETSSKFKKVLEGLKEKGYE | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 33380
Sequence Length: 307
Pathway: Ami... |
Q55513 | MADFVSTSPFGPVLTAMVTPFNADGGVDYGVAEKLADHLITHGSDGLVVCGTTGESPTLSWEEEHELFRVVKQTVGDRGSVIAGTGSNCTREAMEATQIAAKLGVDGSLQVVPYYNKPPQEGLLAHFQAIANCAPELPLMLYNIPGRTGQSLAPETVYRLAEVENIVAIKEATGSLEQASLIRAHTPDDFAIYAGDDVLTLPLLAVGGAGVVSVASHLVGDRLQAMVQHFAQGATAQALEIHLQLIPLFKILFCATNPIPVKTALGLQGWPVGSFRPPLCALSPGHTEQLRDVLRDLALLP | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 31821
Sequence Length: 301
Pathway: Ami... |
Q9X1K9 | MFRGVGTAIVTPFKNGELDLESYERLVRYQLENGVNALIVLGTTGESPTVNEDEREKLVSRTLEIVDGKIPVIVGAGTNSTEKTLKLVKQAEKLGANGVLVVTPYYNKPTQEGLYQHYKYISERTDLGIVVYNVPGRTGVNVLPETAARIAADLKNVVGIKEANPDIDQIDRTVSLTKQARSDFMVWSGNDDRTFYLLCAGGDGVISVVSNVAPKQMVELCAEYFSGNLEKSREVHRKLRPLMKALFVETNPIPVKAALNLMGFIENELRLPLVPASEKTVELLRNVLKESGLL | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 32390
Sequence Length: 294
Pathway: Ami... |
B9KY71 | MLRGTFVALITPFAGEEIDEPRLRDLVDWLIANRVDGLVPCGTTGETPSLSDTEWQRVAAVVIEQAAGRVPVIVGTGTNSTMVTIQRTRVARELGATAAMVVTPYYNKPQQDGLYRHVAAIADAVDLPLVIYNVPSRTGVNLAPETARRLLDIAPVIAFKDSSGSLDQVSELVLAVGDRSSVLSGDDSLTLPIIAVGGQGVVSVLANIAPAATATMVRAALDGDLARARQLHGELFPLARALFIETNPVPVKTAAELLGLCSATVRLPLAPLAPANRERLLAALASCPHTASLLARPMGEAA | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 31674
Sequence Length: 302
Pathway: Ami... |
Q5SJQ1 | MFRGSIPPLPTPFRRGRLDEEALRRLVERVVQGGSHGVSVGGTTGEPGTQTLEERKRAIEVVLDQVAGRVPVIPGTGALRLEETLELTRFAKEAGAQGAMVIVPYYVKPNQEGLYRYFAEVARTVPDFPLLIYNIPGRAGVEIAPKTVGRLRRDFPNIVGLKHSSKDLEYLSHLFLEAGRDFLVFCGLESLTLPMMSLGAVGTIAATANWLPKEVALLCEKALAGDYQGARELHFHLLEANEAIFWDTNPIPLKTVLSWMGLLEKEWRPPLGPTTPEVEERLRRMAERYGLLPKEKEAA | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 33176
Sequence Length: 299
Pathway: Ami... |
B5YKK4 | MFKGSMVAIVTPFKKGKIDEKAFEKLIEWHIKEGTHGIVPCGTTGEASTLDYEEHYKVIEITVKVVNKRIPVIAGTGSNSTDEAIMITKKAEKLGADAALLVTPYYNKPTQEGLYRHYKEIADKTGIPLILYNVPGRTSVNILPQTVARLAEHPRIVGIKEATGDMKQVSELIRLCGDKITVLSGDDFTNLTLLALGGKGAISVTANICPKDMAELFNAWEKGDIEHARKLHYKLEPLNKAMFIETNPIPVKTALAMMGKIKEEFRLPLCEMSQTNKEKLAEVLRSAGLIK | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 32118
Sequence Length: 291
Pathway: Ami... |
B8GN57 | MFHGSMVALVTPMEADGSVSDASLAELVEFHIQKGTDAIVAVGTTGESATLDFDEHCEVIRKVVDRVAGRIPVIAGTGANSTSEAIELTRCAMQAGADACLLVTPYYNKPTQEGLYLHHKAVAEAVPIPQILYNVPGRTAVDMHNDTVVRLAEISNIVGLKDATGDLDRARDLVARCGGKIDLYSGDDATAMEFLLLGGKGVISVTANVAPAEMHQMCEAAMRGDRAAAEAINARIDLLHRNLFLEANPIPVKWALEQMGLIPPGIRLPLTRLSERFHAPVREALAAAGITLNA | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 31282
Sequence Length: 294
Pathway: Ami... |
Q42948 | MSSSIIGRCHFVADSIEAAGTKRRTTRWRSPRAAVIPSFHLPMRSNEVKNRTFADDIKALRLITAIKTPYLPDGRFDLEAYDTLVNLQIENGAEGVIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGSIKVIGNTGSNSTREAIHATEQGFAVGMHAALHINPYYGKTSLEGLISHFESVLPMGPTIIYNVPSRTGQDIPPRVIQTMAKSPNLAGVKECVGNDRVEQYTSDGVVVWSGNDDECHVSRWDYGATGVISVTSNLVPGLMRELMFGGKNPALNSKLMPLMEWLFHEPNPIALNTALAQLGVVRPVFRLPYVPLT... | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 39576
Sequence Length: 359
Pathway: Ami... |
Q8RQN0 | MAIKVGVLGAKGRVGQTIVAAVNDTDDLELVAEVDHDDDLSLLVDSGAEVVVDFTTPNAVMGNLEFCINNGISAVVGTTGFDEDRLAQVRSWCASNEGVGVLIAPNFAISAVLTMVFARQAARFFESAEVIELHHPNKLDAPSGTAIHTAQGIAEARREAGMAAQPDATEQALDGSRGADVDGIPVHAVRMSGMVAHEAVIFGTQGQTLTIKQDSYDRNSFAPGVLVGIRNIAQHPGLTVGLEHYLDL | Function: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH
Sequence Mass (Da): 26055
Sequence Length: 248
Pathway: Amino-acid biosynthesis;... |
Q4JV62 | MTRIGVLGARGRVGSAVVAAVEADANHELVAAIDHGDDLQALVDNKAEVVVDFTVPDAVMGNLEFCINNGIHAVVGTTGWTEERFETVRGWLQESPETGVLVAPNFAISAVLTMKFAEIAAPFFESAEVVELHHPNKVDAPSGTAVHTAEGIARARKAAGLAEQPDATTQSLDGARGADVQGVPVHAVRMTGMVAHEQVIFGTKGQTLTLKQDSYDRESFVPGIMIGVDKIGDNPGLTIGLEKFLGLDGDVNGGAKA | Function: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH
Sequence Mass (Da): 26873
Sequence Length: 257
Pathway: Amino-acid biosynthesis;... |
B6J2F3 | MAINVIINGINGKIGRVVKENITAQSDLELVSGTGRQDDLAKTIQTTHADVVIDFTTPQSVFHNAEIIIQSGARPVIGTTGLTLEQIALLDKQCRNKKLGAIVAPNFSVGAVLMMKYAKEAAHYFPDVEIIEMHHSQKIDAPSGTAIKTAQMIGEMRSSKKDEPFKDRARGEIKNGIPIHSIRLPGLFSHQSVIFGSNGETLTIRHDGMDRNCTMPGIFMACRKVMELDYLVYGLENLL | Function: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH
Sequence Mass (Da): 26214
Sequence Length: 239
Pathway: Amino-acid biosynthesis;... |
Q46KV7 | MSSANQSIPVLVAGAMGRMGSEVVKAINSSKDFQLVGAIDNQKDKEGQDIGSLLGLGELDVFLSSDFEGSLCAASQNVPKDGSNNGAVLVDFTHPKFAYKHTRTSIAYGVHPVIGTTGITADQLDDLSKFADKASLGSAIIPNFSVGMVLLQQAAAAAARFYEFAELTEMHHNKKADAPSGTCIKTAELIEEQRSNFNRSFVEEEESIKGSRGGSRASGLRLHSVRLPGLVAHQQVMFGSNGETYELSHNTIDRSAYMPGVLLVIKKIRSFNKLVYGLEKIL | Function: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH
Sequence Mass (Da): 30280
Sequence Length: 282
Pathway: Amino-acid biosynthesis;... |
Q5NPM9 | MTKESSVKIGLIGAAGRMGKAIQEAASQQDIQLSGGIGRKGAEFGSYNDSESLAKASDVLIDFSTAAALKDNIEAALHHKKPIIIGTTGLTEADHQLIEQAASKIPVILAANTSLGVNMLAALVKQAAAKLGSDWDIEIVEMHHRHKKDAPSGTALLLGRAAAEGRGEKLEDIADLQRCPATEPRETGRIGFASLRGGSVAGDHMVVFASEGERIELGHRAESRIIFARGALKAALWLADQSAGFYQMKDVLGL | Function: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH
Sequence Mass (Da): 26772
Sequence Length: 254
Pathway: Amino-acid biosynthesis;... |
P9WPZ4 | MTVSRLRPYATTVFAEMSALATRIGAVNLGQGFPDEDGPPKMLQAAQDAIAGGVNQYPPGPGSAPLRRAIAAQRRRHFGVDYDPETEVLVTVGATEAIAAAVLGLVEPGSEVLLIEPFYDSYSPVVAMAGAHRVTVPLVPDGRGFALDADALRRAVTPRTRALIINSPHNPTGAVLSATELAAIAEIAVAANLVVITDEVYEHLVFDHARHLPLAGFDGMAERTITISSAAKMFNCTGWKIGWACGPAELIAGVRAAKQYLSYVGGAPFQPAVALALDTEDAWVAALRNSLRARRDRLAAGLTEIGFAVHDSYGTYFLCA... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Function: Involved in the lysine biosynthetic pathways. It catalyzes the transfer of an amino group from L-glutamate to N-succinyl-2-l-amino-6-oxoheptanedioate (N-succinyl-2-l-amino-6-ketopimelate) in a PLP-dependent reaction, yielding as products N-succinyl-l-2,6-diam... |
Q5L9Q6 | MKKVRAAIVGYGNIGRYVLEALQAAPDFEIAGVVRRAGAENKPAELNDYAVVKDIKELQGVDVAILCTPTRSVEKYAKEILAMGINTVDSFDIHTGIVDLRRELGACAKEHGAVSIISAGWDPGSDSIVRTMLEAIAPKGITYTNFGPGMSMGHTVAVKAIDGVKAALSMTIPTGTGIHRRMVYIELKDGYKFEEVAAAIKSDAYFVNDETHVKQVPSVDALLDMGHGVNLTRKGVSGKTQNQLFEFNMRINNPALTAQVLVCVARASMKQQPGCYTMVEVPVIDLLPGDREEWIGHLV | Function: Catalyzes the reversible NADPH-dependent reductive amination of L-2-amino-6-oxopimelate, the acyclic form of L-tetrahydrodipicolinate, to generate the meso compound, D,L-2,6-diaminopimelate. Probably plays a role in lysine biosynthesis. Exhibits a high substrate specificity for meso-2,6-diaminopimelate (m-DAP... |
P04964 | MTNIRVAIVGYGNLGRSVEKLIAKQPDMDLVGIFSRRATLDTKTPVFDVADVDKHADDVDVLFLCMGSATDIPEQAPKFAQFACTVDTYDNHRDIPRHRQVMNEAATAAGNVALVSTGWDPGMFSINRVYAAAVLAEHQQHTFWGPGLSQGHSDALRRIPGVQKAVQYTLPSEDALEKARRGEAGDLTGKQTHKRQCFVVADAADHERIENDIRTMPDYFVGYEVEVNFIDEATFDSEHTGMPHGGHVITTGDTGGFNHTVEYILKLDRNPDFTASSQIAFGRAAHRMKQQGQSGAFTVLEVAPYLLSPENLDDLIARDV | Function: Catalyzes the reversible NADPH-dependent reductive amination of L-2-amino-6-oxopimelate, the acyclic form of L-tetrahydrodipicolinate, to generate the meso compound, D,L-2,6-diaminopimelate. Probably plays a role in lysine biosynthesis. Exhibits a high substrate specificity for meso-2,6-diaminopimelate, since... |
Q9KWR0 | MSAIRVGIVGYGNLGRGVEFAISQNPDMELVAVFTRRDPSTVSVASNASVYLVDDAEKFQDDIDVMILCGGSATDLPEQGPHFAQWFNTIDSFDTHAKIPEFFDAVDAAAQKSGKVSVISVGWDPGLFSLNRVLGEAVLPVGTTYTFWGDGLSQGHSDAVRRIEGVKNAVQYTLPIKDAVERVRNGENPELTTREKHARECWVVLEEGADAPKVEQEIVTMPNYFDEYNTTVNFISEDEFNANHTGMPHGGFVIRSGESGANDKQILEFSLKLESNPNFTSSVLVAYARAAHRLSQAGEKGAKTVFDIPFGLLSPKSAAQ... | Function: Catalyzes the reversible NADPH-dependent reductive amination of L-2-amino-6-oxopimelate, the acyclic form of L-tetrahydrodipicolinate, to generate the meso compound, D,L-2,6-diaminopimelate. Probably plays a role in lysine biosynthesis. Exhibits a high substrate specificity, since alpha-ketoglutarate, pyruvat... |
Q8EGH9 | MEALRQRIEAAFEARTDITPSTVDERVRSDVQHVINMLDKGELRVAEKIDGLWHVHQWLKKAVLLSFRIFDNAVIDGAETKYFDKVPLKFAEYDEARFKAEAIRVVPSATVRKGSFIGKNTVLMPSYVNLGAYVDEGTMVDTWATVGSCAQIGKNVHLSGGVGIGGVLEPLQAGPTIIEDNCFIGARSEIVEGVVVEEGSVISMGVYIGQSTRIYDRETGEVHYGRVPAGSVVVSGNLPSACGKYSLYAAIIVKKVDAKTRSKVGINELLRIVD | Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = (S)-2-succinylamino-6-oxoheptanedioate + CoA
Sequence Mass (Da): 29873
Sequence Length: 274
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): s... |
Q2SX11 | MSATLALTEQLIARASVTPDDQHCQQLMIERLAALGFECETIASHGVTNFWAVKRGTAGREGKLLAFAGHTDVVPTGPLEQWSSPPFVPTHRDGKLYGRGAADMKASLAGFVVAAEEFVAAHPQHRGSIGFLITSDEEGPATDGTVKVVEALAARGERLDYCIVGEPTSTATLGDVVKNGRRGSMSGELVVKGVQGHIAYPHLAKNPIHLLAPALAELAAEQWDEGNEYFPPTTWQVSNLRAGTGATNVIPGHADLLFNFRFSTASTVEGLQARVHAILDKHGLDYALNWSVSGLPFLTPRGELSNALDAAIRAETGLSP... | Cofactor: Binds 2 Zn(2+) or Co(2+) ions per subunit.
Function: Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacteria... |
Q0P9K4 | MNAKEFLIELLKFKSVTPNDDGALNFIAMELSDFEAFFIEKEGIKNLLLTKKFKDEGEHLAFGGHVDVVPAGEGWSNNAFAPVEKEGFIYARGAQDMKSGVAAFVDAAKNADFKGARLSLILTSDEEGEAIYGTKAVLEWMQERDMLPDYAVVAEPTCVKKIGDSIKIGRRGSINGKLLIRGKQGHVAYPEKCINPVHDFAPVLKLLAGFDLDPGSAEFSPSKIVITDIRGGMGVCNVTPNDLKLMFNVRNSPDTSLEDVKSYVEKICHGLNYELELKQSSEAFLTNIDNKIVQKMNESVQKITHEVPELNTKGGTSDAR... | Cofactor: Binds 2 Zn(2+) or Co(2+) ions per subunit.
Function: Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacteria... |
B0T134 | MTSPAPEPVSIDSVALAQALIRRPSVTPADEGAMDVLQRQLEALGFNCRRMKFGEIENLYARRGTERPNLCFAGHTDVVPVGDSAAWTQGPFEAEIQDGMLYGRGAVDMKSAIAAFVAAVSNLPRDLPGSLSFLITGDEEGVAEDGTVRVVQALAAEGEVIDHCIVGEPTSANLLGDMVKIGRRGSINAWIAVDGRQGHVAYPQRAANPIPVMVDILSRLQSRVLDEGYEGFQPSNLEVTTIDVGNTATNVIPASAKARINIRFNPAHQGKDLRAWIEQECRDAADGFSGRVEALCKIGGEAFLTQPGAFTDVIVAAVGD... | Cofactor: Binds 2 Zn(2+) or Co(2+) ions per subunit.
Function: Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacteria... |
B3PBB9 | MTPPATPLTPTLQLAHDLIRCRSVTPEDDGCQELMIRRLEAIGFKTERLRFGEVDNFWAIRGGDGPILAFAGHTDVVPTGPETHWNNPPFEPTIIDGMLHGRGAADMKGSLASMVVACENFVARHPNHKGRIAFLITSDEEGPSINGTVKVVEWLEARHTKMTWCIVGEPSSTTRVGDVIKNGRRGSLGGVLKVKGIQGHVAYPHLADNPIHTLAPALAELAAEHWDNGNEFFPATSFQVSNINGGTGATNVIPGEVTVVFNFRFSTELTDAILRERTQAILDKHELKYELEWILSGQPFLTPRGDLVNAVVDAINTATG... | Cofactor: Binds 2 Zn(2+) or Co(2+) ions per subunit.
Function: Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacteria... |
Q3IYS2 | MPIDPVALTADLVRCPSVTPEEGGALDLIERILSGAGFDCTRVDRNGVPNLFARWGRKGANRTFGFNGHTDVVPVGDAAAWTRDPFGGEIADGWLWGRGATDMKSGVAAFVAAAVDFVQETPPDGAVVLTITGDEEGDSTDGTVALLDWMAAEGEAMSVCLVGEPTCPERLGEMMKIGRRGSMTAFFTARGVQGHSAYPHRAKNPVAALARLIDRLSSHDLDYGTEHFDASTLAVTTFDTGNPATNVIPALCRATVNIRFNDAHSGASLTRWLEEEAARVAADTGVEIALSAKISGESFLTPPGELSELVARAVEAETGL... | Cofactor: Binds 2 Zn(2+) or Co(2+) ions per subunit.
Function: Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacteria... |
Q8R9S4 | MRFTKMHGLGNDFIVIEAVEGVDYSELAVKLCDRHFGIGADGLLVVEPSHIADIKMRIFNADGSEAEMCGNGSRCFAKYVYEKGIVSKQKMTVETLAGVIMPELFVENGKIKSVKVYMGSPIFESSKIPVKSEKQKFIDEPVKIDGKTYRLSSVRVGVPHTILFVSSFEESFMKELGPKIEKSSLFPEGTNVDFVKVEDEENISVRTWERGVGLTLACGSGASASAVVSSLLGRTRRSVNVHFKAGVLLVEWKEDNSIYLSGEVEEVFRGEIEI | 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): 30259
Sequ... |
Q9PMD8 | MKFYKYCASGNDFVITNADRKEDRSALAKELCNRYEGIGADGFIVILPHEKYDFEWEFYNNDGSRAAMCGNGSRAAAHFAHHINKINPNMSFLTGAGIIKAKVNQDKVEVSLGKIKSVQNTFEELGKTWQLCNTGVPHLVHFCQNLDEFDTMLCQKMRQKYNANVNFVKILDENHLKVRTYERGVEDETLACGTGMGACFYLAFLNKKVQNKVKITPKSGEEVGFAYKNEELFFEGKVKYCFEANYNFF | 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): 28410
Sequ... |
Q9A280 | MSRTFLKMNGLGNDFVVIQTLTEAFDPTPEQIRAIAKRPGVDGKGGIGCDQVIAIDPPRAEGASAYVRFWNSDGEVAGACGNGTRCVAWLLMQSAGKDAVAFDTVAGRLSGVAAGDKLVTVDMGPPGLDWTQIPLAEEMNTERVELQVGPIDAPLVHTPVCVSMGNPHVVFFVDAPVTDDFARGTGSLVEHHPLFPEGVNVGFAHIASRDHIRLKVWERGAGLTQACGTGACAAQVAAVRRGLTDRKARVEFDTGSLTIEWRESDGHVIMTGPITMEYAGKLPELVAA | 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): 30546
Sequ... |
Q3IZB6 | MMDMGASSGLGFMKMHGAGNDFVVIDSRGRGGALVTAGLARALGDRHRGVGFDQLAEIRDQEGADCALDFWNSDGSRSGTCGNATRCVSDYLMRDLGRDEVNLVTARGRLHARRREDGLVAVNMGAPQLLWSEIPLARAMETDSLPLEGTPSAVGMGNPHCIYFVEDAEAVDLAGRGAAVETDPLFPERTNVEFASLIGPDRLRLRVWERGAGITLACGSGACATAVAAARRGLTGRQVRLEMDGGVLEVDWRDEGVWLSGPVARVFEGHLSPEMMALA | 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): 29744
Sequ... |
Q9PJW2 | MGSFSPLMTYRYHLYSGTGNSFILGEFIPPLQHIVFLCQKEKVDGFLCVEPSEIADAKLTIFNSDGSEASMCGNGLRCVMAHVAQSLGLEDVSIETVRGVYQGKFFSMDRVLVDMTLLDWKKTKKTLTHVLPGMPEEVFFIDTGVPHVVVFVPDVNKVPVQEWGAFLRYHEDFRPNGVNVDFVQTKKEDTLLVYTYERGCERETLSCGTGMLASALVAADVFSLEQDFSLLVCSRSGNIVKIFSENGKVFLEGPVTLLNCSENIGEFAP | 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): 29864
Sequ... |
Q9ZDB7 | MINKINFVKMHGLGNDFVIVNKRDLATSYNLSHLAKNMADRHTGIGCDQCIIYEENNDFYTMIIYNIDGSSAKLCGNAIRCLAKLIYLDTGKQNITVMVGKKKLLCNVKAANKISVNVGNVSFNETWMPSRDKIWKFAERYMLDLKEMLCVDIGNPHLIIFSKLEPQDKTIIGQKLQAKELFADGVNVNFAEVKDNKIYLSVWERGAGLTLACGSGACASFAAGLKLGFVHSPSTVVFEYGNLIMREEDGNIIMQGAATFVMRGEYYYEK | 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): 30185
Sequ... |
Q21P78 | MRLRFTKMHGLGNDFVMIDAISQRVTITPERARQLADRHFGVGCDQVLVVETPDSPDADFKYRIFNHDGSEVENCGNGARCFAVFVRQRGLTAKSVITVETAVGRMVLHVQEDDQVTVDMGAPILSPADIPLAAPQQATSYTLPTQGAGDITIGAVSMGNPHAVYCVNDCKTAPVETLGPEIEAHPHFPKKVNAGFMQVVSPSEINLRVYERGAGETLACGTGACAAVVAGRLQGLLENTVKVNLPGGSLSITWEGVDSPVMMTGPATTVFHGQVKI | 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): 29528
Sequ... |
Q9UIK4 | MFQASMRSPNMEPFKQQKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAHEIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWITPVDNQQAMVRRESVVNLENFRKQYVRRRWKLSFS... | Function: Calcium/calmodulin-dependent serine/threonine kinase involved in multiple cellular signaling pathways that trigger cell survival, apoptosis, and autophagy. Regulates both type I apoptotic and type II autophagic cell death signals, depending on the cellular setting. The former is caspase-dependent, while the l... |
Q8VDF3 | MVQASMRSPNMETFKQQKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVCREEIEREVSILRQVLHPNIITLHDVYENRTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAHEIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWITPVDTQQAMVRRESVVNLENFKKQYVRRRWKLSFS... | Function: Calcium/calmodulin-dependent serine/threonine kinase involved in multiple cellular signaling pathways that trigger cell survival, apoptosis, and autophagy. Capable of regulating both type I apoptotic and type II autophagic cell death signals. The former involves caspase activation, chromatin and mitochondrial... |
O43293 | MSTFRQEDVEDHYEMGEELGSGQFAIVRKCRQKGTGKEYAAKFIKKRRLSSSRRGVSREEIEREVNILREIRHPNIITLHDIFENKTDVVLILELVSGGELFDFLAEKESLTEDEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVPNPRIKLIDFGIAHKIEAGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEYFSNTSELAKDFIRRLLVKDPKRRMTIAQSLEHSWIKAIRRRNVRGEDSGRKPERRRLKTTRLKEYTIKSHSSLPPNNSYA... | Function: Serine/threonine kinase which is involved in the regulation of apoptosis, autophagy, transcription, translation and actin cytoskeleton reorganization. Involved in the regulation of smooth muscle contraction. Regulates both type I (caspase-dependent) apoptotic and type II (caspase-independent) autophagic cell ... |
Q9NR28 | MAALKSWLSRSVTSFFRYRQCLCVPVVANFKKRCFSELIRPWHKTVTIGFGVTLCAVPIAQKSEPHSLSSEALMRRAVSLVTDSTSTFLSQTTYALIEAITEYTKAVYTLTSLYRQYTSLLGKMNSEEEDEVWQVIIGARAEMTSKHQEYLKLETTWMTAVGLSEMAAEAAYQTGADQASITARNHIQLVKLQVEEVHQLSRKAETKLAEAQIEELRQKTQEEGEERAESEQEAYLRED | Function: Promotes apoptosis by activating caspases in the cytochrome c/Apaf-1/caspase-9 pathway. Acts by opposing the inhibitory activity of inhibitor of apoptosis proteins (IAP). Inhibits the activity of BIRC6/bruce by inhibiting its binding to caspases.
PTM: Ubiquitinated by BIRC7/livin.
Sequence Mass (Da): 27131
Se... |
Q76PD3 | MSVEVDKSSHSKPKIEKKSKRNKRKWLNDENKTHVTASEAAIERLKKSASFSQAAQQALKQSRKEDNERDIEMQDVDAEAQPHDLLPIPQPSVEDFVDSKPHVKNITSVLPKWLAEPITVDPNTTVEFSSLNISSKLVERLQKQNITRGFAVQAAVLPLLLQDGRHGPMYSYGGDVCVSAATGSGKTLSYVIPIVQCLSHRTVPRLRCVVIVPTRELTVQVAKTFEYYMSGAGLQVCAWTGQKSLRHETYQLNGDENECRIDVLVSTPGRLVDHIRNDESFSLQHLRYMVIDEADRLLDQSFQDWVDTVMMEISHPKCLQ... | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 68345
Sequence Length: 604
Domain: The Q motif is unique to and characteristic of the DEAD bo... |
A7TFZ9 | MFAVRFDPSQLVEESVEDEAPKKVIPLKRSKSDEEDESSEEETESSEDEEEKEKEEVADEDSMDVDDESSGDDDEEAEEGEVDAASDHPDKHNSVMSRFQQTLALQDKMDSESLVNENEEVNDENIVESHNLERIPQPAKVKESAVAPAAVSQYKSAAWLNTETIHYDSSMVRKFSDFEDQIDPKLLKNIQQNFSTDTFPIQSILLETLLPTLNFSYNITKKNFTRRVGDVLVNASTGSGKTLAYSIPILQILSKRTVNKLRALVIVPTKLLINQVYETFNNLAQGTSLIVSISKLENSLKEENKKLLQNEPDILITTPG... | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 72193
Sequence Length: 637
Domain: The Q motif is unique to and characteristic of the DEAD bo... |
Q6CDN5 | MFTGVRRFDPTQGGQASPVPFKKVKHEEEESKPETNADEHSEVEYEEESGDDSMDEAEEAKKPVEVKDEEESEDENLTADQKRKKKQEAANLAKRAEEKALERKRKREQHMGEEDSDSEDDLAPIKISGNNKIKLAKGTIRAKGFEELPQTEIYEDKPDESATISRKTQLQTQPILRNATYVEIDDVGSFDEFDLSKNMMKNLDTLGYTKAFSVQKAVIPWLLAQQKLLAPDRKPDLLVSASTGSGKTATYGIPIIEKLRDRIVPRIRAVVVLPTKPLVMQVRDVLENLSKGSSLSVVALRNDRSTKRERAVLETADIVV... | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 68223
Sequence Length: 607
Domain: The Q motif is unique to and characteristic of the DEAD bo... |
P53734 | MFASRFDPSQLTAPAASAPEGIVGTTPPAIVPLKRQATESDNEEYGSHQDSDESSNSSSEEDEDRMQVDYGASEEDSSEVEEEESKPSTHSTVLSRFKQTVSLQERLGASDIAESKEDEGIEDEAASTHQLKQIPQPEFVKNPMNLNTNSLQFKSTGWLNTEKIYYDNSLIKPFSDYANELEAKLLQNICKNFSTNTFPIQSIILDSILPVLNFTLNVSKRNFTRRIGDILVNAATGSGKTLAYSIPIVQTLFKRQINRLRCIIIVPTKLLINQVYTTLTKLTQGTSLIVSIAKLENSLKDEHKKLSNLEPDILITTPGR... | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 70362
Sequence Length: 629
Domain: The Q motif is unique to and characteristic of the DEAD bo... |
Q4WV71 | MADDSLLLNFSLGDNNIIQPETKLKGGTWRDRLSAKKIAKHHAKGPRTAGDEDSAPRAPRNPNRIEVPSSRPTKRQRTDGGDSGKQQSHGHPHSNQPRQFISSLFTKNPEPQKAEEVKEEGHVENAKPTNAPLIDGLDTFTNLGLSPNLAAHLLTKLELKAPTAIQKASISQLLKEEGDAFIQAETGSGKTLAYLLPLVQRIMALSKPGAQTDATGQPIVHRDSGLFAIVLAPTRELCKQISVVLENLLRCAHWIVAGTVIGGEKKKSEKARLRKGLNILVATPGRLADHLDNTQALDVSNVRWLVLDEGDRLMELGFEE... | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 83357
Sequence Length: 758
Domain: The Q motif is unique to and characteristic of the DEAD bo... |
A2RA55 | MADDGLLLNFAIPDTTVLRPEKTKVKGGTWRDRLSAKKIAAHRTNNPRKEKSASNGEQNSNPRNPNRIQVSGPRPVKRQRIEDDDGNGGSQPRQQQQQHPGAPRQFVSSLFSKNPRPRNAVEEKNEAGAEVEDAKPTNAPLIDGLDTFTNLGLSAPLAAHLLTKLEVKAPTAIQKASITQLLKEESDAFIQAETGSGKTMAYLLPLVQRIMTISLNQKKREEGEQVQRDSGLFAIVLAPTRELCKQIAVVLEGLLRCAHWIVAGTVIGGEKKKSEKARLRKGLNILVATPGRLADHLENTQALDVSNVRWLVLDEGDRLM... | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 85517
Sequence Length: 771
Domain: The Q motif is unique to and characteristic of the DEAD bo... |
Q0CF43 | MADDGMLLNFTFSDDVVKKSEPKLKGGTWRDRLSAKKIAQHRAQPRKPSDGTAAPRPVKNPNRIQVSGTRPAKRQRTDDDHDAGLRDHDRAGQSQHQHQHPRQFISSLFSKNPLPRNAEEPTDEAPAEDAKPTNAPLIDGLDTFTNLGLSPTLAAHLLTKLELKAPTAIQKASISQLLKEESDAFIQAETGSGKTLAYLLPLVQRIMALSHPTNRTDATSTTDAEGQPVVHRDSGLFAIVLAPTRELCKQISVVLEGLLRCAHWIVAGTVIGGEKKKSEKARLRKGLNILVATPGRLADHLENTQALDVSNVRWLVLDEG... | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 84769
Sequence Length: 769
Domain: The Q motif is unique to and characteristic of the DEAD bo... |
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