ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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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 | MDHLPIFCQLRDRDCLIVGGGDVAERKARLLLEAGARLTVNALTFIPQFTVWANEGMLTLVEGPFDETLLDSCWLAIAATDDDTVNQRVSDAAESRRIFCNVVDAPKAASFIMPSIIDRSPLMVAVSSGGTSPVLARLLREKLESLLPQHLGQVARYAGQLRARVKKQFATMGERRRFWEKFFVNDRLAQSLANADEKAVNATTERLFSEPLDHRGEVVLVGAGPGDAGLLTLKGLQQIQQADIVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKRVVRLKGGDPFIFGRGGEELETLCHAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHLKTGGELDWENLAAEKQTLVFYMGLNQAATIQEKLIAFGMQADMPVALVENGTSVKQRVVHGVLTQLGELAQQVESPALIIVGRVVALRDKLNWFSNH | 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 sirohydrochlorin to yield siroheme.
Catalytic Activity: 2 S-adenosyl-L-methionine + uroporphyrinogen III = H(+) + precorrin-2 + 2 S-adenosyl-L-homocysteine
Sequence Mass (Da): 50147
Sequence Length: 457
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1.
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B0SF75 | MAETKKETLAEKVKRLSRGLRGSLVDSLKDEHTGSLRSDDQLLLKFHGMYQQDDRDRRDERALKKLERLYSFMIRLRIPGGMIGPVHWEALHNVAGENSTGTIKITTRQTVQLHGILKSKIKPTIKAFDSVFLDSIAACGDVNRNVTCTSNPAASPLHKEVFGYAGEISRSLLPKTRAYYEIWLDENLLAEKEEPEDPLYKDVYLPRKFKIAIAIPPYNDVDLFTNDIGLIAIIENGQLLGFNVAVGGGLGTTHGNPDTYPRVGTVFGFIPKKDILRVVYEIVTVQRDFGNREDRKLSRLKYTLDRLGVEFYKREVEKRAGISFESAKDFQFTTRSDDFGWKQDAAGNWHYTVFVENGRVCDEHGYNLKTALLEVSKTRRATFRFTCNQNLILSDIFPKDKDLIESILVKFGVHRKTAEVSPIRKNSIACVALNTCSLALAEAQRYLPSLIDKIEPILSKHGLSEEPISIRMTGCPNGCARPYISEIGLVGTSYGKYNLHVGADAEGYRLNKKYKEDLDESAILQELDGLFGKFSKDRKGKESFGDYINRIGILK | 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 NADPH + sulfite
Sequence Mass (Da): 62617
Sequence Length: 555
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1.
EC: 1.8.1.2
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B8IRY2 | MDDHKTASPPRERSYETPPAERPITDAEAARAAALSANEHIKIASGYLRGTLADGLLKHATGAISDDDGQLVKFHGMYLQDDRDLRAERTKKKLEKAYSFMIRLRIAGGVVSPKQWLALDEIARTYANGTLRATTRQTFQYHGVIKSNLKRTMQAIDAVLLDTIAACGDVNRNVMAATNPAQTGAHKAAYQLAKTISDTLLPKTNAWREIWLDGERVVGGEDEAVEPIYGKTYLPRKFKIVVAVPPSNEVDIFAHDLGFIAILDKKNKLKGWNVTVGGGMGMTHGETDTFPRTADVMAFCEPEDALKVAEAVMTVQRDWGNRKSRKNARLKYTIERYGLAAFRAEVERRVGRKLQDPKPFRFESNGDRYGWVEGEDGRHHLTLYLPSGRIKDVEGGPRYLSGLRRIAEVHQGDFRLTGNQNVIVANVPADRKSEIDALVAEYGLNLGVTALRRNSLACVALPTCGLALAESERFMPGLLTELEESLAAHGLQDEDITIRMTGCPNGCARPYIAEIGFVGRGPERYNLYLGAAFDGSRLSKLYAEDVAAKDIRATLDPLFAAYARDRQPGERFGDFVIRAGFVAKTINGPDFHDRTGALKAVA | 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 NADPH + sulfite
Sequence Mass (Da): 66374
Sequence Length: 602
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1.
EC: 1.8.1.2
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Q93244 | MADRNSIGENAAALIGNTPMVYINKLTKGLPGTVAVKIEYMNPAGSVKDRIGAAMLAAAEKDGTVIPGVTTLIEPTSGNTGIALAFVAAAKGYRCIVTMPASMSGERRTLLKAYGSEVVLTDPAKGMKGAIDMANQLKENIPGSIILAQFDNPNNPLVHYQTTGPEIWRQTKGTVDAVVFGVGTGGTITGVGRYLQEQNPGVRVFAVEPEESAILSGRPAGPHKIQGIGAGFAPAVLDTKIYEDVIRIHSDEAIVMAQRLSYEEGLLGGISSGANVAAALQLAARPEMAGKLIVTCLPSCGERYMTSPLYTDIRESAMALAVESLEANLKKLCLHNYDIME | 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 turn promotes hif-1-mediated transcription, regulates behavioral responses to hypoxia .
Catalytic Activity: hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine
Sequence Mass (Da): 35903
Sequence Length: 341
Pathway: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 2/2.
EC: 2.5.1.47
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Q9XEA6 | MGETIAKDVTELIGNTPLVYLNRVTDGCVGRVAAKLESMEPCSSVKDRIGYSMITDAEEKGLITPGKSVLIEPTSGNTGIGLAFMAAAKGYRLVLTMPASMSMERRIILKAFGAELILTDPLLGMKGAVQKAEELAAKTNNSFILQQFENPANPKIHYETTGPEIWKGTGGKVDGLVSGIGTGGTITGAGRYLREQNPDIKIYGVEPVESAVLSGGKPGPHKIQGIGAGFVPGVLDVDLINETVQVSSDEAIEMAKALALKEGLLVGISSGAAAAAAVRLAQRPENEGKLFVVVFPSFGERYLSSVLFQSIKKEAENMVVE | 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 | MSRELMVETGGELIGNTPLLKLNKIGKDLGASIAVKVEYMNPACSVKDRIAFNMIDTAEKAGLITPGKTVLIEPTSGNMGIALAYCGKLRGYKVILTMPASMSIERRCLLKAYGAEVILTDPATAVKGAVQRAEELRDVIPNAYILNQFGNPANPEAHYKTTGPEIWRQTQGKVDIVCFGVGSGGTCTGVGRFLKEKNPSVQVFPVEPFESSVINGLPHSPHKIQGMGTGMIPDILDLTLFSEALRVHSDDAIAMAKKLADEESILGGISSGANVCAAVQLAKRPENKGKLIVTTVNSFGERYLSTALYAELRDNAANMKQLNLDDSIKIAKEYLGI | 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 either S-sulfocysteine or O-acetylserine and hydrogen sulfide . By catalyzing the assimilation of cyanide produced by P.aeruginosa, mediates resistance to infection . Involved in fertility, growth and aging . Does not mediate survival in high levels of hydrogen sulfide .
Catalytic Activity: hydrogen cyanide + L-cysteine = 3-cyano-L-alanine + H(+) + hydrogen sulfide
Sequence Mass (Da): 36154
Sequence Length: 337
EC: 2.5.1.47
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Q79FV4 | MRSRQTRDRYRLLPEGYQVTPGRNRHPGTMVGNTPVLWIPELSGTSDPDRGFWAKLEGFNPGGMKDRPALYMVECARARGDIAPGAAIVESTGGTLGLGLALAGKVYRHPVTLVTDPGLEPIIARMLTAYGAGVDMVTQPHPVGGWQQARKDRVAQLMAEYPGAWNPNQYGNPDNVGAYRSLALELVAQLGRIDVLVCSVGTGGHSAGVARVLREFNPDMRLIGVDTIGSTIFGQPASNRLMRGLGSSIYPRNVDYRAFDEVHWVAPPEAVWACRSLAATHYASGGWSVGAVALVAGWAARNLPADTTIAAVFPDGPQRYFDTIYNDAYCNEHELLGGQPPTEPDEIASPLDAVVTRWTRSTTVIDPTQVVS | 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-sulfocysteine. S-sulfocysteine might also act as a signaling molecule triggering additional responses in redox defense in the pathogen upon exposure to reactive oxygen species during intracellular survival or dormancy. Cannot utilize thiocarboxylated CysO as a sulfur donor and O-acetylserine (OAS) as acceptor substrate.
Catalytic Activity: O-phospho-L-serine + thiosulfate = phosphate + S-sulfo-L-cysteine
Sequence Mass (Da): 40118
Sequence Length: 372
Pathway: Amino-acid biosynthesis; L-cysteine biosynthesis.
EC: 2.8.5.1
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Q9XEA8 | MAESGQSIASDVTALIGNTPLVYLNKVVDGCEAQIAAKLEIMEPCSSVKDRIGYSMITDAEEKGLITPGKSVLIEPTSGNTGIGLAFMAAAKGYKLILTMPASMSMERRIILKAFGAELVLTDPLLGMKGAIQKADELAAKMPNSYILQQFENPANPKIHYETTGPEIWKATAGKVDILVSGIGTGGTVTGTGKYLKEQNPEIKIYGVEPTESAILSGGRPGPHKIQGIGAGFVPGVLDVNLLDEVVQVSSDEAISMAKQLALKEGLLVGISSGAAAVAAIRVAQRPENKGKLVVVVFPSFGERYLSSVLFESIKREAENMVFEP | 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 | MSRELMVQDSGDTIGNTPLVLLRNISKGLDARIAVKVEYLNPSCSVKDRIAKSMVDEAEKAGTIVPGKTVLVEGTSGNLGIALAHIGKIRGYKVILVMPATMSVERRAMLRAYGAEVILSDPAEGHPGVIKKVEMLVDKLPNAHCLDQFSNPANPAAHYRTTGPEIWRQTEGKVDIVCFGVGSSGTVTGVGRYLREQNPNIEIYPVEPYESSVLSGLPRGPHKIQGIGAGIVPGNVDRSLFTEILRIKSDDAMQMARRLADEEAILGGISSGANVVAAVELASRPENKGKLIVTTVNSFAERYFTTELYSDVLNEVSQLTFSSDDEAMGIAKKYLGL | 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 hydrogen cyanide.
Catalytic Activity: hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine
Sequence Mass (Da): 36268
Sequence Length: 337
Pathway: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 2/2.
EC: 2.5.1.47
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O22682 | MAFASPSLRLLPQSPLGRITSKLHRFSTAKLSLFSFHHDSSSSLAVRTPVSSFVVGAISGKSSTGTKSKSKTKRKPPPPPPVTTVAEEQHIAESETVNIAEDVTQLIGSTPMVYLNRVTDGCLADIAAKLESMEPCRSVKDRIGLSMINEAENSGAITPRKTVLVEPTTGNTGLGIAFVAAAKGYKLIVTMPASINIERRMLLRALGAEIVLTNPEKGLKGAVDKAKEIVLKTKNAYMFQQFDNTANTKIHFETTGPEIWEDTMGNVDIFVAGIGTGGTVTGTGGFLKMMNKDIKVVGVEPSERSVISGDNPGYLPGILDVKLLDEVFKVSNGEAIEMARRLALEEGLLVGISSGAAAVAAVSLAKRAENAGKLITVLFPSHGERYITTALFSSINREVQEMRY | 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 (thiol)-lyase (OAS-TL) enzymatic activity . Lacks OAS-TL activity .
Catalytic Activity: O-acetyl-L-serine + thiosulfate = acetate + H(+) + S-sulfo-L-cysteine
Sequence Mass (Da): 43161
Sequence Length: 404
Subcellular Location: Plastid
EC: 2.5.1.144
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Q5BD67 | MPDHSHIYIGSAFVAGVVLTIAFKDLFYPEIEERIRDYRARHSSKSYQNASVDSLAVRHGPPAIVDGIEGCIGNTPLLRIKSLSEATGCEILAKAEFLNGAGQSSKDRVALSMIELAEERGLMTPHSGDTIYEGTSGSTGISLATLARAKGYLAHICMPSDQAIEKSNLLLKLGAIVDRVPPAPIVEKDNFVNRARALAQAHTNSTASESSVGTASQRGRGYFADQFENEANWRAHYNGTGPEIYAQCNGSLDAFVAGAGTGGTISGVALYLKPRIPNMTVVVADPQGSGLYNRVRYGVMFDTKEKEGTRRRRQVDTIVEGIGINRVTANFEAGRELVDDAVRVTDAQALAMARWLVEKDGIFAGSSSAVNCFAAVKTALKLGPGHRIVTMLSDSGSRHLSRFWAKAGNVGGAVDTKLEDVLNAKEDQ | 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-acetyl-L-serine = acetate + L-cysteine
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 45859
Sequence Length: 428
Subcellular Location: Mitochondrion outer membrane
EC: 2.5.1.47
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Q7SHQ1 | MSISDHPRVYGTVALTAAFAAGILVTLGFKDCYPELENRYQRRRNRNLSRSNGDYGVVVPTANRVHRESLIFGPVRLEDHEEVTSNINSSFDWVEGIEGCIGNTPLVMIRSLSEATGCVILAKAELLNGAGGSPKDRVALNMIQDAEERGLLVPGRGDTIYEGTVGSTGISLATLARAKGYKCHICMPNDMAIEKSQLLHHLGATVERVDPAPITSPDHFVNLARRRAREHEAVHADGSVGFFADQFESTANYQAHVKTTGPEIYRQTGGQLDAFVAGAGTGGTIAGVAKYLKEEKNLWETRVVLADPQGSGLFNKIRHGVMYSSTEREGTRRRQQVDTMVEGIGINRITENFESGRVLIDDAVRVTDEQACRMARWLVEHDGIFCGSSTAVNCVAAVVTAMKLPRGSRVVTLLCDSGNRHLSKFWKHIGDMGLENDTQAQAEDLFAELGLEELKR | 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-acetyl-L-serine = acetate + L-cysteine
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 49854
Sequence Length: 456
Subcellular Location: Mitochondrion outer membrane
EC: 2.5.1.47
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P87131 | MAKKYQDLASGIAMGAVFMYLLRRLYESLRVKSSADSLEEDIVNGVEGLIGNTKMVRIKSLSQATGCDILAKAEFLNPGNSPKDRVALQMIRTAEENGDLVPYQSNAVYEGTAGSTGISIAMLCCSLGYDSRIYMPSDQSKEKSDILELLGAHVQRVTPAPIVDPNHFVNTARRNAANHTVDESIPGKGYFANQFENPANWQAHFNSTGPEIWRQCAGKLDAFIAGSGTGGTIAGISRYLKSKDPSITVCLADPPGSGLYHKVLHGVMFDLAEREGTRRRHQVDTIVEGVGINRMTRNFSIAEPLIDMAYRVTDEQAVAMSRYLVTHDGLFVGSSSAVNCVAAVRLAKKLGPGHRIVTLLCDPGSRHFSKLYNEEFLRKKNIVPQVPSSLDFVEA | 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, although the transcript is produced.
Catalytic Activity: hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 43086
Sequence Length: 395
Subcellular Location: Mitochondrion
EC: 2.5.1.47
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P47999 | MAATSSSAFLLNPLTSRHRPFKYSPELSSLSLSSRKAAAFDVSSAAFTLKRQSRSDVVCKAVSIKPEAGVEGLNIADNAAQLIGKTPMVYLNNVVKGCVASVAAKLEIMEPCCSVKDRIGYSMITDAEEKGLITPGKSVLVESTSGNTGIGLAFIAASKGYKLILTMPASMSLERRVLLRAFGAELVLTEPAKGMTGAIQKAEEILKKTPNSYMLQQFDNPANPKIHYETTGPEIWEDTRGKIDILVAGIGTGGTITGVGRFIKERKPELKVIGVEPTESAILSGGKPGPHKIQGIGAGFVPKNLDLAIVDEYIAISSEEAIETSKQLALQEGLLVGISSGAAAAAAIQVAKRPENAGKLIAVVFPSFGERYLSTQLFQSIREECEQMQPEL | 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 | MASLVNNAYAALRTSKLELREVKNLANFRVGPPSSLSCNNFKKVSSSPITCKAVSLSPPSTIEGLNIAEDVSQLIGKTPMVYLNNVSKGSVANIAAKLESMEPCCSVKDRIGYSMIDDAEQKGVITPGKTTLVEPTSGNTGIGLAFIAAARGYKITLTMPASMSMERRVILKAFGAELVLTDPAKGMKGAVEKAEEILKKTPDSYMLQQFDNPANPKIHYETTGPEIWEDTKGKVDIFVAGIGTGGTISGVGRYLKERNPGVQVIGIEPTESNILSGGKPGPHKIQGLGAGFVPSNLDLGVMDEVIEVSSEEAVEMAKQLAMKEGLLVGISSGAAAAAAVRIGKRPENAGKLIAVVFPSFGERYLSSILFQSIREECENMKPE | 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 repression of the CymR regulon occurs. In the absence of cysteine, the OAS pool is high and the CymR-CysK complex is mostly dissociated, leading to a faster dissociation of CymR from its DNA targets and the lifting of CymR-dependent repression.
Catalytic Activity: hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine
Sequence Mass (Da): 32820
Sequence Length: 308
Pathway: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 2/2.
EC: 2.5.1.47
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C4LAG3 | MNSTIAEAIKEEGIENYLKNQQHKSLLRFLTCGSVDDGKSTLIGRLLHDSRQVYEDQLKTLHSDSQKIGTTGEKLDFALLVDGLQAEREQGITIDVAYRYFSTPKRKFIIADTPGHEQYTRNMATGASTCDLAIILIDARRGVLEQTRRHSFIASLLGIRQFIVAVNKMDLVNFDEKVFDSIKKEYLEFASGLPKTDIRVVPISALDGENLVVNSELTPWYQGEPLLTMLENAEVGTRDLDLPFRMPVQLVSRPNLDFRGYMGTVAAGVVKPGDVVKVLPSGKESKVKRIVTFDGDLDYALPGEAVTITLEDEIDISRGDLLVAPDAETQVTQHVLANVVWMTEEPLQANRQYDIKLATRKTRGHVDAIRHRIDVNTLEKHDATELKLNEIGLLELSLTNAVGVDPYNTVRDTGSFIIIDRLSNVTIGAGMVVEALAGKTAGKAEFSEFELEFNALVRKHFPHWQALDISKL | 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 hydrolysis by CysN coupled to ATP hydrolysis by CysD.
Catalytic Activity: ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate
Sequence Mass (Da): 52560
Sequence Length: 472
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3.
EC: 2.7.7.4
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Q9KP20 | MNNAVKEQLAELGIEGYLNQHQHKSLLRFLTCGSVDDGKSTLIGRLLHDSKQIYEDQLAAVHNDSQRVGTTGSRPDLALLVDGLQAEREQGITIDVAYRYFSTQKRKFIIADTPGHEQYTRNMATGASTCDLAVILIDARKGVLDQTRRHSFISNLLGLKHFIVAVNKMDLVDYSQDRFEQIRAEYLEFSKHLQGETEIQIIPLSALEGDNVVEKSRLMDWYQGPSLLELLEYVDIDRDKSSGAFRFPVQYVNRPNLDFRGFAGTIASGVVKVGDKIKALPSGKTSTVTRIVTFDGDLPQAQAGLAVTLTLADEIDISRGDLIVLESAQVDSTNHLLADVVWMTEQPLQVGRDYDIKIAGKKTVGQVKAVRHQYDINNLSTYHAESLPLNGIGLCEWTFTQTVALDKYLDCADTGGFIIIDRLTNVTVGAGLVRDSLQNITGQTESFSAFELELNALVRKHFPHWQAIDLSRLGKA | 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 hydrolysis by CysN coupled to ATP hydrolysis by CysD.
Catalytic Activity: ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate
Sequence Mass (Da): 52880
Sequence Length: 476
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3.
EC: 2.7.7.4
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Q9YBL2 | MALADISGYLDVLDSVRGFSYLENAREVLRSGEARCLGNPRSEPEYVKALYVIGASRIPVGDGCSHTLEELGVFDISVPGEMVFPSPLDFFERGKPTPLVRSRLQLPNGVRVWLKLEWYNPFSLSVKDRPAVEIISRLSRRVEKGSLVADATSSNFGVALSAVARLYGYRARVYLPGAAEEFGKLLPRLLGAQVIVDPEAPSTVHLLPRVMKDSKNEGFVHVNQFYNDANFEAHMRGTAREIFVQSRRGGLALRGVAGSLGTSGHMSAAAFYLQSVDPSIRAVLVQPAQGDSIPGIRRVETGMLWINMLDISYTLAEVTLEEAMEAVVEVARSDGLVIGPSGGAAVKALAKKAAEGDLEPGDYVVVVPDTGFKYLSLVQNALEGAGDSV | 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: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 2/2.
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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 | MKVILLFVLAVFTVFVSSRGIPLEEQSQFLEFQDKFNKKYSHEEYLERFEIFKSNLGKIEELNLIAINHKADTKFGVNKFADLSSDEFKNYYLNNKEAIFTDDLPVADYLDDEFINSIPTAFDWRTRGAVTPVKNQGQCGSCWSFSTTGNVEGQHFISQNKLVSLSEQNLVDCDHECMEYEGEQACDEGCNGGLQPNAYNYIIKNGGIQTESSYPYTAETGTQCNFNSANIGAKISNFTMIPKNETVMAGYIVSTGPLAIAADAVEWQFYIGGVFDIPCNPNSLDHGILIVGYSAKNTIFRKNMPYWIVKNSWGADWGEQGYIYLRRGKNTCGVSNFVSTSII | 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.-
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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
Subcellular Location: Secreted
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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 | MAGLSLEFTVNTWNLRSLSQVPCPLRHGFRFPRRLTRRRTILMCSDSSSQSWNVPVLSSYEVGERLKLARGGQQFLAMYSSVVDGITTDPAAMVLPLDDHMVHRGHGVFDTALIINGYLYELDQHLDRILRSASMAKIPLPFDRETIKRILIQTVSVSGCRDGSLRYWLSAGPGDFLLSPSQCLKPTLYAIVIKTNFAINPIGVKVVTSSIPIKPPEFATVKSVNYLPNVLSQMEAEAKGAYAGIWVCKDGFIAEGPNMNVAFVVNGGKELVMPRFDNVLSGCTAKRTLTLAEQLVSKGILKTVKVMDVTVEDGKKADEMMLIGSGIPIRPVIQWDEEFIGEGKEGPIAKALLDLLLEDMRSGPPSVRVLVPY | 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 is transferred from D-Glu to pyruvate or oxaloacetate to produce D-Ala or D-Asp, respectively. Also involved in folate biosynthesis, acting as an aminodeoxychorismate lyase converting 4-amino-4-deoxychorismate (ADC) to p-aminobenzoate (PABA).
Catalytic Activity: 2-oxoglutarate + D-alanine = D-glutamate + pyruvate
Sequence Mass (Da): 41065
Sequence Length: 373
Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 4-aminobenzoate from chorismate: step 2/2.
Subcellular Location: Plastid
EC: 2.6.1.21
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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 the reverse of the first, transferring the amino group from the pyridoxamine to a second alpha-keto acid to form the product D-amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essential bacterial cell wall components (By similarity).
Catalytic Activity: 2-oxoglutarate + D-alanine = D-glutamate + pyruvate
Sequence Mass (Da): 31182
Sequence Length: 282
EC: 2.6.1.21
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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 the reverse of the first, transferring the amino group from the pyridoxamine to a second alpha-keto acid to form the product D-amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essential bacterial cell wall components.
Catalytic Activity: 2-oxoglutarate + D-alanine = D-glutamate + pyruvate
Sequence Mass (Da): 32396
Sequence Length: 283
EC: 2.6.1.21
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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 the reverse of the first, transferring the amino group from the pyridoxamine to a second alpha-keto acid to form the product D-amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essential bacterial cell wall components (By similarity).
Catalytic Activity: 2-oxoglutarate + D-alanine = D-glutamate + pyruvate
Sequence Mass (Da): 32403
Sequence Length: 289
EC: 2.6.1.21
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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 the reverse of the first, transferring the amino group from the pyridoxamine to a second alpha-keto acid to form the product D-amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essential bacterial cell wall components (By similarity).
Catalytic Activity: 2-oxoglutarate + D-alanine = D-glutamate + pyruvate
Sequence Mass (Da): 31477
Sequence Length: 283
EC: 2.6.1.21
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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 the reverse of the first, transferring the amino group from the pyridoxamine to a second alpha-keto acid to form the product D-amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essential bacterial cell wall components (By similarity).
Catalytic Activity: 2-oxoglutarate + D-alanine = D-glutamate + pyruvate
Sequence Mass (Da): 31908
Sequence Length: 282
EC: 2.6.1.21
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B7JB00 | MPTPATIKSYQDIKANIEGACQRIAPLWPLKHFVAVNPYVGLRDQPFWRADQTLRKITGKGLTMPRPYYEEQIANGRIIQEDLDEALKQMHSNWSVTQLKQVMKQRSASRNVPFPVFADAMFADDRRDWPGFVVERISQYCAAYFDEGQATWSMPWRDDPMYQAWLKFMHFDKSPRMVGLRGIGEAAAALPAAAETAIALALKELSVPFDLIDDYLFAALLSIGGWAGWARYLRWQAELKGETDQSLRDLLAIRVCWDAILHKTCADIAVRKQWHLMLHTQQNRAIEKPSEHVDAILQTALEIGYQRSLIKSLKEASRPSNTVIERPVAQAAFCIDVRSEIIRRALETVAPGIQTLGFAGFFGVLMEYVPFGSNAPKGHLPVIFNPPYRVCEDLSHASEDETQRHAAKRQLRLRVATAWKSFKTSAVSTFTFVEATGLLYAPKLFGDSMGWTRTVPHPDERGLDSGTKQRLRPRLIASGNGKSSAKSTGIPETERAGVGEFILKNMGLTQTFARLILLAGHGSTTVNNPQGTGLDCGACAGQTGEASARIAVTLLNDPATRRGLEEKGLKIPKDTYFIAGLHDTTTDEVTIFDTEDLPTTHAKDLAQLRQWLADAGELTRLERATLLGTASQAPEVVTRDMRRRTRDWAEVRPEWALAGNAAFIAAPRQRTRGVDLEGRAFLHDYDWHKDAGFSTLELIMTAPMVVANWINMQYYGSMVDNLRFGSGNKVLHNVVGGSIGVLEGNGGDLRVGFALQSLHDGKRWIHEPVRLNVVIEAPQAEMESIISRHILVRELVDNGWLYLFQIDDDGSVYRRVCDKQWPRMT | 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 | MELGRKLYIRSLVNVAGEPLSYFWPMRNFVYHNPLHELEGEHFSKAIKEGEEIFKGRAFLRRKDYIDFLNKGLIKEEKLLNSLKENVNLEGAPLTYEDLLRLIKDEKLKVYENTYLIREADTDLVEKLKGFFSENPKEVMENLFSEFGKKYTIADFVDLFFGESVNRTVNELLIKLSLDFLDEGQSVVEMPRRKEGFFRAFRELAKYNLRFIIRGGRELGELMESFEEPEEAIDNILKSYGIPEELWERYITLELAKLKGIAGYIKWRSHNKHYYFQRVYPSDLVEFLAVRLILEKGILEHRKKVYPFEPTYENFKRFFEEKIEEAFLTYEYATKRVPAELSSQVRENLKNAESFINTYLSRKAHINASNFALFLKDWLGERVKELSKEELKKVLEIYGEFQEKEGFIWLEALEDSLIERLTEGVLRANQEKEKPKAQALFCIDVRSERYRRNLEKIGNYETYGIAGFFGVPMAFVEIHKGHEEFLCPVLIKPRNVVLEIPKEMKEEYEVTHLLEHILHDLKQNVLTPYVTVEAIGFLFGFDFIGKTFMPYSYSKLKEKLLESKENVDYIINKPSREEVKELVNRVYETILKRVFEHEYGIKNPEKPLLEETLKVCLGETDYSERLELYGFKGEKQREFIERLRKVYKVDRGYWNILFERLSKLGFTLDEQASLIGRALKMVGLTEFAPFVFIIGHGSKSDNNPYESALDCGACGGASGLYNAIVFCRMANNPEVRKRIKEKFGINIPENTYFVPGLHNTTTDEVHFYDLEQFPQEVKEKLKEIKEDFDKASMLTASERYKELFDEEAEDELRKIYKVVENAYDWSQVRPEWGLSGNYAFVIGRRELTKHLNLEGKVFLHSYDYRVDRRGFLLEVILSGPAIVGQWINMEYYFSTTDNEVYGSGSKVYHNVVGRFGVISGNFSDLRTGLPTQTVYKEGKPLHIPARLIILLEAPYEFALSVINRVYAIRNLIQNEWVNFVIFDPESKKFYRYKKGSWNELKTEVKDG | 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 | MPMASGDESMSARSENPVQSARFDEATVLHELEHYLPKQAPLKDFVHHNTLHAFQDSKFHDAARNASGIFGYNLSLKLDKYRDLYHRGEITPAVLDWVVRRHKGDQSDLWKTKVVAGSFAPPPLPRIGAVRANWKKNLRIDLDSLVHPLLFRILCSYLDQGISMWTFPSGGEGFLCAIRELERHSFTSFFRRERARRLLLEQDCSIAGLLKLLVRDEALFERYLFDQQFAHPGWSGMVTVIEAQPDTLIDSRRIGLRELIVFELLLEIDALDEHFDEQWSPLEAELGGEPLDILAEVPRTELHDALAIWQEALEWSFYDPVLSAIQRQPAESPALPVKSFQGLFCIDDRICSFRRHIESLDPHCETYGTPGFFGVEFYFKPENAKSHTKVCPGSIEPRYLIKETGSRDRLEAEPHFSKHSHDLLGGWVISQTLGFWSAVKLFDSILKPSASPLGASSFRHMDRASSLTILNRSPDDREDGLQIGFSVAEMAERAENLLGSIGLTQDFAPIVYVVGHGASNTNNPHYAAYDCGACSGRPGSVNARVICFMLNHPEVRAILAGKGIEIPAATQFVGALHDTTRDEIAFYDEDSLSPDSRARHRANAAVFDKALALNAKERSRRFELTDSQQSPERVHEAVKARAVSLFEPRPELNHATNALCIVGRRFLSRKLFLDRRSFLNSYDYRVDPDGRFLLGILRAAAPVCGGINLEYFFSHVDNQKLGAGSKLPHNVMGLIGVANGNDGDLRPGLPSQMIEVHHPVRMMIVVEHFPAVVLNTIRQQPATWEWFANEWLNLTVVDPETHELFRFRDGIFEPYRALTERLEVAADLEKLFETQADNLPVLALS | 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 | MSVSSVVTKESFKKKDVNMNIQEKDINDFVQSASRVIAPLWPISTFAARHPWVGLEKQSFEQVADWLKEIRDVDIYPSASMIHSAKRRGEIDESFLYAGLHRWLDSQSFHIPREKVERYCQAALKLDKLPSHLLLSKELNTLAAEINNVNTESTEDFSMQPISSLIENQDSERLANILDYHVIKWCKLYLDNFQSSWAMPNREKGFYHAWHHLIKYDPALSKQQRKALKDWPQDANAALVRALSELKIPKSKIQTYLEGHLLSLPGWAGIILWRSKQSIREHALLTEYLAVRISMEWAIVNPYLSLVNHRLKKKVSIVPLLASWIHWGDLSIEEWSQMSATEQNELLSIAHHFDEKLRRKLWWEAWEQTHAERLSQEILSKQCVNNKKKFVLAQMAFCIDVRSEPFRRQLEKAGPFETIGIAGFFGLPIATSELGSHHSHPSLPVMQKPKHRIKELASEDELKSYQQRKKVDHSLSYTFKMMKQNVLTSLLLPELSGPFLGLQMIARSFVPRRLGSFIRNLRKTWLRKPDTRFSLDYAHDTESEIPIGFSKEEKVNYVRQTLKMMGLTENFAPLVVICGHSSQSTNNPYAAALECGACGGAAGGFNARIFATLCNLPEVREGLSAEGIKIPEDTVFAAAEHKTTVDELEWIYIPELSESAREALNHIEAIMPKVSHNANRERLAQLPNFKTKMKNPRAEAHRFAEDWSEIRPEWGLARNASFIIGQRELTQDCDLEGRAFLHNYDWKQDESGDILASIIAGPGTVAQWINLQYYASTVAPHYYGSGNKATQTVTAGLGVMQGNASDLLSGVPWQSVMQSDDEAYHSPLRLLIVIQAPSQYIERLLNNDFIFREKVQNGWVRLASVDPEVGWKNW | 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 protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12379
Sequence Length: 114
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
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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 protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12880
Sequence Length: 117
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
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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 protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12514
Sequence Length: 115
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
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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 protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12511
Sequence Length: 113
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
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Q8PUQ3 | MADIIIKNAYVLTMDPDAGDIKKGTVVIEDGKITEIGVKTKESADTVIDAKGSVVMPGLVNTHTHAAMTLFRGYADDLQLAEWLEKHIWPAEAQLTAEDVYRGSLLACLEMIRSGTTSFADMYFFMDETAKAVEASGLRASLSHGLIELWNEEKGENDLKEGKRFVRAWQGAAKGRIKTMYGPHAPNTCSDEFLAKVKEAARQDGAGLHIHVLETEAELLAMKERYGKCSVHMLDDIGFFGPDVLAAHCVWLSDGDIEVLREKGVNVSHNPISNMKLASGTAPVYKMLERGVNVSLGTDGCASNNNLDLFEEMKTAALLHKLSTCNPTALPARQVLQMATVNGAKALGTETGMLKTGMKADMIIVDMKKPHLTPCFDVPSHLVYSAGGSDVRTTIVDGKILMQDYRVMVLDEQKVIEEAQKAAEELVARVNS | 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, but all these substrates are efficiently deaminated. Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions. May also be involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens.
Catalytic Activity: 5'-deoxyadenosine + H(+) + H2O = 5'-deoxyinosine + NH4(+)
Sequence Mass (Da): 47085
Sequence Length: 432
Pathway: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis.
EC: 3.5.4.41
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O27549 | MDNESILITGPEILDAGGIRRGSVLIEDNRIADVSNTLSPGDADTVIDGTGKLLIPGLVNTHTHLSMTLFRGIADDLPLDRWLNDHIWPAEARLNGDYCYAGALLGCIEMIRSGTTSFNDMYFYMDHVARAVEEAGLRCVISHGMIDLGDTEKMTAELRESRRIIKECHGMADDRIRVALGPHSPYTCSEELLKETAALADKNDLMIHIHVSETENEVSEVSRSHGMTPVEYLDEVGVLGPRTVAAHCVWLKDWEIDVLAERDVKVSHNPSSNMKLASGVSPVARLLQRGVNVSLGTDGAASNNNLDMFQEMKTASLLQKVNLEDPTALPAMDVFSMATLNGARALGIDAGLIAPGKLADIVILNTRRPHLTPWRNPPSHTVYSASGADVDTVICDGRILLRDGELEVLEEKYVMELAEAAAAELTG | 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, but all these substrates are efficiently deaminated. Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions. May also be involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens.
Catalytic Activity: 5'-deoxyadenosine + H(+) + H2O = 5'-deoxyinosine + NH4(+)
Sequence Mass (Da): 46442
Sequence Length: 427
Pathway: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis.
EC: 3.5.4.41
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A0B7V2 | MLIRSASIIRNGSLLKNIDILIEGNRISEVGRDLRPNDDEIIDARNMLAVPGLVNSHTHLAMTLLRGYADDMELIPWLQEKIWPLEARLKPSDVRAGVKLGCLELIRFGVTCYNDMYYFMDETAAATREMGIRGVLSGVLFDMRPEFINDVEPFIKKWRDDDLIKPAVGPHAVYTCSEETLLRAKDIAERYDVKIHIHLSETRDEVDTFVNQRHMSPVEYLENLGFLSERVVAAHCVWLTPRDIRILAERHVNVAHCPISNLKLASGIAPVATLIEHGVNVCLGTDGASSNNNLDIFEEMKVAAVVQKCSVGRSAILPADAVWRMATENAYKAFSLDMGIRRGALADLALINMRRPWFIPVTSMISHLVYSMSGEASYTICNGRVLMRDGVIEGEAKILDEAQRCYERLISEE | 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, but all these substrates are efficiently deaminated. Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions. May also be involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens.
Catalytic Activity: 5'-deoxyadenosine + H(+) + H2O = 5'-deoxyinosine + NH4(+)
Sequence Mass (Da): 46382
Sequence Length: 413
Pathway: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis.
EC: 3.5.4.41
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A0A369NIV7 | MGNLTMSRRTFVKTAAITGAAAAAFGASTHTALAEETYSSVSGNDTVAVKTCCRGCGKMECGVKVIVQNGRAIRVEGDEGAFQSMGNCCTKSQSSIQAAYHPDRLHYPMKRTNPKGEEPGWQRISWDEAMQSIVDNFMDIKAKHGGEAIACQVGTSRIWCMHSESILKNMLETPNNVEAWQICKGPRHFATTMVSQFAMSWMETITRPKVYVQWGGASELSNYDDSCRTTVDVASRADVHISVDPRMANMGKEADYWQHLRPGTDGALALAWTNVIIEKKLYDELYVKKWTNAPFLVCEDMEPSGFPTVRTDGSYWDVKTALLKESDIKEGGSPYKFLVYDNNWEKLKAEGVEHEYGAFTWFNADQEGVIDETGGFWEGENYDSEKARQGREAAQDNLLPGQTQGWLPDPMPFDPAIDPALEGEFEITLKDGKTVKVKPVWEHYKARAAEYKPEVAAEITGIPASEIEAAATAYGTRIDPSTGYGNGGIQYMLAVEHFCSAIQNCRAFDNLVGITGNMDTPGGNRGPTIVPIDGDLQGFSAWAPGATTPPEEVNRKQIGIDKFPLLGWWQYWCDSHSLWDAVITGDPYPVRALWNESGNFMSQTNTTRAWEALCSLDFYVDLNLWHTPQNDTADIILPVAHWIELNSPRASQGSAGAMGATVKCVQPPAEAKYDPEIVMDLARRMNWKWTDEPGNEWPDINWQLDDSIKLLTDDELTYTTWHVENGKPTFERHGVPMAEVTPKYKTWDEYVKAFQEHGWWQAKDIEPRNWGTYRRYQTGAMRARDRVWGRLDYTAGKGIGDWKPGWFTPTMKQEIWSTVMESHHPDHPEWRLPTYTEPPHGPKDGDRIKEYPLTATTGRRIPVYFHSEHRQLPWCRELWPVPRVEINPKTAAEYGIEQGDWVWIETEWGKIREVADLYYGVKEDVINLEHTWWYPEVKDAGHGWQFSQVNQLIDHYAQDPHSGTSNLRAYQVKIYKATPENSPFNNPVPCDSTGTPIIHTSDDPRLKEWLPTYEGRE | 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 that dopamine dehydroxylation influences the multiple side effects of L-dopa administration linked to dopamine production in the treatment of Parkinson's disease.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Catalytic Activity: AH2 + dopamine = 3-tyramine + A + H2O
Sequence Mass (Da): 115026
Sequence Length: 1017
EC: 1.1.-.-
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Q08IT1 | MWKQKGAQGNDPYLYSTNNFVGRQYWEFQPDAGTPEEREEVEKARKDYVNNKKLHGIHPCSDMLMRRQLIKESGIDLLSIPPLRLDENEQVNYDAVTTAVKKALRLNRAIQAHDGHWPAENAGSLLYTPPLIIALYISGTIDTILTKQHKKELIRFVYNHQNEDGGWGSYIEGHSTMIGSVLSYVMLRLLGEGLAESDDGNGAVERGRKWILDHGGAAGIPSWGKTYLAVLGVYEWEGCNPLPPEFWLFPSSFPFHPAKMWIYCRCTYMPMSYLYGKRYHGPITDLVLSLRQEIYNIPYEQIKWNQQRHNCCKEDLYYPHTLVQDLVWDGLHYFSEPFLKRWPFNKLRKRGLKRVVELMRYGATETRFITTGNGEKALQIMSWWAEDPNGDEFKHHLARIPDFLWIAEDGMTVQSFGSQLWDCILATQAIIATNMVEEYGDSLKKAHFFIKESQIKENPRGDFLKMCRQFTKGAWTFSDQDHGCVVSDCTAEALKCLLLLSQMPQDIVGEKPEVERLYEAVNVLLYLQSRVSGGFAVWEPPVPKPYLEMLNPSEIFADIVVEREHIECTASVIKGLMAFKCLHPGHRQKEIEDSVAKAIRYLERNQMPDGSWYGFWGICFLYGTFFTLSGFASAGRTYDNSEAVRKGVKFFLSTQNEEGGWGESLESCPSEKFTPLKGNRTNLVQTSWAMLGLMFGGQAERDPTPLHRAAKLLINAQMDNGDFPQQEITGVYCKNSMLHYAEYRNIFPLWALGEYRKRVWLPKHQQLKI | 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 membrane protein
Sequence Mass (Da): 88343
Sequence Length: 769
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 4.2.1.125
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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 vitro, degrades peptidoglycans from both Gram-negative and Gram-positive bacteria . Is not able to traverse the protective outer membane of Gram-negative bacteria . Is not able to kill Borrelia burgdorferi, one of the Lyme disease-causing bacteria .
PTM: May be posttranslationnally modified, since the saliva wild-type protein is slightly heavier that the recombinant one.
Sequence Mass (Da): 15688
Sequence Length: 142
Subcellular Location: Secreted
EC: 3.4.-.-
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P20792 | MRIRHVVFCLLALVYGAETSDDDLDERTNIFIRDKLIPALKLAEVTKVNFTRLHLCHCSREVGCNARTTGWVPGIEFLNETDRSFYENTCYTDGSCYQSARPSPEISHFGCMDEKSVTDETEFHDTAAKVCTNNTKDPHATVWICCDKGNFCANETIIHLAPGPQQSSTWLILTILALLTFIVLLGIAIFLTRKSWEAKFDWYIRFKPKPGDPLRETENNVPMVTMGDGAGSSVPEVAPIEQQGSTMSTSAGNSFPPGIMPNNMKDMLDVLEETSGSGMGPTTLHKLTIGGQIRLTGRVGSGRFGNVSRGDYRGEAVAVKVFNALDEPAFHKETEIFETRMLRHPNVLRYIGSDRVDTGFVTELWLVTEYHPSGSLHDFLLENTVNIETYYNLMRSTASGLAFLHNQIGGSKESNKPAMAHRDIKSKNIMVKNDLTCAIGDLGLSLSKPEDAASDIIANENYKCGTVRYLAPEILNSTMQFTVFESYQCADVYSFSLVMWETLCRCEDGDVLPREAATVIPYIEWTDRDPQDAQMFDVVCTRRLRPTENPLWKDHPEMKHIMEIIKTCWNGNPSARFTSYICRKRMDERQQLLLDKKAKAVAQTAGVTVQDRKILGPQKPKDESPANGAPRIVQKEIDREDEQENWRETAKTPNGHISSNDDSSRPLLG | 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 . Involved in sensitivity to CO2 levels . In AWC neurons, acts to promote expression of srsx-3, a member of the GPCR family .
Catalytic Activity: ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-L-threonyl-[receptor-protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 75006
Sequence Length: 669
Subcellular Location: Membrane
EC: 2.7.11.30
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Q61475 | MIRGRAPRTRPSPPPPLLPLLSLSLLLLSPTVRGDCGPPPDIPNARPILGRHSKFAEQSKVAYSCNNGFKQVPDKSNIVVCLENGQWSSHETFCEKSCVAPERLSFASLKKEYLNMNFFPVGTIVEYECRPGFRKQPPLPGKATCLEDLVWSPVAQFCKKKSCPNPKDLDNGHINIPTGILFGSEINFSCNPGYRLVGVSSTFCSVTGNTVDWDDEFPVCTEIHCPEPPKINNGIMRGESDSYTYSQVVTYSCDKGFILVGNASIYCTVSKSDVGQWSSPPPRCIEKSKVPTKKPTINVPSTGTPSTPQKPTTESVPNPGDQPTPQKPSTVKVSATQHVPVTKTTVRHPIRTSTDKGEPNTGGDRYIYGHTCLITLTVLHVMLSLIGYLT | 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 factor B to enzymatically active C2a and Bb and thereby prevents the formation of C4b2a and C3bBb, the amplification convertases of the complement cascade. Inhibits complement activation by destabilizing and preventing the formation of C3 and C5 convertases, which prevents complement damage.
Location Topology: Lipid-anchor
Sequence Mass (Da): 42618
Sequence Length: 390
Domain: The first Sushi domain (SCR1) is not necessary for function. SCR2 and SCR4 provide the proper conformation for the active site on SCR3 (By similarity).
Subcellular Location: Cell membrane
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Q61476 | MVSSTWGYDPRAGAGDLVITTTAAGAVTIAVLLFQTVCGDCGPPPDIPNARPILGRHSKFAEQSKVAYSCNNGFKQVPDKSNIVVCLENGQWSSHETFCEKSCDTPERLSFASLKKEYFNMNFFPVGTIVEYECRPGFRKQPSLSGKSTCLEDLVWSPVAQFCKKKSCPNPKDLDNGHINIPTGILFGSEINFSCNPGYRLVGITSILCTIIGNTVDWDDEFPVCTEIFCPDPPKINNGIMRGESDSYKYSQVVIYSCDKGFILFGNSTIYCTVSKSDVGQWSSPPPQCIEESKVPIKKPVVNVPSTGIPSTPQKPTTESVPNPGDQPTPQKPSTVKVPATQHEPDTTTRTSTDKGESNSGGDRYIYGFVAVIAMIDSLIIVKTLWTILSPNRRSDFQGKERKDVSK | 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 factor B to enzymatically active C2a and Bb and thereby prevents the formation of C4b2a and C3bBb, the amplification convertases of the complement cascade. Inhibits complement activation by destabilizing and preventing the formation of C3 and C5 convertases, which prevents complement damage.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 44511
Sequence Length: 407
Domain: The first Sushi domain (SCR1) is not necessary for function. SCR2 and SCR4 provide the proper conformation for the active site on SCR3 (By similarity).
Subcellular Location: Membrane
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Q0ID68 | MVKVNGNYLKLKAGYLFPEIGRRVKAFSSANPEAQLIRLGIGDVTEPLPQACRDAMKSAIDEMGTAEGFHGYGPEQGYAWLREAIARDDFQARGCEISAEEIFVSDGSKCDSSNILDILGSGNRIAVTDPVYPVYVDSNVMAGRTGESGDDGRYGGLTYLPISADNGFAAQIPSEPVDLIYLCYPNNPTGAVATKAQLKKWVDYARANKALILFDAAYEAFIQDPELPHSIYEIEGARDCAIEFRSFSKNAGFTGTRCALTVVPKGLKGKADDGSEVELWGLWNRRQSTKFNGVSYIIQRGAEAVYSDAGKQEVKALVSFYMENAAIIRRELSAAGIEVHGGQHAPYVWLKTPSGMDSWSFFDHLLQKANVVGTPGSGFGAAGEGYFRLSAFNSRSNVDEAMARIRNL | 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-tetrahydrodipicolinate + H(+) + H2O + L-glutamate
Sequence Mass (Da): 44370
Sequence Length: 408
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (aminotransferase route): step 1/1.
EC: 2.6.1.83
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Q55828 | MASINDNYLKLKAGYLFPEIARRVNAFTTANPNAQVIKLGIGDVTEPLPLACRQAMAKAIDDMGDRQTFKGYGPEQGYAWLREKIAQHDFQARGCEVNAEEIFISDGSKCDTGNILDIFGKDNTIAVTDPVYPVYVDTNVMAGHTGDANEKGEYGGLVYLPISAENDFVAAIPSKKVDLIYLCFPNNPTGATATKAYLKQWVDYALAHGSIIFFDAAYEAFITDPTLPHSIYEIEGARDCAIEFRSFSKNAGFTGTRCALTVVPKTLTAKAADGSDVELWKLWNRRQSTKFNGVSYIIQRGAEAVYSPEGQAQVQELIAFYLENARIIREKLAAAGLQVYGGINAPYVWVKTPHGLSSWDFFDKLLHTVNVVGTPGSGFGAAGEGYFRISAFNSRANVEEAMERITSTLKLG | 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-tetrahydrodipicolinate + H(+) + H2O + L-glutamate
Sequence Mass (Da): 45088
Sequence Length: 412
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (aminotransferase route): step 1/1.
EC: 2.6.1.83
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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: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Subcellular Location: Cytoplasm
EC: 4.3.3.7
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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: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Subcellular Location: Cytoplasm
EC: 4.3.3.7
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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: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Subcellular Location: Cytoplasm
EC: 4.3.3.7
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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: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Subcellular Location: Cytoplasm
EC: 4.3.3.7
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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: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Subcellular Location: Cytoplasm
EC: 4.3.3.7
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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: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Subcellular Location: Cytoplasm
EC: 4.3.3.7
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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: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Subcellular Location: Cytoplasm
EC: 4.3.3.7
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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: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Subcellular Location: Cytoplasm
EC: 4.3.3.7
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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: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Subcellular Location: Cytoplasm
EC: 4.3.3.7
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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: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Subcellular Location: Cytoplasm
EC: 4.3.3.7
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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: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Subcellular Location: Cytoplasm
EC: 4.3.3.7
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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: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Subcellular Location: Cytoplasm
EC: 4.3.3.7
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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: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Subcellular Location: Cytoplasm
EC: 4.3.3.7
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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: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Subcellular Location: Cytoplasm
EC: 4.3.3.7
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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: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Subcellular Location: Cytoplasm
EC: 4.3.3.7
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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: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Subcellular Location: Cytoplasm
EC: 4.3.3.7
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Q42948 | MSSSIIGRCHFVADSIEAAGTKRRTTRWRSPRAAVIPSFHLPMRSNEVKNRTFADDIKALRLITAIKTPYLPDGRFDLEAYDTLVNLQIENGAEGVIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGSIKVIGNTGSNSTREAIHATEQGFAVGMHAALHINPYYGKTSLEGLISHFESVLPMGPTIIYNVPSRTGQDIPPRVIQTMAKSPNLAGVKECVGNDRVEQYTSDGVVVWSGNDDECHVSRWDYGATGVISVTSNLVPGLMRELMFGGKNPALNSKLMPLMEWLFHEPNPIALNTALAQLGVVRPVFRLPYVPLTKAKREEFVKIVKEIGRENFIGERDVQILDDNDFILVGRY | 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: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Subcellular Location: Plastid
EC: 4.3.3.7
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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; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.
Subcellular Location: Cytoplasm
EC: 1.17.1.8
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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; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.
Subcellular Location: Cytoplasm
EC: 1.17.1.8
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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; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.
Subcellular Location: Cytoplasm
EC: 1.17.1.8
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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; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.
Subcellular Location: Cytoplasm
EC: 1.17.1.8
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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; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.
Subcellular Location: Cytoplasm
EC: 1.17.1.8
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P9WPZ4 | MTVSRLRPYATTVFAEMSALATRIGAVNLGQGFPDEDGPPKMLQAAQDAIAGGVNQYPPGPGSAPLRRAIAAQRRRHFGVDYDPETEVLVTVGATEAIAAAVLGLVEPGSEVLLIEPFYDSYSPVVAMAGAHRVTVPLVPDGRGFALDADALRRAVTPRTRALIINSPHNPTGAVLSATELAAIAEIAVAANLVVITDEVYEHLVFDHARHLPLAGFDGMAERTITISSAAKMFNCTGWKIGWACGPAELIAGVRAAKQYLSYVGGAPFQPAVALALDTEDAWVAALRNSLRARRDRLAAGLTEIGFAVHDSYGTYFLCADPRPLGYDDSTEFCAALPEKVGVAAIPMSAFCDPAAGQASQQADVWNHLVRFTFCKRDDTLDEAIRRLSVLAERPAT | 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-diaminoheptanedioate (N-succinyl-diaminopimelate) and 2-oxoglutarate (By similarity).
Catalytic Activity: 2-oxoglutarate + N-succinyl-(2S,6S)-2,6-diaminoheptanedioate = (S)-2-succinylamino-6-oxoheptanedioate + L-glutamate
Sequence Mass (Da): 42209
Sequence Length: 397
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 2/3.
Subcellular Location: Cytoplasm
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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), since the activity with L,L-2,6-diaminopimelate is less than 5% of the activity observed with m-DAP. Can use NAD(+) only very poorly since the activity observed in the presence of NAD(+) is about 14% of that with NADP(+).
Catalytic Activity: H2O + meso-2,6-diaminoheptanedioate + NADP(+) = (S)-2-amino-6-oxoheptanedioate + H(+) + NADPH + NH4(+)
Sequence Mass (Da): 32327
Sequence Length: 299
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate: step 1/1.
EC: 1.4.1.16
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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 L,L-2,6-diaminopimelate, D,D-2,6-diaminopimelate, L-glutamate, L-alanine, L-leucine, L-valine, L-aspartate, L-threonine, L-homoserine, L-methionine, L-lysine, L-serine, L-phenylalanine, L-tyrosine, L-tryptophan, L-ornithine, L-histidine, L-arginine, D-glutamate, and D-alanine are not substrates for the oxidative deamination reaction. Can use NAD(+) only poorly since the activity observed in the presence of NAD(+) is about 3% of that with NADP(+).
Catalytic Activity: H2O + meso-2,6-diaminoheptanedioate + NADP(+) = (S)-2-amino-6-oxoheptanedioate + H(+) + NADPH + NH4(+)
Sequence Mass (Da): 35199
Sequence Length: 320
Domain: Is composed of three domains: a dinucleotide binding domain, a dimerization domain, and a substrate-binding domain.
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate: step 1/1.
EC: 1.4.1.16
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Q9KWR0 | MSAIRVGIVGYGNLGRGVEFAISQNPDMELVAVFTRRDPSTVSVASNASVYLVDDAEKFQDDIDVMILCGGSATDLPEQGPHFAQWFNTIDSFDTHAKIPEFFDAVDAAAQKSGKVSVISVGWDPGLFSLNRVLGEAVLPVGTTYTFWGDGLSQGHSDAVRRIEGVKNAVQYTLPIKDAVERVRNGENPELTTREKHARECWVVLEEGADAPKVEQEIVTMPNYFDEYNTTVNFISEDEFNANHTGMPHGGFVIRSGESGANDKQILEFSLKLESNPNFTSSVLVAYARAAHRLSQAGEKGAKTVFDIPFGLLSPKSAAQLRKELL | 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, pyruvate, oxaloacetate, glyoxylate, alpha-ketobutyrate, alpha-ketovalerate, alpha-ketocaproate, alpha-ketoisocaproate, alpha-ketoisovalerate, and phenylpyruvate are not substrates for the reductive amination reaction, and L,L-2,6-diaminopimelate, D,D-2,6-diaminopimelate, DL-alpha-aminopimelate, meso- and DL-2,5-diaminoadipate, L-djenkolate, L-cystine, L-lysine, S-(beta-aminoethy1)-L-homocysteine, L-ornithine, L-arginine, L-alpha,gamma-diaminobutyrate, L-histidine, L-phenylalanine, L-tyrosine, L-glutamate, L-aspartate, L-leucine, L-valine, L-methionine, L-serine, L-alanine, L-alpha-aminobutyrate, D-lysine, D-glutamate, D-leucine, D-alanine, D-phenylalanine, epsilon-aminocaproate, 7-aminoheptanoate, and 8-aminooctanoate are not substrates for the oxidative deamination reaction. Cannot use NAD(+) or NAD(+) analogs instead of NADP(+) for the oxidative deamination reaction.
Catalytic Activity: H2O + meso-2,6-diaminoheptanedioate + NADP(+) = (S)-2-amino-6-oxoheptanedioate + H(+) + NADPH + NH4(+)
Sequence Mass (Da): 35576
Sequence Length: 326
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate: step 1/1.
EC: 1.4.1.16
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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): step 1/3.
Subcellular Location: Cytoplasm
EC: 2.3.1.117
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Q2SX11 | MSATLALTEQLIARASVTPDDQHCQQLMIERLAALGFECETIASHGVTNFWAVKRGTAGREGKLLAFAGHTDVVPTGPLEQWSSPPFVPTHRDGKLYGRGAADMKASLAGFVVAAEEFVAAHPQHRGSIGFLITSDEEGPATDGTVKVVEALAARGERLDYCIVGEPTSTATLGDVVKNGRRGSMSGELVVKGVQGHIAYPHLAKNPIHLLAPALAELAAEQWDEGNEYFPPTTWQVSNLRAGTGATNVIPGHADLLFNFRFSTASTVEGLQARVHAILDKHGLDYALNWSVSGLPFLTPRGELSNALDAAIRAETGLSPELSTTGGTSDGRFIARICPQVIEFGPPNASIHKIDEHIEVRFVEPLKNVYRRVLEQLIA | 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 bacterial cell walls.
Catalytic Activity: H2O + N-succinyl-(2S,6S)-2,6-diaminoheptanedioate = (2S,6S)-2,6-diaminoheptanedioate + succinate
Sequence Mass (Da): 40649
Sequence Length: 379
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 3/3.
EC: 3.5.1.18
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Q0P9K4 | MNAKEFLIELLKFKSVTPNDDGALNFIAMELSDFEAFFIEKEGIKNLLLTKKFKDEGEHLAFGGHVDVVPAGEGWSNNAFAPVEKEGFIYARGAQDMKSGVAAFVDAAKNADFKGARLSLILTSDEEGEAIYGTKAVLEWMQERDMLPDYAVVAEPTCVKKIGDSIKIGRRGSINGKLLIRGKQGHVAYPEKCINPVHDFAPVLKLLAGFDLDPGSAEFSPSKIVITDIRGGMGVCNVTPNDLKLMFNVRNSPDTSLEDVKSYVEKICHGLNYELELKQSSEAFLTNIDNKIVQKMNESVQKITHEVPELNTKGGTSDARYFAKYGVKVVEFGVCNDRIHAIDERVSIEEFEKLCLVFKDLIENF | 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 bacterial cell walls.
Catalytic Activity: H2O + N-succinyl-(2S,6S)-2,6-diaminoheptanedioate = (2S,6S)-2,6-diaminoheptanedioate + succinate
Sequence Mass (Da): 40457
Sequence Length: 365
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 3/3.
EC: 3.5.1.18
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B0T134 | MTSPAPEPVSIDSVALAQALIRRPSVTPADEGAMDVLQRQLEALGFNCRRMKFGEIENLYARRGTERPNLCFAGHTDVVPVGDSAAWTQGPFEAEIQDGMLYGRGAVDMKSAIAAFVAAVSNLPRDLPGSLSFLITGDEEGVAEDGTVRVVQALAAEGEVIDHCIVGEPTSANLLGDMVKIGRRGSINAWIAVDGRQGHVAYPQRAANPIPVMVDILSRLQSRVLDEGYEGFQPSNLEVTTIDVGNTATNVIPASAKARINIRFNPAHQGKDLRAWIEQECRDAADGFSGRVEALCKIGGEAFLTQPGAFTDVIVAAVGDATGRVPELSTTGGTSDARFIRSLCPVVEFGLVGATMHAVDERVPVQEIRDLANIYQALIGRYFAAFA | 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 bacterial cell walls.
Catalytic Activity: H2O + N-succinyl-(2S,6S)-2,6-diaminoheptanedioate = (2S,6S)-2,6-diaminoheptanedioate + succinate
Sequence Mass (Da): 41275
Sequence Length: 387
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 3/3.
EC: 3.5.1.18
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B3PBB9 | MTPPATPLTPTLQLAHDLIRCRSVTPEDDGCQELMIRRLEAIGFKTERLRFGEVDNFWAIRGGDGPILAFAGHTDVVPTGPETHWNNPPFEPTIIDGMLHGRGAADMKGSLASMVVACENFVARHPNHKGRIAFLITSDEEGPSINGTVKVVEWLEARHTKMTWCIVGEPSSTTRVGDVIKNGRRGSLGGVLKVKGIQGHVAYPHLADNPIHTLAPALAELAAEHWDNGNEFFPATSFQVSNINGGTGATNVIPGEVTVVFNFRFSTELTDAILRERTQAILDKHELKYELEWILSGQPFLTPRGDLVNAVVDAINTATGLDAELSTSGGTSDGRFIAPTGAQVVELGPINATIHKVNECISAEDLNKLTAIYERTLEILLA | 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 bacterial cell walls.
Catalytic Activity: H2O + N-succinyl-(2S,6S)-2,6-diaminoheptanedioate = (2S,6S)-2,6-diaminoheptanedioate + succinate
Sequence Mass (Da): 41347
Sequence Length: 382
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 3/3.
EC: 3.5.1.18
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Q3IYS2 | MPIDPVALTADLVRCPSVTPEEGGALDLIERILSGAGFDCTRVDRNGVPNLFARWGRKGANRTFGFNGHTDVVPVGDAAAWTRDPFGGEIADGWLWGRGATDMKSGVAAFVAAAVDFVQETPPDGAVVLTITGDEEGDSTDGTVALLDWMAAEGEAMSVCLVGEPTCPERLGEMMKIGRRGSMTAFFTARGVQGHSAYPHRAKNPVAALARLIDRLSSHDLDYGTEHFDASTLAVTTFDTGNPATNVIPALCRATVNIRFNDAHSGASLTRWLEEEAARVAADTGVEIALSAKISGESFLTPPGELSELVARAVEAETGLRPEPSTSGGTSDARFVRAHCPVVEFGLVGKTMHQVDERVEVAQIEPLKAIYLRILKDYFA | 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 bacterial cell walls.
Catalytic Activity: H2O + N-succinyl-(2S,6S)-2,6-diaminoheptanedioate = (2S,6S)-2,6-diaminoheptanedioate + succinate
Sequence Mass (Da): 40427
Sequence Length: 380
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 3/3.
EC: 3.5.1.18
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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
Sequence Length: 274
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.1.1.7
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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
Sequence Length: 249
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.1.1.7
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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
Sequence Length: 288
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.1.1.7
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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
Sequence Length: 279
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.1.1.7
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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
Sequence Length: 269
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.1.1.7
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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
Sequence Length: 270
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.1.1.7
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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
Sequence Length: 277
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.1.1.7
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Q9UIK4 | MFQASMRSPNMEPFKQQKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAHEIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWITPVDNQQAMVRRESVVNLENFRKQYVRRRWKLSFSIVSLCNHLTRSLMKKVHLRPDEDLRNCESDTEEDIARRKALHPRRRSSTS | 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 latter is caspase-independent and is characterized by the accumulation of autophagic vesicles. Acts as a mediator of anoikis and a suppressor of beta-catenin-dependent anchorage-independent growth of malignant epithelial cells. May play a role in granulocytic maturation . Regulates granulocytic motility by controlling cell spreading and polarization .
PTM: Autophosphorylation at Ser-318 inhibits its catalytic activity. Dephosphorylated at Ser-318 in response to activated Fas and TNF-alpha receptors.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 42898
Sequence Length: 370
Domain: The autoinhibitory domain sterically blocks the substrate peptide-binding site by making both hydrophobic and electrostatic contacts with the kinase core.
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q8VDF3 | MVQASMRSPNMETFKQQKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVCREEIEREVSILRQVLHPNIITLHDVYENRTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAHEIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWITPVDTQQAMVRRESVVNLENFKKQYVRRRWKLSFSIVSLCNHLTRSLMKKVHLRTSEDLRNCESDTEENIARRKALHPRRRSSTS | 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 condensation while the latter involves caspase-independent cell death in conjunction with accumulation of mature autophagic vesicles, plasma membrane blebs, and nuclear condensation without DNA degradation. Mediator of anoikis and a suppressor of beta-catenin-dependent anchorage-independent growth of malignant epithelial cells. May play a role in granulocytic maturation (By similarity). Regulates granulocytes motility by controlling cell spreading and polarization .
PTM: Autophosphorylation at Ser-318 inhibits its catalytic activity. Dephosphorylated at Ser-318 in response to activated Fas and TNF-alpha receptors.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 42778
Sequence Length: 370
Domain: The autoinhibitory domain sterically blocks the substrate peptide-binding site by making both hydrophobic and electrostatic contacts with the kinase core.
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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O43293 | MSTFRQEDVEDHYEMGEELGSGQFAIVRKCRQKGTGKEYAAKFIKKRRLSSSRRGVSREEIEREVNILREIRHPNIITLHDIFENKTDVVLILELVSGGELFDFLAEKESLTEDEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVPNPRIKLIDFGIAHKIEAGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEYFSNTSELAKDFIRRLLVKDPKRRMTIAQSLEHSWIKAIRRRNVRGEDSGRKPERRRLKTTRLKEYTIKSHSSLPPNNSYADFERFSKVLEEAAAAEEGLRELQRSRRLCHEDVEALAAIYEEKEAWYREESDSLGQDLRRLRQELLKTEALKRQAQEEAKGALLGTSGLKRRFSRLENRYEALAKQVASEMRFVQDLVRALEQEKLQGVECGLR | 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 deaths signal, depending on the cellular setting. Involved in regulation of starvation-induced autophagy. Regulates myosin phosphorylation in both smooth muscle and non-muscle cells. In smooth muscle, regulates myosin either directly by phosphorylating MYL12B and MYL9 or through inhibition of smooth muscle myosin phosphatase (SMPP1M) via phosphorylation of PPP1R12A; the inhibition of SMPP1M functions to enhance muscle responsiveness to Ca(2+) and promote a contractile state. Phosphorylates MYL12B in non-muscle cells leading to reorganization of actin cytoskeleton. Isoform 2 can phosphorylate myosin, PPP1R12A and MYL12B. Overexpression leads to condensation of actin stress fibers into thick bundles. Involved in actin filament focal adhesion dynamics. The function in both reorganization of actin cytoskeleton and focal adhesion dissolution is modulated by RhoD. Positively regulates canonical Wnt/beta-catenin signaling through interaction with NLK and TCF7L2. Phosphorylates RPL13A on 'Ser-77' upon interferon-gamma activation which is causing RPL13A release from the ribosome, RPL13A association with the GAIT complex and its subsequent involvement in transcript-selective translation inhibition. Enhances transcription from AR-responsive promoters in a hormone- and kinase-dependent manner. Involved in regulation of cell cycle progression and cell proliferation. May be a tumor suppressor.
PTM: The phosphorylation status is critical for kinase activity, oligomerization and intracellular localization. Phosphorylation at Thr-180, Thr-225 and Thr-265 is essential for activity. The phosphorylated form is localized in the cytoplasm promoted by phosphorylation at Thr-299; nuclear translocation or retention is maximal when it is not phosphorylated. Phosphorylation increases the trimeric form, and its dephosphorylation favors a kinase-inactive monomeric form. Both isoform 1 and isoform 2 can undergo autophosphorylation.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 52536
Sequence Length: 454
Subcellular Location: Nucleus
EC: 2.7.11.1
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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
Sequence Length: 239
Domain: The mature N-terminus mediates interaction with XIAP/BIRC4.
Subcellular Location: Mitochondrion
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Q76PD3 | MSVEVDKSSHSKPKIEKKSKRNKRKWLNDENKTHVTASEAAIERLKKSASFSQAAQQALKQSRKEDNERDIEMQDVDAEAQPHDLLPIPQPSVEDFVDSKPHVKNITSVLPKWLAEPITVDPNTTVEFSSLNISSKLVERLQKQNITRGFAVQAAVLPLLLQDGRHGPMYSYGGDVCVSAATGSGKTLSYVIPIVQCLSHRTVPRLRCVVIVPTRELTVQVAKTFEYYMSGAGLQVCAWTGQKSLRHETYQLNGDENECRIDVLVSTPGRLVDHIRNDESFSLQHLRYMVIDEADRLLDQSFQDWVDTVMMEISHPKCLQNKSNILDLDQNISPTFLPDIDTLLPYRLPSPLQKLVFSATLTRDPSKIASLKLHNPRLVLVQNKDMEVDDGGEIEDDAIVFSVPPTLQEYHVSVSSEKPILLYHLIHSKNLTNILCFVKSNEAAARLHRLLELIHESLNQSFSCGLFTSSLSRDERKKIISRFATGDLNLLVCSDLMARGIDVANTQNVINYDPPLSVRSYVHRIGRTARAGREGFAWTLVQSHEGHHFSKLVKQLRRTLPIKRIKIEFSHISEEFVVAYDKALEALRVEVFNSRYPQQKSFLT | 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 box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Nucleus
EC: 3.6.4.13
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A7TFZ9 | MFAVRFDPSQLVEESVEDEAPKKVIPLKRSKSDEEDESSEEETESSEDEEEKEKEEVADEDSMDVDDESSGDDDEEAEEGEVDAASDHPDKHNSVMSRFQQTLALQDKMDSESLVNENEEVNDENIVESHNLERIPQPAKVKESAVAPAAVSQYKSAAWLNTETIHYDSSMVRKFSDFEDQIDPKLLKNIQQNFSTDTFPIQSILLETLLPTLNFSYNITKKNFTRRVGDVLVNASTGSGKTLAYSIPILQILSKRTVNKLRALVIVPTKLLINQVYETFNNLAQGTSLIVSISKLENSLKEENKKLLQNEPDILITTPGRLVDHLQSGAVNLRNLKFLVLDEADRLLNQSFQNWCNELLNKLKTDKQDHMPGNIVKMVFSATLTTNTEKLHGLQFYNPKLFVMDSVKLYHLPRMLQEYNLHIPTAKTSYKPLFLLRLLSEINGSKMLVFVKSNESSLRLASLLSIMIEHKLGSQFDINSVNSNNTKAENRRIVNEFASNNNTSKVQVLITTDVMSRGVDINDITDVLNYDVPISSQQYIHRCGRTARAQSKGTAYNMLIGKGERTFWATHIDNDISRDIDGCQPQVWGQHDQQNQKDEGQEEEAQVLPLLTVDPETESIYKECLNSLKEKVDTNRK | 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 box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Nucleus
EC: 3.6.4.13
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Q6CDN5 | MFTGVRRFDPTQGGQASPVPFKKVKHEEEESKPETNADEHSEVEYEEESGDDSMDEAEEAKKPVEVKDEEESEDENLTADQKRKKKQEAANLAKRAEEKALERKRKREQHMGEEDSDSEDDLAPIKISGNNKIKLAKGTIRAKGFEELPQTEIYEDKPDESATISRKTQLQTQPILRNATYVEIDDVGSFDEFDLSKNMMKNLDTLGYTKAFSVQKAVIPWLLAQQKLLAPDRKPDLLVSASTGSGKTATYGIPIIEKLRDRIVPRIRAVVVLPTKPLVMQVRDVLENLSKGSSLSVVALRNDRSTKRERAVLETADIVVAAPGRLVEQVKENPELFSYIEFLVVDEADRLLGQDYYDWASVLQNNQQRAQAGKTNLTEHYVRNMQTLIFSATLTANPEHIASMDIHNPGVFVIGSSDSYSIPKSLTEIVTHVSAAEKPLMLCELLVQRDINRGVVFTKSSETAARVARMMEIMDADIFHKDWKIAAVSAETSSVHRRRSMKQFIDGKIDFLVCTDLVSRGIDFVVDNVINYDIPSGKREYVHRVGRTARAGREGNAYTFLTGSGEAKWFREIGEFVGRTQEVDATHINSSHNDGYQEALAKLEEEV | 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 box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Nucleus
EC: 3.6.4.13
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P53734 | MFASRFDPSQLTAPAASAPEGIVGTTPPAIVPLKRQATESDNEEYGSHQDSDESSNSSSEEDEDRMQVDYGASEEDSSEVEEEESKPSTHSTVLSRFKQTVSLQERLGASDIAESKEDEGIEDEAASTHQLKQIPQPEFVKNPMNLNTNSLQFKSTGWLNTEKIYYDNSLIKPFSDYANELEAKLLQNICKNFSTNTFPIQSIILDSILPVLNFTLNVSKRNFTRRIGDILVNAATGSGKTLAYSIPIVQTLFKRQINRLRCIIIVPTKLLINQVYTTLTKLTQGTSLIVSIAKLENSLKDEHKKLSNLEPDILITTPGRLVDHLNMKSINLKNLKFLIIDEADRLLNQSFQGWCPKLMSHLKTDKLDTLPGNVIKMIFSATLTTNTEKLNGLNLYKPKLFLKQTDKLYQLPNKLNEFNINIPTAKSVYKPLILLYSICQFMAHSPIAAKILIFVKSNESSIRLSKLLQLICESRSQSSVLKNLQNLAVSINSVNSNNSKAENKKIVANFSHHSESAGITILITTDIMSRGIDINDITQVINYDPPMSSQQYVHRVGRTARANELGSAYNLLVGRGERTFFDDLNKDLDRDGKSVQPLELDFTLLESDSELYTSSLESLKNYHNNTAQA | 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 box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Nucleus
EC: 3.6.4.13
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Q4WV71 | MADDSLLLNFSLGDNNIIQPETKLKGGTWRDRLSAKKIAKHHAKGPRTAGDEDSAPRAPRNPNRIEVPSSRPTKRQRTDGGDSGKQQSHGHPHSNQPRQFISSLFTKNPEPQKAEEVKEEGHVENAKPTNAPLIDGLDTFTNLGLSPNLAAHLLTKLELKAPTAIQKASISQLLKEEGDAFIQAETGSGKTLAYLLPLVQRIMALSKPGAQTDATGQPIVHRDSGLFAIVLAPTRELCKQISVVLENLLRCAHWIVAGTVIGGEKKKSEKARLRKGLNILVATPGRLADHLDNTQALDVSNVRWLVLDEGDRLMELGFEEEIQGIVKKLDARQRPSRIPGIPARRTTILCSATLKMSVQKLGEISLKDAVHIKADPEDEDEKARRSKAEESAYRVPAQLKQSYAVVAAKLRLVTLTAFFKRTFMRKGSVMKAIIFVSCADSVDFHFEVFTRKQVKEDGGEPSDTDKSEEKPPSSPHGTIAPATAFSNPSNPVTLFRLHGSLPQNVRTSTLGAFAKNKEASVLICTDVASRGLDLPNVDLVVEYDPAFSAEDHLHRIGRTARVGRDGRALIFLQPGCEENYVEVLKRGYRDGGKALTRADANEILKRGFGGNVESGNKDWETKATDWQCEVERWALENPEYLEMARRAFQSHIRAYATHIAAERSMFNIKELHLGHLAKAFALRDRPSKINVPGLRQGKEETKKDFKAERNSAAGKKRKAGGADLADDIPSANNTATAAQKMRAKMKEHMAGANEFNLA | 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 box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Nucleus
EC: 3.6.4.13
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A2RA55 | MADDGLLLNFAIPDTTVLRPEKTKVKGGTWRDRLSAKKIAAHRTNNPRKEKSASNGEQNSNPRNPNRIQVSGPRPVKRQRIEDDDGNGGSQPRQQQQQHPGAPRQFVSSLFSKNPRPRNAVEEKNEAGAEVEDAKPTNAPLIDGLDTFTNLGLSAPLAAHLLTKLEVKAPTAIQKASITQLLKEESDAFIQAETGSGKTMAYLLPLVQRIMTISLNQKKREEGEQVQRDSGLFAIVLAPTRELCKQIAVVLEGLLRCAHWIVAGTVIGGEKKKSEKARLRKGLNILVATPGRLADHLENTQALDVSNVRWLVLDEGDRLMELGFEKELAGIIQKLDARQRPSRIPGIPAKRTTILCSATLKMTVQKLGEISLKDAVHIQADPADEDGEPRKKDEDDAFRVPAQLKQSYAIVASKLRLVTLTAFMKRTFMRKGSVMKAIIFVSCADSVDFHFEVFTRKNGDEEEKKEESEDSDEEDAEEKRKKLGASAHGTIAPATAFSNPSNPVALHRLHGSLPQHVRTATLGAFARNREPSVLICTDVASRGLDLPNVDLVVEYDPAFSAEDHLHRIGRTARLGRDGRALIFLMPGCEEGYVDILKKGYRDGGKALTRNSADDILKRGFGGNVESQNVDWEEKATEWQLDVERWALENKNYLEMARRAYQSHIRAYATHIANERSMFNIKELHLGHLAKSFALRDRPSKINVPGLRQAQADTKKDFKADRKPVAGKKRKAGGHDDDDDDVPRQTDTLTAAQKMRAKMKEHMAGASEFNLA | 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 box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Nucleus
EC: 3.6.4.13
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Q0CF43 | MADDGMLLNFTFSDDVVKKSEPKLKGGTWRDRLSAKKIAQHRAQPRKPSDGTAAPRPVKNPNRIQVSGTRPAKRQRTDDDHDAGLRDHDRAGQSQHQHQHPRQFISSLFSKNPLPRNAEEPTDEAPAEDAKPTNAPLIDGLDTFTNLGLSPTLAAHLLTKLELKAPTAIQKASISQLLKEESDAFIQAETGSGKTLAYLLPLVQRIMALSHPTNRTDATSTTDAEGQPVVHRDSGLFAIVLAPTRELCKQISVVLEGLLRCAHWIVAGTVIGGEKKKSEKARLRKGLNILVATPGRLADHLENTQALDVSNVRWLVLDEGDRLMELGFEQELQGIIKKLDARQRPSRIPGVPTKRTTILCSATLKMNVQKLGEMSLKDAIHIKADPADEDGDAKPKNDDESAFTVPAQLKQSYAIVAAKLRLVTLTAFLKRTFMRKGSVMKAIVFVSCADSVDFHFEVFTRKLQDSDENAEDSDASDTKEKPAAFTHNTIARATAFSNPSNPVTLHRLHGSLPQHVRTSTLASFARNKDASVLVCTDVASRGLDLPNVDLVIEYDPAFSAEDHLHRIGRTARLGRDGRALIFLQPGCEEGYVEILKRGYRDGGKALTRTNADDILKRGFGGNVESENKDWEEKATDWQMDLERWALEKPESLEMARRAYQSHIRAYATHVASERSMFNIKELHLGHLAKAFALRDRPSKINVPGLRQGKDDTKKDYKAARAPAAGKKRKTPGGRDDDDIPAAADTASAAQKMRAKMKEHMAGASEFNLA | 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 box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Nucleus
EC: 3.6.4.13
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