ID CYAS_METAC Reviewed; 416 AA. AC Q8TKU7; DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot. DT 23-MAR-2010, sequence version 2. DT 03-APR-2013, entry version 58. DE RecName: Full=Cysteate synthase; DE Short=CS; DE Short=Cya synthase; DE EC=2.5.1.76; GN OrderedLocusNames=MA_3297; OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / OS C2A). OC Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; OC Methanosarcinaceae; Methanosarcina. OX NCBI_TaxID=188937; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A; RX PubMed=11932238; DOI=10.1101/gr.223902; RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., RA FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., RA Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R., RA Linton L., McEwan P., McKernan K., Talamas J., Tirrell A., Ye W., RA Zimmer A., Barber R.D., Cann I., Graham D.E., Grahame D.A., Guss A.M., RA Hedderich R., Ingram-Smith C., Kuettner H.C., Krzycki J.A., RA Leigh J.A., Li W., Liu J., Mukhopadhyay B., Reeve J.N., Smith K., RA Springer T.A., Umayam L.A., White O., White R.H., de Macario E.C., RA Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L., Paulsen I.T., RA Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H., Lander E., RA Metcalf W.W., Birren B.; RT "The genome of Methanosarcina acetivorans reveals extensive metabolic RT and physiological diversity."; RL Genome Res. 12:532-542(2002). RN [2] RP FUNCTION AS A CYSTEATE SYNTHASE, CATALYTIC ACTIVITY, COFACTOR, RP SUBSTRATE SPECIFICITY, KINETIC PARAMETERS, ENZYME REGULATION, LACK OF RP FUNCTION AS A THREONINE SYNTHASE, SUBUNIT, AND PATHWAY. RX PubMed=19761441; DOI=10.1042/BJ20090999; RA Graham D.E., Taylor S.M., Wolf R.Z., Namboori S.C.; RT "Convergent evolution of coenzyme M biosynthesis in the RT Methanosarcinales: cysteate synthase evolved from an ancestral RT threonine synthase."; RL Biochem. J. 424:467-478(2009). CC -!- FUNCTION: Specifically catalyzes the beta-elimination of phosphate CC from L-phosphoserine and the beta-addition of sulfite to the CC dehydroalanine intermediate to produce L-cysteate. Does not CC display threonine synthase activity like the paralog protein ThrC. CC -!- CATALYTIC ACTIVITY: O-phospho-L-serine + sulfite = L-cysteate + CC phosphate. CC -!- COFACTOR: Pyridoxal phosphate. CC -!- ENZYME REGULATION: Is inhibited by AP3 (DL-2-amino-3- CC phosphonopropionate) and, to a lesser extent, by L-aspartate or CC AP4 (DL-2-amino-4-phosphonobutyrate). Is also inhibited by EDTA in CC vitro. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.43 mM for O-phospho-L-serine; CC KM=51 uM for sulfite; CC -!- PATHWAY: Cofactor biosynthesis; coenzyme M biosynthesis. CC -!- SUBUNIT: Homotrimer. CC -!- SIMILARITY: Belongs to the threonine synthase family. Cysteate CC synthase subfamily. CC -!- SEQUENCE CAUTION: CC Sequence=AAM06667.1; Type=Erroneous initiation; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE010299; AAM06667.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_618187.1; NC_003552.1. DR STRING; 188937.MA3297; -. DR EnsemblBacteria; AAM06667; AAM06667; MA_3297. DR GeneID; 1475190; -. DR GenomeReviews; AE010299_GR; MA_3297. DR KEGG; mac:MA3297; -. DR eggNOG; COG0498; -. DR KO; K15527; -. DR ProtClustDB; CLSK900494; -. DR BioCyc; MACE188937:GI2O-3362-MONOMER; -. DR BioCyc; MetaCyc:MONOMER-15915; -. DR UniPathway; UPA00355; -. DR GO; GO:0044686; F:cysteate synthase activity; IEA:HAMAP. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:HAMAP. DR GO; GO:0019295; P:coenzyme M biosynthetic process; IEA:HAMAP. DR HAMAP; MF_02109; Cya_synthase; 1; -. DR InterPro; IPR022401; Cysteate_synthase. DR InterPro; IPR001926; Trp_syn_b_sub_like_PLP_eny_SF. DR Pfam; PF00291; PALP; 1. DR SUPFAM; SSF53686; PyrdxlP-dep_enz_bsu; 1. DR TIGRFAMs; TIGR03844; cysteate_syn; 1. PE 1: Evidence at protein level; KW Coenzyme M biosynthesis; Complete proteome; Pyridoxal phosphate; KW Reference proteome; Transferase. FT CHAIN 1 416 Cysteate synthase. FT /FTId=PRO_0000392650. FT BINDING 130 130 Pyridoxal phosphate (By similarity). FT MOD_RES 104 104 N6-(pyridoxal phosphate)lysine (By FT similarity). SQ SEQUENCE 416 AA; 45536 MW; DDBB25E58C9ADA3B CRC64; MGRFILKCLK CGREYSQEYR LTCENDDSFL RAEYLEKKLE LRKQPGIGRF HSWLPVQEEL TTEAGPITYK SEALARELGL SNLYIGFSGY WPEKGAFIKT CSFKELEAHP TMQLLKESGG KAIVLASAGN TGRAFAHVSA LTGTDVYIVV PDSGIPKLWL PEEPTDSIHL ISMTPGNDYT DAINLAGRIA KLPGMVPEGG ARNVARREGM GTVMLDAAVT IGKMPDHYFQ AVGSGTGGIS AWEASLRLRE DGRFGSKLPK LQLTQNLPFV PMYNAWQEGR RDIIPEIDMK DAKKRIEETY ATVLTNRAPP YSVTGGLYDA LVDTDGIMYA VSKEEALDAK ALFESLEGID ILPPSAVAAA SLLKAVEAGN VGKDDTILLN IAGGGFKRLK EDFTLFQIEP EITVSNPDVP LEELKL //