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-AUG-2022, entry version 107.
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; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; 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., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
RN   [2]
RP   FUNCTION AS A CYSTEATE SYNTHASE, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE
RP   SPECIFICITY, KINETIC PARAMETERS, ACTIVITY REGULATION, LACK OF FUNCTION AS A
RP   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 Methanosarcinales:
RT   cysteate synthase evolved from an ancestral threonine synthase.";
RL   Biochem. J. 424:467-478(2009).
CC   -!- FUNCTION: Specifically catalyzes the beta-elimination of phosphate from
CC       L-phosphoserine and the beta-addition of sulfite to the dehydroalanine
CC       intermediate to produce L-cysteate. Does not display threonine synthase
CC       activity like the paralog protein ThrC. {ECO:0000269|PubMed:19761441}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + O-phospho-L-serine + sulfite = L-cysteate + phosphate;
CC         Xref=Rhea:RHEA:26486, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57524, ChEBI:CHEBI:58090; EC=2.5.1.76;
CC         Evidence={ECO:0000269|PubMed:19761441};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:19761441};
CC   -!- ACTIVITY REGULATION: Is inhibited by AP3 (DL-2-amino-3-
CC       phosphonopropionate) and, to a lesser extent, by L-aspartate or AP4
CC       (DL-2-amino-4-phosphonobutyrate). Is also inhibited by EDTA in vitro.
CC       {ECO:0000269|PubMed:19761441}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.43 mM for O-phospho-L-serine {ECO:0000269|PubMed:19761441};
CC         KM=51 uM for sulfite {ECO:0000269|PubMed:19761441};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme M biosynthesis.
CC       {ECO:0000269|PubMed:19761441}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:19761441}.
CC   -!- SIMILARITY: Belongs to the threonine synthase family. Cysteate synthase
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM06667.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE010299; AAM06667.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_048066469.1; NC_003552.1.
DR   AlphaFoldDB; Q8TKU7; -.
DR   SMR; Q8TKU7; -.
DR   STRING; 188937.MA_3297; -.
DR   EnsemblBacteria; AAM06667; AAM06667; MA_3297.
DR   GeneID; 1475190; -.
DR   KEGG; mac:MA_3297; -.
DR   HOGENOM; CLU_666687_0_0_2; -.
DR   InParanoid; Q8TKU7; -.
DR   OrthoDB; 16594at2157; -.
DR   PhylomeDB; Q8TKU7; -.
DR   BioCyc; MetaCyc:MON-15915; -.
DR   BRENDA; 2.5.1.76; 7224.
DR   SABIO-RK; Q8TKU7; -.
DR   UniPathway; UPA00355; -.
DR   Proteomes; UP000002487; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0044686; F:cysteate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003941; F:L-serine ammonia-lyase activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0030378; F:serine racemase activity; IBA:GO_Central.
DR   GO; GO:0018114; F:threonine racemase activity; IBA:GO_Central.
DR   GO; GO:0019295; P:coenzyme M biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0070179; P:D-serine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006563; P:L-serine metabolic process; IBA:GO_Central.
DR   GO; GO:0042866; P:pyruvate biosynthetic process; IBA:GO_Central.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   HAMAP; MF_02109; Cya_synthase; 1.
DR   InterPro; IPR022401; Cysteate_synthase.
DR   InterPro; IPR001926; PLP-dep.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   TIGRFAMs; TIGR03844; cysteate_syn; 1.
PE   1: Evidence at protein level;
KW   Coenzyme M biosynthesis; Pyridoxal phosphate; Reference proteome;
KW   Transferase.
FT   CHAIN           1..416
FT                   /note="Cysteate synthase"
FT                   /id="PRO_0000392650"
FT   BINDING         130
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         104
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
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