ID   CYAS_METPS              Reviewed;         427 AA.
AC   D1Z042;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Cysteate synthase {ECO:0000255|HAMAP-Rule:MF_02109};
DE            Short=CS {ECO:0000255|HAMAP-Rule:MF_02109};
DE            Short=Cya synthase {ECO:0000255|HAMAP-Rule:MF_02109};
DE            EC=2.5.1.76 {ECO:0000255|HAMAP-Rule:MF_02109};
GN   OrderedLocusNames=MCP_1992;
OS   Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 /
OS   SANAE).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=304371;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17711 / JCM 13418 / NBRC 101707 / SANAE;
RX   PubMed=21829548; DOI=10.1371/journal.pone.0022898;
RA   Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H.,
RA   Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R.,
RA   Mori K., Fujita N., Imachi H., Takai K.;
RT   "Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella
RT   paludicola, the first cultivated representative of the order
RT   Methanocellales.";
RL   PLoS ONE 6:E22898-E22898(2011).
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. {ECO:0000255|HAMAP-Rule:MF_02109}.
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:0000255|HAMAP-Rule:MF_02109};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02109};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme M biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_02109}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_02109}.
CC   -!- SIMILARITY: Belongs to the threonine synthase family. Cysteate synthase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_02109}.
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DR   EMBL; AP011532; BAI62064.1; -; Genomic_DNA.
DR   AlphaFoldDB; D1Z042; -.
DR   SMR; D1Z042; -.
DR   STRING; 304371.MCP_1992; -.
DR   EnsemblBacteria; BAI62064; BAI62064; MCP_1992.
DR   KEGG; mpd:MCP_1992; -.
DR   PATRIC; fig|304371.9.peg.2033; -.
DR   eggNOG; arCOG01434; Archaea.
DR   OMA; NLPFVPM; -.
DR   UniPathway; UPA00355; -.
DR   Proteomes; UP000001882; Chromosome.
DR   GO; GO:0044686; F:cysteate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019295; P:coenzyme M biosynthetic process; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Coenzyme M biosynthesis; Pyridoxal phosphate; Reference proteome;
KW   Transferase.
FT   CHAIN           1..427
FT                   /note="Cysteate synthase"
FT                   /id="PRO_0000392644"
FT   BINDING         130
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02109"
FT   BINDING         382
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02109"
FT   MOD_RES         104
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02109"
SQ   SEQUENCE   427 AA;  47102 MW;  7049A67306088FE1 CRC64;
     MGTYTLECAG CRHTIPDNYT LRCECGAGLI RARYTARQIS PRDLPGMWRY YDWLPTRGHL
     DTPGAPVTFK SQGLSKELGL KELYISFNGY WPEMGARMDT CSFKELEAPP TIVRAREHGG
     RAMVLASVGN TARAFAYLST LTGFPVVIVV PRKSAHNLWI PGREPGDSIK LITMEEGNDY
     SDAIRLSERI AGIEGVMPEG GARNVARRDG MGVTMLDAAV TMKRMPDDYF QAIGSGTGGI
     AAWEAALRLR DDGRFGDRLP KLHLAQNLPF APMYYAWKAG RRDIIPELDM PEAKKQIEAM
     YTDILSNRNP PYGVTGGVYD ALIDTQGDMY AVTNDEAIRA KRIFEKAEGI DILPPAAVAV
     AALLQACDRG LEKKRTVLLN ITGGGLERLR KEVSMSMVKP CLNVEGPEVP LENITKAIQW
     QTLSKKS