ID   CYAS_METAR              Reviewed;         417 AA.
AC   Q0W896;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=UNCMA_27800; ORFNames=LRC440;
OS   Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=351160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22066 / NBRC 105507 / MRE50;
RX   PubMed=16857943; DOI=10.1126/science.1127062;
RA   Erkel C., Kube M., Reinhardt R., Liesack W.;
RT   "Genome of rice cluster I archaea -- the key methane producers in the rice
RT   rhizosphere.";
RL   Science 313:370-372(2006).
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}.
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; AM114193; CAJ35397.1; -; Genomic_DNA.
DR   RefSeq; WP_012037095.1; NC_009464.1.
DR   AlphaFoldDB; Q0W896; -.
DR   SMR; Q0W896; -.
DR   STRING; 351160.LRC440; -.
DR   EnsemblBacteria; CAJ35397; CAJ35397; LRC440.
DR   GeneID; 5144375; -.
DR   KEGG; rci:LRC440; -.
DR   PATRIC; fig|351160.9.peg.2846; -.
DR   eggNOG; arCOG01434; Archaea.
DR   OMA; NLPFVPM; -.
DR   OrthoDB; 16594at2157; -.
DR   UniPathway; UPA00355; -.
DR   Proteomes; UP000000663; 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..417
FT                   /note="Cysteate synthase"
FT                   /id="PRO_0000392656"
FT   BINDING         128
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02109"
FT   BINDING         380
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02109"
FT   MOD_RES         102
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02109"
SQ   SEQUENCE   417 AA;  44945 MW;  2D25CB885042BFBC CRC64;
     MGEYTLVCPC SGKTVPDHYT LNCDCGSLIR TEYAARQLTL RNLPGMWKFY DWLPASGHTD
     TPGTTVTYRS EGLAKELGID LHVAFNGYWP ELGADMKTCS FKELEAPPTI VRAKEHGGKA
     MVLASAGNTA RAFSYLSTIT GFPLIVVVPK QNIDRLWIPG REPGASVKLI SVGGGCDYTD
     AINLSNRIAA LPGMMPEGGA KNVARRDGMG TVMLDAAVTM KGMPDDYFQA IGSGTGGIAA
     WEASMRLRAD GRFGSKLPRL HLAQNLPFVP MLNAWKEGRR EIIPERDMPD AKKSIAEMYS
     DVLSNRTPPY GVGGGVFDAM KATDGLMYGI TREEAVAAKK LFEAREGIDI LPPAAVAVAA
     LVQASEKGLL EGRKVVLNVT GGGQERLMKE VPIYQVEPVL EVPGPDVPME EILKVIA