ID   CYAS_METBF              Reviewed;         416 AA.
AC   Q465N2;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=Mbar_A3541;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(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}.
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DR   EMBL; CP000099; AAZ72410.1; -; Genomic_DNA.
DR   RefSeq; WP_011308449.1; NC_007355.1.
DR   AlphaFoldDB; Q465N2; -.
DR   SMR; Q465N2; -.
DR   STRING; 269797.Mbar_A3541; -.
DR   EnsemblBacteria; AAZ72410; AAZ72410; Mbar_A3541.
DR   GeneID; 3627563; -.
DR   KEGG; mba:Mbar_A3541; -.
DR   eggNOG; arCOG01434; Archaea.
DR   HOGENOM; CLU_666687_0_0_2; -.
DR   OMA; NLPFVPM; -.
DR   OrthoDB; 16594at2157; -.
DR   UniPathway; UPA00355; -.
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; Transferase.
FT   CHAIN           1..416
FT                   /note="Cysteate synthase"
FT                   /id="PRO_0000392652"
FT   BINDING         130
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   416 AA;  45675 MW;  BAEC94360171BA17 CRC64;
     MGNFKLKCLK CGREYGQEYR LTCENDNAFL RAEYSEKRLV LRNQPGIGRF HSWLPVQEEL
     TTDAGPITYK SEAFARELGL SNLYIGFSGY WPERGAFIKT CSFKELEAHP TMQLLKETGG
     KAVVLASAGN TGRAFAHVSA LTGTDVYIVV PESGASKLWL PEEPTESVHL ISMSPGNDYT
     DAINLAGRIA KLPGMVSEGG ARNIARRDGM GTVMLDAAVT IGKMPDHYFQ AVGSGTGGIS
     VWEAAMRLRT DGRFGQKLPK LQLAQNLPFV PMYNAWQEKR REIIPELDMK DAKKQVEETY
     ATVLTNRTPP YGVMGGLYDA LTDTDGIMYA ITREEALEAK ALFESLEGID ILPPSAVATA
     SLLKAVEEGN VSKDETILLN LAGGGYKRLK EDYTLYQIEP VATAKNPDIS LDELKI