ID   CYAS_METB6              Reviewed;         424 AA.
AC   A7IA69;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=Mboo_2116;
OS   Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanoregulaceae; Methanoregula.
OX   NCBI_TaxID=456442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21154 / JCM 14090 / 6A8;
RX   PubMed=25998264; DOI=10.1099/mic.0.000117;
RA   Braeuer S., Cadillo-Quiroz H., Kyrpides N., Woyke T., Goodwin L.,
RA   Detter C., Podell S., Yavitt J.B., Zinder S.H.;
RT   "Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic
RT   peatland environments.";
RL   Microbiology 161:1572-1581(2015).
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; CP000780; ABS56630.1; -; Genomic_DNA.
DR   RefSeq; WP_012107688.1; NC_009712.1.
DR   AlphaFoldDB; A7IA69; -.
DR   SMR; A7IA69; -.
DR   STRING; 456442.Mboo_2116; -.
DR   EnsemblBacteria; ABS56630; ABS56630; Mboo_2116.
DR   GeneID; 5411214; -.
DR   KEGG; mbn:Mboo_2116; -.
DR   eggNOG; arCOG01434; Archaea.
DR   HOGENOM; CLU_666687_0_0_2; -.
DR   OMA; NLPFVPM; -.
DR   OrthoDB; 16594at2157; -.
DR   UniPathway; UPA00355; -.
DR   Proteomes; UP000002408; 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..424
FT                   /note="Cysteate synthase"
FT                   /id="PRO_0000392648"
FT   BINDING         132
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02109"
FT   BINDING         381
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02109"
FT   MOD_RES         106
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02109"
SQ   SEQUENCE   424 AA;  45201 MW;  982AAE1E997FDE10 CRC64;
     MIPKYRIRCI SGGEIVPDIT SLSCPAGHDS LLRTEYTSRR LQLSYHSGIF RYLCWLPVTA
     PLLPSGGPVT FTSDELSREL GLSRLAISFS GYSPEHHASL TTGSFKELEA LATLQRLWEL
     GKKIPVIASA GNTGRAFAGL SAQYGKPVVV VVPSSAVSRL WTTTPAQDVF LVAVDGDYTD
     AIAVSTALAT VPGCVPEGGA RNVARRDGMG TTVLDAAVTL GRIPDHYFQA VGSGTGAIAA
     WEAALRLIGD GRYGTKLPRL HLAQNKPFTP IVLAWQQRRR TFKPELDMPD APNAIKEVMS
     PVLTNRSPPY GIGGGLFDAL QATEGQMYAV SNDEGKKGMA LIRDTLGIDP DPAAAVATAA
     LVQAAAAGTV GPDDSILLNI TGGGYERIRE DYTLYPIEPS VTVNQHETGD TLKAELSRWV
     AHYG