ID   CYAS_METHJ              Reviewed;         422 AA.
AC   Q2FSC3;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=Mhun_2977;
OS   Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 /
OS   JF-1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX   NCBI_TaxID=323259;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1;
RX   PubMed=26744606; DOI=10.1186/s40793-015-0124-8;
RA   Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H.,
RA   Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M.,
RA   Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.;
RT   "Complete genome sequence of Methanospirillum hungatei type strain JF1.";
RL   Stand. Genomic Sci. 11:2-2(2016).
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; CP000254; ABD42664.1; -; Genomic_DNA.
DR   RefSeq; WP_011449917.1; NC_007796.1.
DR   AlphaFoldDB; Q2FSC3; -.
DR   SMR; Q2FSC3; -.
DR   STRING; 323259.Mhun_2977; -.
DR   EnsemblBacteria; ABD42664; ABD42664; Mhun_2977.
DR   GeneID; 3922460; -.
DR   KEGG; mhu:Mhun_2977; -.
DR   eggNOG; arCOG01434; Archaea.
DR   HOGENOM; CLU_666687_0_0_2; -.
DR   OMA; NLPFVPM; -.
DR   OrthoDB; 16594at2157; -.
DR   UniPathway; UPA00355; -.
DR   Proteomes; UP000001941; 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..422
FT                   /note="Cysteate synthase"
FT                   /id="PRO_0000392655"
FT   BINDING         131
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02109"
FT   BINDING         379
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02109"
FT   MOD_RES         105
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02109"
SQ   SEQUENCE   422 AA;  45660 MW;  AFB64CF5F7C5B2C4 CRC64;
     MTGYTLTCPV CNKEFSDSYT LTCPGGCQGL IRAKYAARQI TLHDAPGVFK YMDWLPVTGV
     LRTRAEPVCF KSEGLARALG LSDLWIVFSG YWPEVGAFAV SGSFKEFEAF PTMQRLSERT
     KGIIQVSSAG NTGRAFAEVS AETCQPVIIV VPESARDRLF TTSPAHDTLL ITISGDYTDA
     INLGSRICTL PGIFPEGGAK NVARRDGMGT VMLAGTLAMG TLPDWYLQAV GSGTGGIAAY
     EASLRLIADG RFGTRMPRLL LFQNEPFIPM VRAWQEKRRE IKDEDMPDAE QAISQVYSDV
     LTNRTPPYGI VGGVFDTLIA TNGLMAGVSS ADAQEAGKLF SSSEGIDPDP AAAVCVAGLM
     RAVRSGVIKP DEKILLNITG GGYARGRKDL PRFVKAPDIM VSKETPFEKI SAKVQEWMRY
     YA