CYAS_METLZ
ID CYAS_METLZ Reviewed; 412 AA.
AC A2SQS1;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=Mlab_0503;
OS Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanocorpusculaceae; Methanocorpusculum.
OX NCBI_TaxID=410358;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43576 / DSM 4855 / Z;
RX PubMed=21304657; DOI=10.4056/sigs.35575;
RA Anderson I.J., Sieprawska-Lupa M., Goltsman E., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Tice H., Dalin E., Barry K., Pitluck S., Hauser L.,
RA Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT "Complete genome sequence of Methanocorpusculum labreanum type strain Z.";
RL Stand. Genomic Sci. 1:197-203(2009).
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; CP000559; ABN06677.1; -; Genomic_DNA.
DR RefSeq; WP_011832878.1; NC_008942.1.
DR AlphaFoldDB; A2SQS1; -.
DR SMR; A2SQS1; -.
DR STRING; 410358.Mlab_0503; -.
DR EnsemblBacteria; ABN06677; ABN06677; Mlab_0503.
DR GeneID; 4794996; -.
DR KEGG; mla:Mlab_0503; -.
DR eggNOG; arCOG01434; Archaea.
DR HOGENOM; CLU_666687_0_0_2; -.
DR OMA; NLPFVPM; -.
DR OrthoDB; 16594at2157; -.
DR UniPathway; UPA00355; -.
DR Proteomes; UP000000365; 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..412
FT /note="Cysteate synthase"
FT /id="PRO_0000392646"
FT BINDING 131
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 105
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02109"
SQ SEQUENCE 412 AA; 44181 MW; 5D1AECD95EA028CD CRC64;
MGDYVLRCLT GGEVLEDHYT LACPHHPGFV RAEYTAKQLT VRENLPGVFR FSDWLPVRGS
VPTRSRPVTF QNRELCRELG QPNLWITFTG YYPERGCYVP TGSFKELEAL PTIVRLNEAG
GGTLVVASAG NTGRAFAQMS AEFGTPVVLV VPESSADKLW TAGYFDHSSI RLVTVRGDYT
DAIKTADKIC EAPGFFPEGG GKNIARRDGM GCVMLDGAVT IGKLPEYYFQ AVGSGTGGIA
AWEAAIRLIG DGRFGSKFPE LHLSQNLPFV PMVRAWNAGR DHIIDEDMPD AQASISAVSA
HVLTNRTPPY GICGGVYDAM KSCGGQMYTV ENKDAASAAS LFAEAENGID IDPAAAVAFA
SLISAAEEGS IRTNADILLN ITGGGYQRVK KDCETAKIGV YETVDTGEVP VL