ID   A0A1D9FRQ3_9CLOT        Unreviewed;       314 AA.
AC   A0A1D9FRQ3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Cysteine synthase {ECO:0000256|ARBA:ARBA00019371, ECO:0000256|RuleBase:RU003985};
DE            EC=2.5.1.47 {ECO:0000256|ARBA:ARBA00012681, ECO:0000256|RuleBase:RU003985};
GN   ORFNames=BJL90_20155 {ECO:0000313|EMBL:AOY77973.1};
OS   Clostridium formicaceticum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1497 {ECO:0000313|EMBL:AOY77973.1, ECO:0000313|Proteomes:UP000177894};
RN   [1] {ECO:0000313|EMBL:AOY77973.1, ECO:0000313|Proteomes:UP000177894}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27076 {ECO:0000313|EMBL:AOY77973.1,
RC   ECO:0000313|Proteomes:UP000177894};
RA   Bao T., Cheng C., Zhao J., Yang S.-T., Wang J., Wang M.;
RT   "Complete Genome Sequence of Acetogen Clostridium formicoaceticum ATCC
RT   27076.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine;
CC         Xref=Rhea:RHEA:14829, ChEBI:CHEBI:29919, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:35235, ChEBI:CHEBI:58340; EC=2.5.1.47;
CC         Evidence={ECO:0000256|ARBA:ARBA00000298,
CC         ECO:0000256|RuleBase:RU003985};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR605856-50, ECO:0000256|RuleBase:RU003985};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC       from L-serine: step 2/2. {ECO:0000256|ARBA:ARBA00004962}.
CC   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family. {ECO:0000256|ARBA:ARBA00007103,
CC       ECO:0000256|RuleBase:RU003985}.
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DR   EMBL; CP017603; AOY77973.1; -; Genomic_DNA.
DR   RefSeq; WP_070972473.1; NZ_CP020559.1.
DR   AlphaFoldDB; A0A1D9FRQ3; -.
DR   STRING; 1497.BJL90_20155; -.
DR   KEGG; cfm:BJL90_20155; -.
DR   OrthoDB; 9808024at2; -.
DR   UniPathway; UPA00136; UER00200.
DR   Proteomes; UP000177894; Chromosome.
DR   GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:UniProtKB-UniRule.
DR   CDD; cd01561; CBS_like; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR005856; Cys_synth.
DR   InterPro; IPR005859; CysK.
DR   InterPro; IPR001216; P-phosphate_BS.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   NCBIfam; TIGR01139; cysK; 1.
DR   NCBIfam; TIGR01136; cysKM; 1.
DR   PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR   PANTHER; PTHR10314:SF194; CYSTATHIONINE BETA-SYNTHASE; 1.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   PROSITE; PS00901; CYS_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU003985};
KW   Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192,
KW   ECO:0000256|RuleBase:RU003985};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR605856-50};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003985}.
FT   DOMAIN          9..297
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   BINDING         77
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   BINDING         181..185
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   BINDING         269
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   MOD_RES         47
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-51"
SQ   SEQUENCE   314 AA;  33517 MW;  82D445FE113143FD CRC64;
     MARIAKNLTD LIGNTPLLEL TAYNETKNLE GKLIAKLEYF NPGGSVKDRV GYAMIKDAED
     KGLLNKDSII IEPTSGNTGI ALAFVAAAKG YKLILTMPDT MSIERRNLLK ALGAELILTP
     GAEGMKGAIK KAEELAAATA NSFIPQQFNN PANPDFHRKT TAEEIWRDTD GKVDIFVGGV
     GTGGTITGVG EVLKQKNSDI KIIAVEPTDS PVLSGGQPGP HKIQGIGAGF VPSILNTEII
     DEVYQVKNQE AFEATRDLAK IEGLLVGISS GAAVYAATEI AKRPENKGKN IVVLLPDTGE
     RYLSTPLFEE VENN
//