ID K0I4B4_9BURK Unreviewed; 300 AA.
AC K0I4B4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Cysteine synthase {ECO:0000256|ARBA:ARBA00012681, ECO:0000256|RuleBase:RU003985};
DE EC=2.5.1.47 {ECO:0000256|ARBA:ARBA00012681, ECO:0000256|RuleBase:RU003985};
GN Name=cysM {ECO:0000313|EMBL:AFU47375.1};
GN ORFNames=C380_18405 {ECO:0000313|EMBL:AFU47375.1};
OS Acidovorax sp. KKS102.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=358220 {ECO:0000313|EMBL:AFU47375.1, ECO:0000313|Proteomes:UP000006306};
RN [1] {ECO:0000313|EMBL:AFU47375.1, ECO:0000313|Proteomes:UP000006306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KKS102 {ECO:0000313|EMBL:AFU47375.1,
RC ECO:0000313|Proteomes:UP000006306};
RX PubMed=23209225; DOI=10.1128/JB.01848-12;
RA Ohtsubo Y., Maruyama F., Mitsui H., Nagata Y., Tsuda M.;
RT "Complete Genome Sequence of Acidovorax sp. Strain KKS102, a
RT Polychlorinated-Biphenyl Degrader.";
RL J. Bacteriol. 194:6970-6971(2012).
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|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; CP003872; AFU47375.1; -; Genomic_DNA.
DR RefSeq; WP_015015341.1; NC_018708.1.
DR AlphaFoldDB; K0I4B4; -.
DR STRING; 358220.C380_18405; -.
DR KEGG; ack:C380_18405; -.
DR PATRIC; fig|358220.3.peg.3748; -.
DR eggNOG; COG0031; Bacteria.
DR HOGENOM; CLU_021018_1_0_4; -.
DR OrthoDB; 9805733at2; -.
DR UniPathway; UPA00136; UER00200.
DR Proteomes; UP000006306; 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; IPR005858; CysM.
DR InterPro; IPR001216; P-phosphate_BS.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR01136; cysKM; 1.
DR NCBIfam; TIGR01138; cysM; 1.
DR PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR PANTHER; PTHR10314:SF162; CYSTEINE SYNTHASE B; 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 6..287
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 180..184
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT BINDING 261
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 300 AA; 32390 MW; E147C305CD9DC251 CRC64;
MKYPTIEDAV GNTPLVALQR IGAQDNAARG NVVLGKLEGN NPAGSVKDRP ALSMIRRAEE
RGDIRPGDTL IEATSGNTGI ALAMAAAIKG YRMVLVMPED LSIERAQTMK AFGAELVLTP
KSGGMEHARD LAEAMQKRGE GKVLDQFGNP DNPRIHYETT GPEIWEQTGG RITHFVSAMG
TTGTITGVSR FLKEKNPAIQ IIGAQPEEGS RIPGIRKWPQ EYLPKIYDAS TVDELVYVSQ
DSAEDMCRRL AREEGIFAGI SAAGACWVAQ QIAARDSNAT IVFIVCDRGD RYLSTGVFPA
//
