CYSK_STAES
ID CYSK_STAES Reviewed; 310 AA.
AC Q8CMT6;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Cysteine synthase;
DE Short=CSase;
DE EC=2.5.1.47;
DE AltName: Full=O-acetylserine (thiol)-lyase;
DE Short=OAS-TL;
DE AltName: Full=O-acetylserine sulfhydrylase;
GN Name=cysK; OrderedLocusNames=SE_2270;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-serine: step 2/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000305}.
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DR EMBL; AE015929; AAO05912.1; -; Genomic_DNA.
DR RefSeq; NP_765825.1; NC_004461.1.
DR RefSeq; WP_001832242.1; NZ_WBME01000023.1.
DR AlphaFoldDB; Q8CMT6; -.
DR SMR; Q8CMT6; -.
DR STRING; 176280.SE_2270; -.
DR EnsemblBacteria; AAO05912; AAO05912; SE_2270.
DR GeneID; 50019576; -.
DR KEGG; sep:SE_2270; -.
DR PATRIC; fig|176280.10.peg.2213; -.
DR eggNOG; COG0031; Bacteria.
DR HOGENOM; CLU_021018_1_0_9; -.
DR OMA; FWDSGER; -.
DR UniPathway; UPA00136; UER00200.
DR Proteomes; UP000001411; Chromosome.
DR GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
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; PLP-dep.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR TIGRFAMs; TIGR01139; cysK; 1.
DR TIGRFAMs; TIGR01136; cysKM; 1.
DR PROSITE; PS00901; CYS_SYNTHASE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cysteine biosynthesis; Pyridoxal phosphate;
KW Transferase.
FT CHAIN 1..310
FT /note="Cysteine synthase"
FT /id="PRO_0000167101"
FT BINDING 76
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 180..184
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT MOD_RES 46
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 310 AA; 33152 MW; E231BA75F40A63EE CRC64;
MAQKPVDYVT QIIGNTPVVK LRNVVDDDAA DIYVKLEYQN PGGSVKDRIA LAMIEKAERE
GKIKPGDTIV EPTSGNTGIG LAFVCAAKGY KAVFTMPETM SQERRNLLKA YGAELVLTPG
SEAMKGAIKK AKELKEEHGY FEPQQFENPA NPEIHELTTG PELVEQFEGR QIDAFLAGVG
TGGTLSGVGK VLKKEYPNVE IVAIEPEASP VLSGGEPGPH KLQGLGAGFV PDTLNTEVYD
SIIKVGNDTA MDMARRVARE EGILAGISSG AAIYAAIQKA KELGKGKTVV TVLPSNGERY
LSTPLYSFDN