ID   CYSK_STRP6              Reviewed;         313 AA.
AC   Q5XAQ3; P82484;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 92.
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 {ECO:0000250|UniProtKB:P37887}; OrderedLocusNames=M6_Spy1375;
OS   Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=286636;
RN   [1] {ECO:0000312|EMBL:AAT87510.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-946 / MGAS10394;
RX   PubMed=15272401; DOI=10.1086/422697;
RA   Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA   Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT   "Progress toward characterization of the group A Streptococcus metagenome:
RT   complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL   J. Infect. Dis. 190:727-738(2004).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 2-22; 91-124 AND 221-243.
RC   STRAIN=JRS4 / Serotype M6 {ECO:0000269|Ref.2};
RA   Hogan D.A., Du P., Stevenson T.I., Whitton M., Kilby G.W., Rogers J.,
RA   VanBogelen R.A.;
RT   "Two-dimensional gel electrophoresis map of Streptococcus pyogenes
RT   proteins.";
RL   Submitted (MAY-2000) to UniProtKB.
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|UniProtKB:P47998};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC       from L-serine: step 2/2.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P47998}.
CC   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family. {ECO:0000255}.
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DR   EMBL; CP000003; AAT87510.1; -; Genomic_DNA.
DR   RefSeq; WP_011184813.1; NC_006086.1.
DR   AlphaFoldDB; Q5XAQ3; -.
DR   SMR; Q5XAQ3; -.
DR   EnsemblBacteria; AAT87510; AAT87510; M6_Spy1375.
DR   KEGG; spa:M6_Spy1375; -.
DR   HOGENOM; CLU_021018_1_0_9; -.
DR   OMA; FWDSGER; -.
DR   UniPathway; UPA00136; UER00200.
DR   Proteomes; UP000001167; 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   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Cysteine biosynthesis; Direct protein sequencing;
KW   Pyridoxal phosphate; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.2"
FT   CHAIN           2..313
FT                   /note="Cysteine synthase"
FT                   /id="PRO_0000259398"
FT   REGION          215..220
FT                   /note="SAT1 binding"
FT                   /evidence="ECO:0000250"
FT   BINDING         75
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         179..183
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         267
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         45
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   313 AA;  33243 MW;  3FB5F881A0F669A3 CRC64;
     MTKIYKTITE LVGQTPIIKL NRLIPNEAAD VYVKLEAFNP GSSVKDRIAL SMIEAAEAEG
     LISPGDVIIE PTSGNTGIGL AWVGAAKGYR VIIVMPETMS LERRQIIQAY GAELVLTPGA
     EGMKGAIAKT ETLAIELGAW MPMQFNNPAN PSIHEKTTAQ EILEAFKEIS LDAFVSGVGT
     GGTLSGVSHV LKKASPETVI YAVEAEESAV LSGQEPGPHK IQGISAGFIP NTLDTKAYDQ
     IIRVKSKDAL ETARLTGAKE GFLVGISSGA ALYAAIEVAK QLGKGKHVLT ILPDNGERYL
     STELYDVPVI KTK