CYSK_SALTI
ID CYSK_SALTI Reviewed; 323 AA.
AC P0A1E4; P12674;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Cysteine synthase A;
DE Short=CSase A;
DE EC=2.5.1.47;
DE AltName: Full=O-acetylserine (thiol)-lyase A;
DE Short=OAS-TL A;
DE AltName: Full=O-acetylserine sulfhydrylase A;
GN Name=cysK; OrderedLocusNames=STY2666, t0427;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
CC -!- FUNCTION: Two cysteine synthase enzymes are found. Both catalyze the
CC same reaction. Cysteine synthase B can also use thiosulfate in place of
CC sulfide to give cysteine thiosulfonate as a product (By similarity).
CC {ECO:0000250}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL513382; CAD07662.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO68145.1; -; Genomic_DNA.
DR RefSeq; NP_456967.1; NC_003198.1.
DR RefSeq; WP_000036904.1; NZ_WSUR01000025.1.
DR AlphaFoldDB; P0A1E4; -.
DR SMR; P0A1E4; -.
DR STRING; 220341.16503649; -.
DR EnsemblBacteria; AAO68145; AAO68145; t0427.
DR KEGG; stt:t0427; -.
DR KEGG; sty:STY2666; -.
DR PATRIC; fig|220341.7.peg.2702; -.
DR eggNOG; COG0031; Bacteria.
DR HOGENOM; CLU_021018_1_2_6; -.
DR OMA; FWDSGER; -.
DR UniPathway; UPA00136; UER00200.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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 Allosteric enzyme; Amino-acid biosynthesis; Cysteine biosynthesis;
KW Pyridoxal phosphate; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..323
FT /note="Cysteine synthase A"
FT /id="PRO_0000167088"
FT BINDING 8
FT /ligand="hydrogen sulfide"
FT /ligand_id="ChEBI:CHEBI:29919"
FT /ligand_note="allosteric inhibitor; ligand shared between
FT dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P0A1E3"
FT BINDING 35
FT /ligand="hydrogen sulfide"
FT /ligand_id="ChEBI:CHEBI:29919"
FT /ligand_note="allosteric inhibitor; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A1E3"
FT BINDING 72
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 177..181
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 269
FT /ligand="hydrogen sulfide"
FT /ligand_id="ChEBI:CHEBI:29919"
FT /ligand_note="allosteric inhibitor; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A1E3"
FT BINDING 273
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT MOD_RES 42
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 323 AA; 34536 MW; CE74168FAAE99B9E CRC64;
MSKIYEDNSL TIGHTPLVRL NRIGNGRILA KVESRNPSFS VKCRIGANMI WDAEKRGVLK
PGVELVEPTS GNTGIALAYV AAARGYKLTL TMPETMSIER RKLLKALGAN LVLTEGAKGM
KGAIQKAEEI VASDPQKYLL LQQFSNPANP EIHEKTTGPE IWEDTDGQVD VFISGVGTGG
TLTGVTRYIK GTKGKTDLIT VAVEPTDSPV IAQALAGEEI KPGPHKIQGI GAGFIPGNLD
LKLIDKVVGI TNEEAISTAR RLMEEEGILA GISSGAAVAA ALKLQEDESF TNKNIVVILP
SSGERYLSTA LFADLFTEKE LQQ
