CYSK_SALTY
ID CYSK_SALTY Reviewed; 323 AA.
AC P0A1E3; P12674;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Cysteine synthase A;
DE Short=CSase A;
DE EC=2.5.1.47 {ECO:0000269|PubMed:4977445};
DE AltName: Full=O-acetylserine (thiol)-lyase A {ECO:0000303|PubMed:3290198};
DE Short=OAS-TL A;
DE AltName: Full=O-acetylserine sulfhydrylase A {ECO:0000303|PubMed:4977445};
GN Name=cysK; OrderedLocusNames=STM2430;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-16 AND
RP 321-323.
RC STRAIN=LT2;
RX PubMed=3290198; DOI=10.1128/jb.170.7.3150-3157.1988;
RA Byrne C.R., Monroe R.S., Ward K.A., Kredich N.M.;
RT "DNA sequences of the cysK regions of Salmonella typhimurium and
RT Escherichia coli and linkage of the cysK regions to ptsH.";
RL J. Bacteriol. 170:3150-3157(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RC STRAIN=LT2;
RX PubMed=4977445; DOI=10.1016/s0021-9258(19)78241-6;
RA Kredich N.M., Becker M.A., Tomkins G.M.;
RT "Purification and characterization of cysteine synthetase, a bifunctional
RT protein complex, from Salmonella typhimurium.";
RL J. Biol. Chem. 244:2428-2439(1969).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE,
RP COFACTOR, SUBUNIT, AND SEQUENCE REVISION TO 267-268.
RX PubMed=9761678; DOI=10.1006/jmbi.1998.2037;
RA Burkhard P., Rao G.S.J., Hohenester E., Schnackerz K.D., Cook P.F.,
RA Jansonius J.N.;
RT "Three-dimensional structure of O-acetylserine sulfhydrylase from
RT Salmonella typhimurium.";
RL J. Mol. Biol. 283:121-133(1998).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) MUTANT ALA-42 IN COMPLEX WITH
RP PYRIDOXAL PHOSPHATE.
RX PubMed=10452898; DOI=10.1006/jmbi.1999.3002;
RA Burkhard P., Tai C.-H., Ristroph C.M., Cook P.F., Jansonius J.N.;
RT "Ligand binding induces a large conformational change in O-acetylserine
RT sulfhydrylase from Salmonella typhimurium.";
RL J. Mol. Biol. 291:941-953(1999).
RN [6] {ECO:0007744|PDB:1FCJ}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE,
RP COFACTOR, AND ALLOSTERIC REGULATION.
RX PubMed=11023792; DOI=10.1006/jmbi.2000.4109;
RA Burkhard P., Tai C.-H., Jansonius J.N., Cook P.F.;
RT "Identification of an allosteric anion-binding site on O-acetylserine
RT sulfhydrylase: structure of the enzyme with chloride bound.";
RL J. Mol. Biol. 303:279-286(2000).
CC -!- FUNCTION: Two cysteine synthase enzymes are found, this enzyme and
CC CysM; both catalyze the same reaction. Cysteine synthase B (CysM) can
CC also use thiosulfate in place of sulfide to give cysteine thiosulfonate
CC as a product. {ECO:0000269|PubMed:4977445}.
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:0000269|PubMed:4977445};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:11023792, ECO:0000269|PubMed:9761678};
CC -!- ACTIVITY REGULATION: O-acetyl-L-serine causes the CysE-CysK complex to
CC dissociate in the absence of hydrogen sulfide.
CC {ECO:0000269|PubMed:4977445}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5 mM for O-acetyl-L-serine as isolated subunit and in complex with
CC CysK {ECO:0000269|PubMed:4977445};
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-serine: step 2/2.
CC -!- SUBUNIT: Part of the cysteine synthase complex formed at a ratio of 2
CC copies of this protein and 1 copy of serine acetyltransferase (cysE).
CC The complex reversibly dissociates in the presence of O-acetyl-L-serine
CC but in the absence of hydrogen sulfide (PubMed:4977445). Homodimer
CC (PubMed:10452898, PubMed:11023792, PubMed:9761678).
CC {ECO:0000269|PubMed:10452898, ECO:0000269|PubMed:11023792,
CC ECO:0000269|PubMed:4977445, ECO:0000269|PubMed:9761678}.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000305}.
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DR EMBL; M21450; AAA27051.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21324.1; -; Genomic_DNA.
DR PIR; B28181; SYEBAC.
DR RefSeq; NP_461365.1; NC_003197.2.
DR RefSeq; WP_000036904.1; NC_003197.2.
DR PDB; 1D6S; X-ray; 2.30 A; A/B=2-323.
DR PDB; 1FCJ; X-ray; 2.00 A; A/B/C/D=2-323.
DR PDB; 1OAS; X-ray; 2.20 A; A/B=2-323.
DR PDB; 6Z4N; X-ray; 1.20 A; AAA/BBB=1-323.
DR PDBsum; 1D6S; -.
DR PDBsum; 1FCJ; -.
DR PDBsum; 1OAS; -.
DR PDBsum; 6Z4N; -.
DR AlphaFoldDB; P0A1E3; -.
DR SMR; P0A1E3; -.
DR STRING; 99287.STM2430; -.
DR PaxDb; P0A1E3; -.
DR PRIDE; P0A1E3; -.
DR EnsemblBacteria; AAL21324; AAL21324; STM2430.
DR GeneID; 1253952; -.
DR KEGG; stm:STM2430; -.
DR PATRIC; fig|99287.12.peg.2567; -.
DR HOGENOM; CLU_021018_1_2_6; -.
DR OMA; FWDSGER; -.
DR PhylomeDB; P0A1E3; -.
DR BioCyc; SENT99287:STM2430-MON; -.
DR BRENDA; 2.5.1.47; 2169.
DR SABIO-RK; P0A1E3; -.
DR UniPathway; UPA00136; UER00200.
DR EvolutionaryTrace; P0A1E3; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004124; F:cysteine synthase activity; IBA:GO_Central.
DR GO; GO:0080146; F:L-cysteine desulfhydrase activity; IBA:GO_Central.
DR GO; GO:0019344; P:cysteine biosynthetic process; IBA:GO_Central.
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 3D-structure; Allosteric enzyme; Amino-acid biosynthesis;
KW Cysteine biosynthesis; Direct protein sequencing; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3290198"
FT CHAIN 2..323
FT /note="Cysteine synthase A"
FT /id="PRO_0000167089"
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:0000305|PubMed:11023792"
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:0000305|PubMed:11023792"
FT BINDING 72
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:10452898,
FT ECO:0000269|PubMed:11023792, ECO:0000269|PubMed:9761678"
FT BINDING 177..181
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
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:0000305|PubMed:11023792"
FT BINDING 273
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:10452898,
FT ECO:0000269|PubMed:11023792, ECO:0000269|PubMed:9761678"
FT MOD_RES 42
FT /note="N6-(pyridoxal phosphate)lysine"
FT CONFLICT 70
FT /note="S -> N (in Ref. 1; AAA27051)"
FT /evidence="ECO:0000305"
FT CONFLICT 267..268
FT /note="GI -> VF (in Ref. 1; AAA27051)"
FT /evidence="ECO:0000305"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:1FCJ"
FT HELIX 8..11
FT /evidence="ECO:0007829|PDB:1FCJ"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:1FCJ"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:1FCJ"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:1FCJ"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:1FCJ"
FT HELIX 42..55
FT /evidence="ECO:0007829|PDB:1FCJ"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:1FCJ"
FT HELIX 72..84
FT /evidence="ECO:0007829|PDB:1FCJ"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:1FCJ"
FT HELIX 98..106
FT /evidence="ECO:0007829|PDB:1FCJ"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:1FCJ"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:1FCJ"
FT HELIX 119..132
FT /evidence="ECO:0007829|PDB:1FCJ"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:1FCJ"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:1FCJ"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:1FCJ"
FT HELIX 148..155
FT /evidence="ECO:0007829|PDB:1FCJ"
FT HELIX 157..164
FT /evidence="ECO:0007829|PDB:1FCJ"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:1FCJ"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:1FCJ"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:1FCJ"
FT HELIX 180..190
FT /evidence="ECO:0007829|PDB:1FCJ"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:1FCJ"
FT STRAND 199..205
FT /evidence="ECO:0007829|PDB:1FCJ"
FT HELIX 210..215
FT /evidence="ECO:0007829|PDB:1FCJ"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:1FCJ"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:1FCJ"
FT HELIX 252..266
FT /evidence="ECO:0007829|PDB:1FCJ"
FT HELIX 272..284
FT /evidence="ECO:0007829|PDB:1FCJ"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:1FCJ"
FT STRAND 295..299
FT /evidence="ECO:0007829|PDB:1FCJ"
FT HELIX 303..306
FT /evidence="ECO:0007829|PDB:1OAS"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:1OAS"
FT HELIX 318..321
FT /evidence="ECO:0007829|PDB:1D6S"
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
