CYSK_HAEIN
ID CYSK_HAEIN Reviewed; 316 AA.
AC P45040;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 155.
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=HI_1103;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH SAT.
RX PubMed=15838047; DOI=10.1128/jb.187.9.3201-3205.2005;
RA Huang B., Vetting M.W., Roderick S.L.;
RT "The active site of O-acetylserine sulfhydrylase is the anchor point for
RT bienzyme complex formation with serine acetyltransferase.";
RL J. Bacteriol. 187:3201-3205(2005).
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; L42023; AAC22758.1; -; Genomic_DNA.
DR PIR; F64182; F64182.
DR RefSeq; NP_439260.1; NC_000907.1.
DR RefSeq; WP_005693427.1; NC_000907.1.
DR PDB; 1Y7L; X-ray; 1.55 A; A=1-316.
DR PDB; 3IQG; X-ray; 1.90 A; X=1-316.
DR PDB; 3IQH; X-ray; 1.90 A; X=1-316.
DR PDB; 3IQI; X-ray; 1.70 A; X=1-316.
DR PDB; 4HO1; X-ray; 1.86 A; X=1-316.
DR PDB; 4LI3; X-ray; 2.59 A; X=1-316.
DR PDB; 4NU8; X-ray; 2.07 A; X=1-316.
DR PDB; 4ORE; X-ray; 2.20 A; X=1-316.
DR PDB; 4ZU1; X-ray; 2.20 A; X=1-316.
DR PDB; 4ZU6; X-ray; 2.03 A; X=1-316.
DR PDB; 5DBE; X-ray; 2.25 A; X=1-316.
DR PDB; 5DBH; X-ray; 1.98 A; X=1-316.
DR PDB; 5XCN; X-ray; 1.69 A; X=1-316.
DR PDB; 5XCP; X-ray; 2.04 A; X=1-316.
DR PDB; 5XCW; X-ray; 1.89 A; X=1-316.
DR PDB; 6AIF; X-ray; 2.30 A; A=1-316.
DR PDB; 7C35; X-ray; 2.10 A; A=1-316.
DR PDB; 7CM8; X-ray; 1.90 A; A=1-316.
DR PDB; 7DJQ; X-ray; 2.30 A; A/B=1-316.
DR PDB; 7EWO; X-ray; 2.40 A; A=1-316.
DR PDBsum; 1Y7L; -.
DR PDBsum; 3IQG; -.
DR PDBsum; 3IQH; -.
DR PDBsum; 3IQI; -.
DR PDBsum; 4HO1; -.
DR PDBsum; 4LI3; -.
DR PDBsum; 4NU8; -.
DR PDBsum; 4ORE; -.
DR PDBsum; 4ZU1; -.
DR PDBsum; 4ZU6; -.
DR PDBsum; 5DBE; -.
DR PDBsum; 5DBH; -.
DR PDBsum; 5XCN; -.
DR PDBsum; 5XCP; -.
DR PDBsum; 5XCW; -.
DR PDBsum; 6AIF; -.
DR PDBsum; 7C35; -.
DR PDBsum; 7CM8; -.
DR PDBsum; 7DJQ; -.
DR PDBsum; 7EWO; -.
DR AlphaFoldDB; P45040; -.
DR SMR; P45040; -.
DR STRING; 71421.HI_1103; -.
DR BindingDB; P45040; -.
DR ChEMBL; CHEMBL1075088; -.
DR PRIDE; P45040; -.
DR EnsemblBacteria; AAC22758; AAC22758; HI_1103.
DR KEGG; hin:HI_1103; -.
DR PATRIC; fig|71421.8.peg.1149; -.
DR eggNOG; COG0031; Bacteria.
DR HOGENOM; CLU_021018_1_0_6; -.
DR OMA; FWDSGER; -.
DR PhylomeDB; P45040; -.
DR BioCyc; HINF71421:G1GJ1-1138-MON; -.
DR BRENDA; 2.5.1.47; 2529.
DR UniPathway; UPA00136; UER00200.
DR EvolutionaryTrace; P45040; -.
DR PRO; PR:P45040; -.
DR Proteomes; UP000000579; 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; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..316
FT /note="Cysteine synthase"
FT /id="PRO_0000167090"
FT BINDING 7
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 268
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 272
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"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:7DJQ"
FT HELIX 7..10
FT /evidence="ECO:0007829|PDB:1Y7L"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:1Y7L"
FT STRAND 20..24
FT /evidence="ECO:0007829|PDB:1Y7L"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:1Y7L"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:1Y7L"
FT HELIX 44..55
FT /evidence="ECO:0007829|PDB:1Y7L"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:5XCP"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:1Y7L"
FT HELIX 72..84
FT /evidence="ECO:0007829|PDB:1Y7L"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:1Y7L"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:4ORE"
FT HELIX 98..106
FT /evidence="ECO:0007829|PDB:1Y7L"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:1Y7L"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:1Y7L"
FT HELIX 119..133
FT /evidence="ECO:0007829|PDB:1Y7L"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:1Y7L"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:5DBH"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:1Y7L"
FT HELIX 148..155
FT /evidence="ECO:0007829|PDB:1Y7L"
FT HELIX 157..164
FT /evidence="ECO:0007829|PDB:1Y7L"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:1Y7L"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:1Y7L"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:1Y7L"
FT HELIX 180..191
FT /evidence="ECO:0007829|PDB:1Y7L"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:1Y7L"
FT HELIX 209..215
FT /evidence="ECO:0007829|PDB:1Y7L"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:1Y7L"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:1Y7L"
FT HELIX 251..265
FT /evidence="ECO:0007829|PDB:1Y7L"
FT HELIX 271..284
FT /evidence="ECO:0007829|PDB:1Y7L"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:1Y7L"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:5XCP"
FT STRAND 293..298
FT /evidence="ECO:0007829|PDB:1Y7L"
FT HELIX 302..305
FT /evidence="ECO:0007829|PDB:5XCN"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:1Y7L"
SQ SEQUENCE 316 AA; 33384 MW; CA753FC79BBD05BD CRC64;
MAIYADNSYS IGNTPLVRLK HFGHNGNVVV KIEGRNPSYS VKCRIGANMV WQAEKDGTLT
KGKEIVDATS GNTGIALAYV AAARGYKITL TMPETMSLER KRLLCGLGVN LVLTEGAKGM
KGAIAKAEEI VASDPSRYVM LKQFENPANP QIHRETTGPE IWKDTDGKVD VVVAGVGTGG
SITGISRAIK LDFGKQITSV AVEPVESPVI SQTLAGEEVK PGPHKIQGIG AGFIPKNLDL
SIIDRVETVD SDTALATARR LMAEEGILAG ISSGAAVAAA DRLAKLPEFA DKLIVVILPS
ASERYLSTAL FEGIEG
