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CYSM_HELPJ
ID   CYSM_HELPJ              Reviewed;         305 AA.
AC   Q9ZMW6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 123.
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=cysM; Synonyms=cysK; OrderedLocusNames=jhp_0099;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
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   -!- 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; AE001439; AAD05678.1; -; Genomic_DNA.
DR   PIR; E71973; E71973.
DR   RefSeq; WP_000603993.1; NC_000921.1.
DR   AlphaFoldDB; Q9ZMW6; -.
DR   SMR; Q9ZMW6; -.
DR   STRING; 85963.jhp_0099; -.
DR   EnsemblBacteria; AAD05678; AAD05678; jhp_0099.
DR   KEGG; hpj:jhp_0099; -.
DR   eggNOG; COG0031; Bacteria.
DR   OMA; RTPVFKF; -.
DR   UniPathway; UPA00136; UER00200.
DR   Proteomes; UP000000804; 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; 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   PROSITE; PS00901; CYS_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cysteine biosynthesis; Pyridoxal phosphate;
KW   Transferase.
FT   CHAIN           1..305
FT                   /note="Cysteine synthase"
FT                   /id="PRO_0000167111"
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         266
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   305 AA;  33127 MW;  4EED8C5ED0A6FF22 CRC64;
     MILTAMQDAI GRTPIFKFTR KDYPIPLKSA IYAKLEHLNP GGSVKDRLGQ YLIKEAFRTR
     KITSTTTIIE PTAGNTGIAL ALVAIKHHLK TIFVVPKKFS TEKQQIMRAL GALVINTPTS
     EGISGAIKKS KELAESIPDS YLPLQFENPD NPAAYYHTLA PEIVQELGTN LTSFVAGIGS
     GGTFAGMAKY LKERIPNIRL IGVEPEGSIL NGGEPGPHEI EGIGVEFIPP FFANLDIDRF
     ETISDEEGFS YTRKLAKKNG LLVGSSSGAA FAAALKEVQR LPEGSQVLTI FPDMADRYLS
     KGIYS
 
 
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