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CYSM_HELPY
ID   CYSM_HELPY              Reviewed;         306 AA.
AC   P56067;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 132.
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=HP_0107;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
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; AE000511; AAD07177.1; -; Genomic_DNA.
DR   PIR; C64533; C64533.
DR   RefSeq; NP_206907.1; NC_000915.1.
DR   PDB; 6AHI; X-ray; 1.90 A; A/B=1-306.
DR   PDBsum; 6AHI; -.
DR   AlphaFoldDB; P56067; -.
DR   SMR; P56067; -.
DR   DIP; DIP-3738N; -.
DR   IntAct; P56067; 1.
DR   MINT; P56067; -.
DR   STRING; 85962.C694_00530; -.
DR   PaxDb; P56067; -.
DR   EnsemblBacteria; AAD07177; AAD07177; HP_0107.
DR   KEGG; hpy:HP_0107; -.
DR   PATRIC; fig|85962.8.peg.114; -.
DR   eggNOG; COG0031; Bacteria.
DR   OMA; RTPVFKF; -.
DR   PhylomeDB; P56067; -.
DR   BioCyc; MetaCyc:HP_RS00545-MON; -.
DR   UniPathway; UPA00136; UER00200.
DR   Proteomes; UP000000429; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004122; F:cystathionine beta-synthase activity; IBA:GO_Central.
DR   GO; GO:0004124; F:cysteine synthase 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; 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   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis; Cysteine biosynthesis;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..306
FT                   /note="Cysteine synthase"
FT                   /id="PRO_0000167110"
FT   BINDING         76
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         180..184
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         46
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   306 AA;  32942 MW;  AE2FF7EE0373DA17 CRC64;
     MMIITTMQDA IGRTPVFKFT NKDYPIPLNS AIYAKLEHLN PGGSVKDRLG QYLIGEGFKT
     GKITSKTTII EPTAGNTGIA LALVAIKHHL KTIFVVPEKF STEKQQIMRA LGALVINTPT
     SEGISGAIKK SKELAESIPD SYLPLQFENP DNPAAYYHTL APEIVQELGT NLTSFVAGIG
     SGGTFAGTAR YLKERIPAIR LIGVEPEGSI LNGGEPGPHE IEGIGVEFIP PFFENLDIDG
     FETISDEEGF SYTRKLAKKN GLLVGSSSGA AFVAALKEAQ RLPEGSQVLT IFPDVADRYL
     SKGIYL
 
 
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