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CPPM_STRHY
ID   CPPM_STRHY              Reviewed;         295 AA.
AC   P11435;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Carboxyvinyl-carboxyphosphonate phosphorylmutase;
DE            EC=2.7.8.23;
DE   AltName: Full=Carboxyphosphonoenolpyruvate phosphonomutase;
DE            Short=CPEP phosphonomutase;
GN   Name=bcpA;
OS   Streptomyces hygroscopicus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces violaceusniger group.
OX   NCBI_TaxID=1912;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 21705 / DSM 41527 / SF-1293;
RX   PubMed=2160937; DOI=10.1128/jb.172.6.3066-3072.1990;
RA   Hidaka T., Imai S., Hara O., Anzai H., Murakami T., Nagaoka K., Seto H.;
RT   "Carboxyphosphonoenolpyruvate phosphonomutase, a novel enzyme catalyzing C-
RT   P bond formation.";
RL   J. Bacteriol. 172:3066-3072(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=1320191; DOI=10.1007/bf00265446;
RA   Hidaka T., Hidaka M., Uozumi T., Seto H.;
RT   "Nucleotide sequence of a carboxyphosphonoenolpyruvate phosphonomutase gene
RT   isolated from a bialaphos-producing organism, Streptomyces hygroscopicus,
RT   and its expression in Streptomyces lividans.";
RL   Mol. Gen. Genet. 233:476-478(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 21705 / DSM 41527 / SF-1293;
RX   PubMed=1330557; DOI=10.1111/j.1432-1033.1992.tb17342.x;
RA   Pollack S.J., Freeman S., Pompliano D.L., Knowles J.R.;
RT   "Cloning, overexpression and mechanistic studies of
RT   carboxyphosphonoenolpyruvate mutase from Streptomyces hygroscopicus.";
RL   Eur. J. Biochem. 209:735-743(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52, AND PROTEIN SEQUENCE OF 2-31.
RX   PubMed=3611020; DOI=10.1128/jb.169.8.3482-3488.1987;
RA   Anzai H., Murakami T., Imai S., Satoh A., Nagaoka K., Thompson C.J.;
RT   "Transcriptional regulation of bialaphos biosynthesis in Streptomyces
RT   hygroscopicus.";
RL   J. Bacteriol. 169:3482-3488(1987).
CC   -!- FUNCTION: Catalyzes the formation of an unusual C-P bond that is
CC       involved in the biosynthesis of the antibiotic bialaphos (BA).
CC       Catalyzes the rearrangement of the carboxyphosphono group of CPEP to
CC       form the C-P bond of phosphinopyruvate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-carboxyvinyl carboxyphosphonate + H(+) = 3-
CC         (hydrohydroxyphosphoryl)pyruvate + CO2; Xref=Rhea:RHEA:14045,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57999,
CC         ChEBI:CHEBI:58348; EC=2.7.8.23;
CC   -!- PATHWAY: Secondary metabolite biosynthesis; bialaphos biosynthesis.
CC   -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; D00609; BAA00484.1; -; Genomic_DNA.
DR   EMBL; M17150; AAA26711.1; -; Genomic_DNA.
DR   EMBL; X67953; CAA48139.1; -; Genomic_DNA.
DR   PIR; S23585; S23585.
DR   AlphaFoldDB; P11435; -.
DR   SMR; P11435; -.
DR   PRIDE; P11435; -.
DR   KEGG; ag:CAA48139; -.
DR   BioCyc; MetaCyc:MON-15044; -.
DR   UniPathway; UPA00197; -.
DR   GO; GO:0008807; F:carboxyvinyl-carboxyphosphonate phosphorylmutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016833; F:oxo-acid-lyase activity; IEA:UniProt.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd00377; ICL_PEPM; 1.
DR   Gene3D; 3.20.20.60; -; 1.
DR   InterPro; IPR012697; CPEP_Pphonmut.
DR   InterPro; IPR039556; ICL/PEPM.
DR   InterPro; IPR018523; Isocitrate_lyase_ph_CS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   TIGRFAMs; TIGR02319; CPEP_Pphonmut; 1.
DR   PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Direct protein sequencing; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:3611020"
FT   CHAIN           2..295
FT                   /note="Carboxyvinyl-carboxyphosphonate phosphorylmutase"
FT                   /id="PRO_0000068818"
FT   VARIANT         68
FT                   /note="I -> T (in strain: ATCC 21705)"
FT   VARIANT         70
FT                   /note="L -> A (in strain: ATCC 21705)"
FT   VARIANT         76
FT                   /note="T -> A (in strain: ATCC 21705)"
SQ   SEQUENCE   295 AA;  32781 MW;  0C45482B24984256 CRC64;
     MAVTKARTFR ELMNAPEILV VPSAYDALSA KVIQQAGFPA VHMTGSGTSA SMLGLPDLGF
     TSVSEQAINL KNIVLTVDVP VIMDADAGYG NAMSVWRATR EFERVGIVGY HLEDQVNPKR
     CGHLEGKRLI STEEMTGKIE AAVEAREDED FTIIARTDAR ESFGLDEAIR RSREYVAAGA
     DCIFLEAMLD VEEMKRVRDE IDAPLLANMV EGGKTPWLTT KELESIGYNL AIYPLSGWMA
     AASVLRKLFT ELREAGTTQK FWDDMGLKMS FAELFEVFEY SKISELEARF VRDQD
 
 
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