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