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Protein

Carboxyvinyl-carboxyphosphonate phosphorylmutase

Gene

bcpA

Organism
Streptomyces hygroscopicus
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the formation of an unusual C-P bond that is involved in the biosynthesis of the antibiotic bialaphos (BA). Catalyzes the rearrangement of the carboxyphosphono group of CPEP to form the C-P bond of phosphinopyruvate.

Catalytic activityi

1-carboxyvinyl carboxyphosphonate = 3-(hydrohydroxyphosphoryl)pyruvate + CO2.

Pathwayi

GO - Molecular functioni

  1. carboxyvinyl-carboxyphosphonate phosphorylmutase activity Source: UniProtKB-EC

GO - Biological processi

  1. antibiotic biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Antibiotic biosynthesis

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15044.
UniPathwayiUPA00197.

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxyvinyl-carboxyphosphonate phosphorylmutase (EC:2.7.8.23)
Alternative name(s):
Carboxyphosphonoenolpyruvate phosphonomutase
Short name:
CPEP phosphonomutase
Gene namesi
Name:bcpA
OrganismiStreptomyces hygroscopicus
Taxonomic identifieri1912 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 295294Carboxyvinyl-carboxyphosphonate phosphorylmutasePRO_0000068818Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP11435.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.20.20.60. 1 hit.
InterProiIPR012697. CPEP_Pphonmut.
IPR018523. Isocitrate_lyase_ph_CS.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
SUPFAMiSSF51621. SSF51621. 1 hit.
TIGRFAMsiTIGR02319. CPEP_Pphonmut. 1 hit.
PROSITEiPS00161. ISOCITRATE_LYASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11435-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVTKARTFR ELMNAPEILV VPSAYDALSA KVIQQAGFPA VHMTGSGTSA
60 70 80 90 100
SMLGLPDLGF TSVSEQAINL KNIVLTVDVP VIMDADAGYG NAMSVWRATR
110 120 130 140 150
EFERVGIVGY HLEDQVNPKR CGHLEGKRLI STEEMTGKIE AAVEAREDED
160 170 180 190 200
FTIIARTDAR ESFGLDEAIR RSREYVAAGA DCIFLEAMLD VEEMKRVRDE
210 220 230 240 250
IDAPLLANMV EGGKTPWLTT KELESIGYNL AIYPLSGWMA AASVLRKLFT
260 270 280 290
ELREAGTTQK FWDDMGLKMS FAELFEVFEY SKISELEARF VRDQD
Length:295
Mass (Da):32,781
Last modified:January 23, 2007 - v3
Checksum:i0C45482B24984256
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti68 – 681I → T in strain: ATCC 21705.
Natural varianti70 – 701L → A in strain: ATCC 21705.
Natural varianti76 – 761T → A in strain: ATCC 21705.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00609 Genomic DNA. Translation: BAA00484.1.
M17150 Genomic DNA. Translation: AAA26711.1.
X67953 Genomic DNA. Translation: CAA48139.1.
PIRiS23585.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00609 Genomic DNA. Translation: BAA00484.1.
M17150 Genomic DNA. Translation: AAA26711.1.
X67953 Genomic DNA. Translation: CAA48139.1.
PIRiS23585.

3D structure databases

ProteinModelPortaliP11435.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00197.
BioCyciMetaCyc:MONOMER-15044.

Family and domain databases

Gene3Di3.20.20.60. 1 hit.
InterProiIPR012697. CPEP_Pphonmut.
IPR018523. Isocitrate_lyase_ph_CS.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
SUPFAMiSSF51621. SSF51621. 1 hit.
TIGRFAMsiTIGR02319. CPEP_Pphonmut. 1 hit.
PROSITEiPS00161. ISOCITRATE_LYASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Carboxyphosphonoenolpyruvate phosphonomutase, a novel enzyme catalyzing C-P bond formation."
    Hidaka T., Imai S., Hara O., Anzai H., Murakami T., Nagaoka K., Seto H.
    J. Bacteriol. 172:3066-3072(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 21705 / SF-1293.
  2. "Nucleotide sequence of a carboxyphosphonoenolpyruvate phosphonomutase gene isolated from a bialaphos-producing organism, Streptomyces hygroscopicus, and its expression in Streptomyces lividans."
    Hidaka T., Hidaka M., Uozumi T., Seto H.
    Mol. Gen. Genet. 233:476-478(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
  3. "Cloning, overexpression and mechanistic studies of carboxyphosphonoenolpyruvate mutase from Streptomyces hygroscopicus."
    Pollack S.J., Freeman S., Pompliano D.L., Knowles J.R.
    Eur. J. Biochem. 209:735-743(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 21705 / SF-1293.
  4. "Transcriptional regulation of bialaphos biosynthesis in Streptomyces hygroscopicus."
    Anzai H., Murakami T., Imai S., Satoh A., Nagaoka K., Thompson C.J.
    J. Bacteriol. 169:3482-3488(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52, PROTEIN SEQUENCE OF 2-31.

Entry informationi

Entry nameiCPPM_STRHY
AccessioniPrimary (citable) accession number: P11435
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: October 1, 2014
This is version 77 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.