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P11435

- CPPM_STRHY

UniProt

P11435 - CPPM_STRHY

Protein

Carboxyvinyl-carboxyphosphonate phosphorylmutase

Gene

bcpA

Organism
Streptomyces hygroscopicus
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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

    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

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    MAVTKARTFR ELMNAPEILV VPSAYDALSA KVIQQAGFPA VHMTGSGTSA    50
    SMLGLPDLGF TSVSEQAINL KNIVLTVDVP VIMDADAGYG NAMSVWRATR 100
    EFERVGIVGY HLEDQVNPKR CGHLEGKRLI STEEMTGKIE AAVEAREDED 150
    FTIIARTDAR ESFGLDEAIR RSREYVAAGA DCIFLEAMLD VEEMKRVRDE 200
    IDAPLLANMV EGGKTPWLTT KELESIGYNL AIYPLSGWMA AASVLRKLFT 250
    ELREAGTTQK FWDDMGLKMS FAELFEVFEY SKISELEARF VRDQD 295
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00609 Genomic DNA. Translation: BAA00484.1 .
    M17150 Genomic DNA. Translation: AAA26711.1 .
    X67953 Genomic DNA. Translation: CAA48139.1 .
    PIRi S23585.

    3D structure databases

    ProteinModelPortali P11435.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00197 .
    BioCyci MetaCyc:MONOMER-15044.

    Family and domain databases

    Gene3Di 3.20.20.60. 1 hit.
    InterProi IPR012697. CPEP_Pphonmut.
    IPR018523. Isocitrate_lyase_ph_CS.
    IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
    [Graphical view ]
    SUPFAMi SSF51621. SSF51621. 1 hit.
    TIGRFAMsi TIGR02319. CPEP_Pphonmut. 1 hit.
    PROSITEi PS00161. ISOCITRATE_LYASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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