Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O86937

- PEPM_STRVR

UniProt

O86937 - PEPM_STRVR

Protein

Phosphoenolpyruvate phosphomutase

Gene

ppm

Organism
Streptomyces viridochromogenes
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 62 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Formation of a carbon-phosphorus bond by converting phosphoenolpyruvate (PEP) to phosphonopyruvate (P-Pyr).

    Catalytic activityi

    Phosphoenolpyruvate = 3-phosphonopyruvate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei69 – 691NucleophileBy similarity

    GO - Molecular functioni

    1. phosphoenolpyruvate mutase activity Source: UniProtKB-EC

    GO - Biological processi

    1. antibiotic biosynthetic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Antibiotic biosynthesis

    Enzyme and pathway databases

    UniPathwayiUPA00168.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoenolpyruvate phosphomutase (EC:5.4.2.9)
    Short name:
    PEP mutase
    Short name:
    PEP phosphomutase
    Short name:
    Phosphoenolpyruvate mutase
    Gene namesi
    Name:ppm
    OrganismiStreptomyces viridochromogenes
    Taxonomic identifieri1938 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 313313Phosphoenolpyruvate phosphomutasePRO_0000068826Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliO86937.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.20.20.60. 1 hit.
    InterProiIPR012698. PEnolPyrv_PMutase_core.
    IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
    [Graphical view]
    SUPFAMiSSF51621. SSF51621. 1 hit.
    TIGRFAMsiTIGR02320. PEP_mutase. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O86937-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNATERPGSD GTGSPESVGS RLKNLLHGPG TCQLMGVHDG LSARIAVAEG    50
    FEALWASGLC MSTARGVRDS DEASWTELLT LVGTMTEAAP GAPVLVDGDT 100
    GYGNFNTARP SPPAPSCLGA AGVCFEDKVF PKMNSFFGDG HQLAPIGEFS 150
    GKIKACKDTQ RDPGFVVVAR TEALISNLPM EEALTRAHAY VEAVADGLFI 200
    HSRMSTPQQI AEFMRQWDGS APILIAPTTY HRPSLDDFAA LGIAGCIWAN 250
    HSMRAAFSAM RDVCQQIRAD RGIFGVEERV APLKEIFGLL DYESLEQDEN 300
    RYTQAPDLAP VQG 313
    Length:313
    Mass (Da):33,477
    Last modified:November 1, 1998 - v1
    Checksum:i64717D362836E935
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X65195 Genomic DNA. Translation: CAJ14044.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X65195 Genomic DNA. Translation: CAJ14044.1 .

    3D structure databases

    ProteinModelPortali O86937.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00168 .

    Family and domain databases

    Gene3Di 3.20.20.60. 1 hit.
    InterProi IPR012698. PEnolPyrv_PMutase_core.
    IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
    [Graphical view ]
    SUPFAMi SSF51621. SSF51621. 1 hit.
    TIGRFAMsi TIGR02320. PEP_mutase. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of the PEP-phosphomutase and the phosphonopyruvate decarboxylase genes from the phosphinothricin tripeptide producer Streptomyces viridochromogenes Tu494."
      Schwartz D., Recktenwald J., Pelzer S., Wohlleben W.
      FEMS Microbiol. Lett. 163:149-157(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Tu494.

    Entry informationi

    Entry nameiPEPM_STRVR
    AccessioniPrimary (citable) accession number: O86937
    Secondary accession number(s): Q4JFE7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 62 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

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

    External Data

    Dasty 3