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P33182

- PEPM_TETPY

UniProt

P33182 - PEPM_TETPY

Protein

Phosphoenolpyruvate phosphomutase

Gene

PEPM

Organism
Tetrahymena pyriformis
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 68 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
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    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 sitei66 – 661NucleophileSequence Analysis

    GO - Molecular functioni

    1. phosphoenolpyruvate mutase activity Source: UniProtKB-EC

    GO - Biological processi

    1. organic phosphonate biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Isomerase

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-16742.
    UniPathwayiUPA00960.

    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:PEPM
    OrganismiTetrahymena pyriformis
    Taxonomic identifieri5908 [NCBI]
    Taxonomic lineageiEukaryotaAlveolataCiliophoraIntramacronucleataOligohymenophoreaHymenostomatidaTetrahymeninaTetrahymenidaeTetrahymena

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 1010Sequence AnalysisPRO_0000014458
    Chaini11 – 300290Phosphoenolpyruvate phosphomutasePRO_0000014459Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliP33182.
    SMRiP33182. Positions 14-300.
    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.

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

    P33182-1 [UniParc]FASTAAdd to Basket

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    MLANSLKSFF SSTRKTTQLK NMIQSKDLSF IMEAHNGLSA AIVEETGFKG    50
    IWGSGLSISA AMGVRDSNEA SYTQVLEVLE FMSDRTKIPI LLDGDTGYGN 100
    YNNARRLVKK LEQRSIAGVC LEDKIFPKRN SLLDDGRQEL APINEFVAKI 150
    KACKDTQQDA DFQVVARVEA FIAGWGLEEA LKRAEAYRNA GADAILMHSK 200
    LKEPSEIEAF MKEWKNRSPV IIVPTNYHTV PTDTFRKWGV NMVIWANHNM 250
    RACVSAMQET SRRIYEDESL VNVEPKVAKV KEVFRLQGED ELKQADKKYL 300
    Length:300
    Mass (Da):33,849
    Last modified:October 1, 1993 - v1
    Checksum:i19D825A69D60AD39
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M85236 Genomic DNA. Translation: AAA30123.1.
    PIRiA42204.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M85236 Genomic DNA. Translation: AAA30123.1 .
    PIRi A42204.

    3D structure databases

    ProteinModelPortali P33182.
    SMRi P33182. Positions 14-300.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00960 .
    BioCyci MetaCyc:MONOMER-16742.

    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. "Phosphonate biosynthesis: molecular cloning of the gene for phosphoenolpyruvate mutase from Tetrahymena pyriformis and overexpression of the gene product in Escherichia coli."
      Seidel H.M., Pompliano D.L., Knowles J.R.
      Biochemistry 31:2598-2608(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 30331 / GL.
    2. "Phosphonate biosynthesis: isolation of the enzyme responsible for the formation of a carbon-phosphorus bond."
      Seidel H.M., Freeman S., Seto H., Knowles J.R.
      Nature 335:457-458(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 11-40.

    Entry informationi

    Entry nameiPEPM_TETPY
    AccessioniPrimary (citable) accession number: P33182
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 68 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    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