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P56839

- PEPM_MYTED

UniProt

P56839 - PEPM_MYTED

Protein

Phosphoenolpyruvate phosphomutase

Gene
N/A
Organism
Mytilus edulis (Blue mussel)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      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.

    Cofactori

    Magnesium.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei58 – 581NucleophileSequence Analysis
    Metal bindingi58 – 581Magnesium

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. phosphoenolpyruvate mutase activity Source: UniProtKB-EC

    GO - Biological processi

    1. organic phosphonate biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Isomerase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-16744.
    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
    OrganismiMytilus edulis (Blue mussel)
    Taxonomic identifieri6550 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaBivalviaPteriomorphiaMytiloidaMytiloideaMytilidaeMytilinaeMytilus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi58 – 581D → A or S: Abolishes enzyme activity. 2 Publications
    Mutagenesisi58 – 581D → N: Strongly reduces enzyme activity. 2 Publications
    Mutagenesisi85 – 851D → A: Strongly reduces enzyme activity and increases KM. 1 Publication
    Mutagenesisi87 – 871D → A: Strongly reduces enzyme activity. 1 Publication
    Mutagenesisi114 – 1141E → A: Strongly reduces enzyme activity. 1 Publication
    Mutagenesisi122 – 1221N → A or D: Strongly reduces enzyme activity. 1 Publication
    Mutagenesisi159 – 1591R → A: Strongly reduces enzyme activity. 1 Publication
    Mutagenesisi190 – 1901H → A: Strongly reduces enzyme activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 295294Phosphoenolpyruvate phosphomutasePRO_0000068824Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.2 Publications

    Structurei

    Secondary structure

    1
    295
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 1610
    Beta strandi17 – 193
    Beta strandi21 – 266
    Helixi29 – 3810
    Beta strandi43 – 453
    Helixi48 – 525
    Turni58 – 603
    Helixi65 – 7612
    Beta strandi82 – 854
    Beta strandi90 – 923
    Helixi93 – 10513
    Beta strandi110 – 1145
    Beta strandi126 – 1283
    Helixi135 – 14814
    Beta strandi155 – 1606
    Turni162 – 1665
    Helixi169 – 18113
    Beta strandi185 – 1895
    Beta strandi193 – 1964
    Helixi197 – 20610
    Beta strandi208 – 2103
    Beta strandi212 – 2143
    Turni218 – 2214
    Helixi224 – 2307
    Beta strandi234 – 2374
    Helixi240 – 25920
    Beta strandi260 – 2623
    Turni263 – 2653
    Helixi266 – 2683
    Helixi272 – 2776
    Helixi281 – 29111

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1M1BX-ray2.25A/B1-295[»]
    1PYMX-ray1.80A/B1-295[»]
    1S2TX-ray2.00A/B1-295[»]
    1S2UX-ray2.00A/B1-295[»]
    1S2VX-ray2.10A/B/C/D1-295[»]
    1S2WX-ray1.69A1-295[»]
    ProteinModelPortaliP56839.
    SMRiP56839. Positions 5-295.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP56839.

    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.

    P56839-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTKVKKTTQ LKQMLNSKDL EFIMEAHNGL SARIVQEAGF KGIWGSGLSV    50
    SAQLGVRDSN EASWTQVVEV LEFMSDASDV PILLDADTGY GNFNNARRLV 100
    RKLEDRGVAG ACLEDKLFPK TNSLHDGRAQ PLADIEEFAL KIKACKDSQT 150
    DPDFCIVARV EAFIAGWGLD EALKRAEAYR NAGADAILMH SKKADPSDIE 200
    AFMKAWNNQG PVVIVPTKYY KTPTDHFRDM GVSMVIWANH NLRASVSAIQ 250
    QTTKQIYDDQ SLVNVEDKIV SVKEIFRLQR DDELVQAEDK YLPKN 295
    Length:295
    Mass (Da):32,912
    Last modified:January 23, 2007 - v3
    Checksum:iA8A7CC4FD6B031F8
    GO

    Cross-referencesi

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1M1B X-ray 2.25 A/B 1-295 [» ]
    1PYM X-ray 1.80 A/B 1-295 [» ]
    1S2T X-ray 2.00 A/B 1-295 [» ]
    1S2U X-ray 2.00 A/B 1-295 [» ]
    1S2V X-ray 2.10 A/B/C/D 1-295 [» ]
    1S2W X-ray 1.69 A 1-295 [» ]
    ProteinModelPortali P56839.
    SMRi P56839. Positions 5-295.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00960 .
    BioCyci MetaCyc:MONOMER-16744.

    Miscellaneous databases

    EvolutionaryTracei P56839.

    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. "Insight into the mechanism of phosphoenolpyruvate mutase catalysis derived from site-directed mutagenesis studies of active site residues."
      Jia Y., Lu Z., Huang K., Herzberg O., Dunaway-Mariano D.
      Biochemistry 38:14165-14173(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-16 AND 115-129, MUTAGENESIS OF ASP-58; ASP-85; ASP-87; GLU-114 AND ARG-159, HOMOTETRAMERIZATION.
    2. "Helix swapping between two alpha/beta barrels: crystal structure of phosphoenolpyruvate mutase with bound Mg(2+)-oxalate."
      Huang K., Li Z., Jia Y., Dunaway-Mariano D., Herzberg O.
      Structure 7:539-548(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH MG(2+) AND AN OXALATE INHIBITOR, HOMOTETRAMERIZATION.
    3. "Dissociative phosphoryl transfer in PEP mutase catalysis: structure of the enzyme/sulfopyruvate complex and kinetic properties of mutants."
      Liu S., Lu Z., Jia Y., Dunaway-Mariano D., Herzberg O.
      Biochemistry 41:10270-10276(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 6-295 IN COMPLEX WITH SULFOPYRUVATE, MUTAGENESIS OF ASP-58; ASN-122 AND HIS-190.

    Entry informationi

    Entry nameiPEPM_MYTED
    AccessioniPrimary (citable) accession number: P56839
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 75 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3