Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P56839 (PEPM_MYTED) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoenolpyruvate phosphomutase

Short name=PEP mutase
Short name=PEP phosphomutase
Short name=Phosphoenolpyruvate mutase
EC=5.4.2.9
OrganismMytilus edulis (Blue mussel)
Taxonomic identifier6550 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaMolluscaBivalviaPteriomorphiaMytiloidaMytiloideaMytilidaeMytilinaeMytilus

Protein attributes

Sequence length295 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

Phosphoenolpyruvate = 3-phosphonopyruvate.

Cofactor

Magnesium.

Pathway

Phosphorus metabolism; phosphonate biosynthesis.

Subunit structure

Homotetramer. Ref.1 Ref.2

Sequence similarities

Belongs to the isocitrate lyase/PEP mutase superfamily. PEP mutase family.

Ontologies

Keywords
   LigandMagnesium
Metal-binding
   Molecular functionIsomerase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processorganic phosphonate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoenolpyruvate mutase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 295294Phosphoenolpyruvate phosphomutase
PRO_0000068824

Sites

Active site581Nucleophile Potential
Metal binding581Magnesium

Experimental info

Mutagenesis581D → A or S: Abolishes enzyme activity. Ref.1 Ref.3
Mutagenesis581D → N: Strongly reduces enzyme activity. Ref.1 Ref.3
Mutagenesis851D → A: Strongly reduces enzyme activity and increases KM. Ref.1
Mutagenesis871D → A: Strongly reduces enzyme activity. Ref.1
Mutagenesis1141E → A: Strongly reduces enzyme activity. Ref.1
Mutagenesis1221N → A or D: Strongly reduces enzyme activity. Ref.3
Mutagenesis1591R → A: Strongly reduces enzyme activity. Ref.1
Mutagenesis1901H → A: Strongly reduces enzyme activity. Ref.3

Secondary structure

......................................................... 295
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P56839 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: A8A7CC4FD6B031F8

FASTA29532,912
        10         20         30         40         50         60 
MSTKVKKTTQ LKQMLNSKDL EFIMEAHNGL SARIVQEAGF KGIWGSGLSV SAQLGVRDSN 

        70         80         90        100        110        120 
EASWTQVVEV LEFMSDASDV PILLDADTGY GNFNNARRLV RKLEDRGVAG ACLEDKLFPK 

       130        140        150        160        170        180 
TNSLHDGRAQ PLADIEEFAL KIKACKDSQT DPDFCIVARV EAFIAGWGLD EALKRAEAYR 

       190        200        210        220        230        240 
NAGADAILMH SKKADPSDIE AFMKAWNNQG PVVIVPTKYY KTPTDHFRDM GVSMVIWANH 

       250        260        270        280        290 
NLRASVSAIQ QTTKQIYDDQ SLVNVEDKIV SVKEIFRLQR DDELVQAEDK YLPKN 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP56839.
SMRP56839. Positions 5-295.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-16744.
UniPathwayUPA00960.

Family and domain databases

Gene3D3.20.20.60. 1 hit.
InterProIPR012698. PEnolPyrv_PMutase_core.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
SUPFAMSSF51621. SSF51621. 1 hit.
TIGRFAMsTIGR02320. PEP_mutase. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP56839.

Entry information

Entry namePEPM_MYTED
AccessionPrimary (citable) accession number: P56839
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 74 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways