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O86937 (PEPM_STRVR) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Gene names
Name:ppm
OrganismStreptomyces viridochromogenes
Taxonomic identifier1938 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length313 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

Catalytic activity

Phosphoenolpyruvate = 3-phosphonopyruvate.

Pathway

Antibiotic biosynthesis; phosphinothricin biosynthesis.

Sequence similarities

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

Ontologies

Keywords
   Biological processAntibiotic biosynthesis
   Molecular functionIsomerase
Gene Ontology (GO)
   Biological_processantibiotic biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionphosphoenolpyruvate mutase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 313313Phosphoenolpyruvate phosphomutase
PRO_0000068826

Sites

Active site691Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
O86937 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 64717D362836E935

FASTA31333,477
        10         20         30         40         50         60 
MNATERPGSD GTGSPESVGS RLKNLLHGPG TCQLMGVHDG LSARIAVAEG FEALWASGLC 

        70         80         90        100        110        120 
MSTARGVRDS DEASWTELLT LVGTMTEAAP GAPVLVDGDT GYGNFNTARP SPPAPSCLGA 

       130        140        150        160        170        180 
AGVCFEDKVF PKMNSFFGDG HQLAPIGEFS GKIKACKDTQ RDPGFVVVAR TEALISNLPM 

       190        200        210        220        230        240 
EEALTRAHAY VEAVADGLFI HSRMSTPQQI AEFMRQWDGS APILIAPTTY HRPSLDDFAA 

       250        260        270        280        290        300 
LGIAGCIWAN HSMRAAFSAM RDVCQQIRAD RGIFGVEERV APLKEIFGLL DYESLEQDEN 

       310 
RYTQAPDLAP VQG 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X65195 Genomic DNA. Translation: CAJ14044.1.

3D structure databases

ProteinModelPortalO86937.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00168.

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...

Entry information

Entry namePEPM_STRVR
AccessionPrimary (citable) accession number: O86937
Secondary accession number(s): Q4JFE7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1998
Last modified: June 11, 2014
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways