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P29247 (PEPM_STRHY) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 66. 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:bcpB
OrganismStreptomyces hygroscopicus
Taxonomic identifier1912 [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

Secondary metabolite biosynthesis; bialaphos 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_0000068825

Sites

Active site691Nucleophile Potential

Sequences

Sequence LengthMass (Da)Tools
P29247 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: DB361EB98F3344BA

FASTA31333,696
        10         20         30         40         50         60 
MNATEQAANG DRGTTRSAGG RLRYLLHAPG ACQLMGVHDG LSARIAVAEG FEALWASGLC 

        70         80         90        100        110        120 
MSTARGVRDS DEASWTELLT LVGTMTDAVP GVPVLVDGDT GYGNFNTARR FAGRAERVGA 

       130        140        150        160        170        180 
AGVCFEDKVF PKMNSFFGDG HQLAPVAEFC GKIRACKDAQ RDPDFVVVAR TEALISKLPM 

       190        200        210        220        230        240 
EEALDRAAAY AEAGADALFI HSRMNTPQQI ATFMERWEGS TPVLIAPTTY HTPSVDDFAA 

       250        260        270        280        290        300 
LGIAGCIWAN HSMRAAFAAM RDVCQRIRTD RGIYGIEDQV APLKEIFGLF DYEGLEKDEN 

       310 
CYTQAPDLAA VQG 

« Hide

References

[1]"Studies on the biosynthesis of bialaphos (SF-1293). 14. Nucleotide sequence of phosphoenolpyruvate phosphomutase gene isolated from a bialaphos producing organism, Streptomyces hygroscopicus, and its expression in Streptomyces lividans."
Hidaka T., Hidaka M., Seto H.
J. Antibiot. 45:1977-1980(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 21705 / SF-1293.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D10016 Genomic DNA. Translation: BAA00905.1.
PIRS27698.

3D structure databases

ProteinModelPortalP29247.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00197.

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_STRHY
AccessionPrimary (citable) accession number: P29247
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: February 19, 2014
This is version 66 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