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P29247

- PEPM_STRHY

UniProt

P29247 - PEPM_STRHY

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Protein

Phosphoenolpyruvate phosphomutase

Gene
bcpB
Organism
Streptomyces hygroscopicus
Status
Reviewed - Annotation score: 2 out of 5 - Protein inferred from homologyi

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 sitei69 – 691Nucleophile Reviewed prediction

GO - Molecular functioni

  1. phosphoenolpyruvate mutase activity Source: UniProtKB-EC

GO - Biological processi

  1. antibiotic biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Antibiotic biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00197.

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:bcpB
OrganismiStreptomyces hygroscopicus
Taxonomic identifieri1912 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 313313Phosphoenolpyruvate phosphomutasePRO_0000068825Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP29247.

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.

P29247-1 [UniParc]FASTAAdd to Basket

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MNATEQAANG DRGTTRSAGG RLRYLLHAPG ACQLMGVHDG LSARIAVAEG    50
FEALWASGLC MSTARGVRDS DEASWTELLT LVGTMTDAVP GVPVLVDGDT 100
GYGNFNTARR FAGRAERVGA AGVCFEDKVF PKMNSFFGDG HQLAPVAEFC 150
GKIRACKDAQ RDPDFVVVAR TEALISKLPM EEALDRAAAY AEAGADALFI 200
HSRMNTPQQI ATFMERWEGS TPVLIAPTTY HTPSVDDFAA LGIAGCIWAN 250
HSMRAAFAAM RDVCQRIRTD RGIYGIEDQV APLKEIFGLF DYEGLEKDEN 300
CYTQAPDLAA VQG 313
Length:313
Mass (Da):33,696
Last modified:December 1, 1992 - v1
Checksum:iDB361EB98F3344BA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D10016 Genomic DNA. Translation: BAA00905.1.
PIRiS27698.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D10016 Genomic DNA. Translation: BAA00905.1 .
PIRi S27698.

3D structure databases

ProteinModelPortali P29247.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00197 .

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. "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.

Entry informationi

Entry nameiPEPM_STRHY
AccessioniPrimary (citable) accession number: P29247
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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