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Protein

Phosphoenolpyruvate phosphomutase

Gene

ppm

Organism
Streptomyces viridochromogenes
Status
Reviewed-Annotation score: 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.

Pathway:iphosphinothricin biosynthesis

This protein is involved in the pathway phosphinothricin biosynthesis, which is part of Antibiotic biosynthesis.
View all proteins of this organism that are known to be involved in the pathway phosphinothricin biosynthesis and in Antibiotic biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei69 – 691NucleophileBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Antibiotic biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00168.

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:ppm
OrganismiStreptomyces viridochromogenes
Taxonomic identifieri1938 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 313313Phosphoenolpyruvate phosphomutasePRO_0000068826Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi591159.SSQG_01039.

Structurei

3D structure databases

ProteinModelPortaliO86937.
ModBaseiSearch...
MobiDBiSearch...

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.

O86937-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNATERPGSD GTGSPESVGS RLKNLLHGPG TCQLMGVHDG LSARIAVAEG
60 70 80 90 100
FEALWASGLC MSTARGVRDS DEASWTELLT LVGTMTEAAP GAPVLVDGDT
110 120 130 140 150
GYGNFNTARP SPPAPSCLGA AGVCFEDKVF PKMNSFFGDG HQLAPIGEFS
160 170 180 190 200
GKIKACKDTQ RDPGFVVVAR TEALISNLPM EEALTRAHAY VEAVADGLFI
210 220 230 240 250
HSRMSTPQQI AEFMRQWDGS APILIAPTTY HRPSLDDFAA LGIAGCIWAN
260 270 280 290 300
HSMRAAFSAM RDVCQQIRAD RGIFGVEERV APLKEIFGLL DYESLEQDEN
310
RYTQAPDLAP VQG
Length:313
Mass (Da):33,477
Last modified:November 1, 1998 - v1
Checksum:i64717D362836E935
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65195 Genomic DNA. Translation: CAJ14044.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65195 Genomic DNA. Translation: CAJ14044.1.

3D structure databases

ProteinModelPortaliO86937.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi591159.SSQG_01039.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00168.

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.
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiPEPM_STRVR
AccessioniPrimary (citable) accession number: O86937
Secondary accession number(s): Q4JFE7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1998
Last modified: June 24, 2015
This is version 63 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.