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Protein

Phosphoenolpyruvate phosphomutase

Gene

PEPM

Organism
Tetrahymena pyriformis
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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 sitei66 – 661NucleophileSequence Analysis

GO - Molecular functioni

  1. phosphoenolpyruvate mutase activity Source: UniProtKB-EC

GO - Biological processi

  1. organic phosphonate biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16742.
UniPathwayiUPA00960.

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:PEPM
OrganismiTetrahymena pyriformis
Taxonomic identifieri5908 [NCBI]
Taxonomic lineageiEukaryotaAlveolataCiliophoraIntramacronucleataOligohymenophoreaHymenostomatidaTetrahymeninaTetrahymenidaeTetrahymena

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 1010Sequence AnalysisPRO_0000014458
Chaini11 – 300290Phosphoenolpyruvate phosphomutasePRO_0000014459Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP33182.
SMRiP33182. Positions 14-300.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P33182-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLANSLKSFF SSTRKTTQLK NMIQSKDLSF IMEAHNGLSA AIVEETGFKG
60 70 80 90 100
IWGSGLSISA AMGVRDSNEA SYTQVLEVLE FMSDRTKIPI LLDGDTGYGN
110 120 130 140 150
YNNARRLVKK LEQRSIAGVC LEDKIFPKRN SLLDDGRQEL APINEFVAKI
160 170 180 190 200
KACKDTQQDA DFQVVARVEA FIAGWGLEEA LKRAEAYRNA GADAILMHSK
210 220 230 240 250
LKEPSEIEAF MKEWKNRSPV IIVPTNYHTV PTDTFRKWGV NMVIWANHNM
260 270 280 290 300
RACVSAMQET SRRIYEDESL VNVEPKVAKV KEVFRLQGED ELKQADKKYL
Length:300
Mass (Da):33,849
Last modified:October 1, 1993 - v1
Checksum:i19D825A69D60AD39
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M85236 Genomic DNA. Translation: AAA30123.1.
PIRiA42204.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M85236 Genomic DNA. Translation: AAA30123.1.
PIRiA42204.

3D structure databases

ProteinModelPortaliP33182.
SMRiP33182. Positions 14-300.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00960.
BioCyciMetaCyc:MONOMER-16742.

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. "Phosphonate biosynthesis: molecular cloning of the gene for phosphoenolpyruvate mutase from Tetrahymena pyriformis and overexpression of the gene product in Escherichia coli."
    Seidel H.M., Pompliano D.L., Knowles J.R.
    Biochemistry 31:2598-2608(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 30331 / GL.
  2. "Phosphonate biosynthesis: isolation of the enzyme responsible for the formation of a carbon-phosphorus bond."
    Seidel H.M., Freeman S., Seto H., Knowles J.R.
    Nature 335:457-458(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 11-40.

Entry informationi

Entry nameiPEPM_TETPY
AccessioniPrimary (citable) accession number: P33182
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: October 1, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

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.