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P33182

- PEPM_TETPY

UniProt

P33182 - PEPM_TETPY

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Protein

Phosphoenolpyruvate phosphomutase

Gene

PEPM

Organism
Tetrahymena pyriformis
Status
Reviewed - 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:
EMBL
GenBank
DDBJ
Links Updated
M85236 Genomic DNA. Translation: AAA30123.1.
PIRiA42204.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M85236 Genomic DNA. Translation: AAA30123.1 .
PIRi A42204.

3D structure databases

ProteinModelPortali P33182.
SMRi P33182. Positions 14-300.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00960 .
BioCyci MetaCyc:MONOMER-16742.

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. "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(1992) [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(1988) [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