Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P33182 (PEPM_TETPY) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 67. 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:PEPM
OrganismTetrahymena pyriformis
Taxonomic identifier5908 [NCBI]
Taxonomic lineageEukaryotaAlveolataCiliophoraIntramacronucleataOligohymenophoreaHymenostomatidaTetrahymeninaTetrahymenidaeTetrahymena

Protein attributes

Sequence length300 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Formation of a carbon-phosphorus bond by converting phosphoenolpyruvate (PEP) to phosphonopyruvate (P-Pyr).

Catalytic activity

Phosphoenolpyruvate = 3-phosphonopyruvate.

Pathway

Phosphorus metabolism; phosphonate biosynthesis.

Sequence similarities

Belongs to the isocitrate lyase/PEP mutase superfamily. PEP mutase family.

Ontologies

Keywords
   Molecular functionIsomerase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processorganic phosphonate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   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

Propeptide1 – 1010 Potential
PRO_0000014458
Chain11 – 300290Phosphoenolpyruvate phosphomutase
PRO_0000014459

Sites

Active site661Nucleophile Potential

Sequences

Sequence LengthMass (Da)Tools
P33182 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 19D825A69D60AD39

FASTA30033,849
        10         20         30         40         50         60 
MLANSLKSFF SSTRKTTQLK NMIQSKDLSF IMEAHNGLSA AIVEETGFKG IWGSGLSISA 

        70         80         90        100        110        120 
AMGVRDSNEA SYTQVLEVLE FMSDRTKIPI LLDGDTGYGN YNNARRLVKK LEQRSIAGVC 

       130        140        150        160        170        180 
LEDKIFPKRN SLLDDGRQEL APINEFVAKI KACKDTQQDA DFQVVARVEA FIAGWGLEEA 

       190        200        210        220        230        240 
LKRAEAYRNA GADAILMHSK LKEPSEIEAF MKEWKNRSPV IIVPTNYHTV PTDTFRKWGV 

       250        260        270        280        290        300 
NMVIWANHNM RACVSAMQET SRRIYEDESL VNVEPKVAKV KEVFRLQGED ELKQADKKYL 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M85236 Genomic DNA. Translation: AAA30123.1.
PIRA42204.

3D structure databases

ProteinModelPortalP33182.
SMRP33182. Positions 14-300.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-16742.
UniPathwayUPA00960.

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_TETPY
AccessionPrimary (citable) accession number: P33182
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: February 19, 2014
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways