P33182 (PEPM_TETPY) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphoenolpyruvate phosphomutase
Short name=PEP mutase
Short name=PEP phosphomutase
Short name=Phosphoenolpyruvate mutase
EC=5.4.2.9

Gene names

Name:

PEPM

Organism

Tetrahymena pyriformis

Taxonomic identifier

5908 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Alveolata › Ciliophora › Intramacronucleata › Oligohymenophorea › Hymenostomatida › Tetrahymenina › Tetrahymenidae › Tetrahymena

Protein attributes

Sequence length	300 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 function	Isomerase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	organic phosphonate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	phosphoenolpyruvate mutase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	1 – 10	10	Potential		PRO_0000014458
	Chain	11 – 300	290	Phosphoenolpyruvate phosphomutase		PRO_0000014459
Sites
	Active site	66	1	Nucleophile Potential

Sequences

	Sequence		Length	Mass (Da)
	P33182 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: 19D825A69D60AD39	FASTA	300	33,849
	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

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.
PIR	A42204.
3D structure databases
ProteinModelPortal	P33182.
SMR	P33182. Positions 14-300.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-16742.
UniPathway	UPA00960.
Family and domain databases
Gene3D	3.20.20.60. 1 hit.
InterPro	IPR012698. PEnolPyrv_PMutase_core. IPR015813. Pyrv/PenolPyrv_Kinase. [Graphical view]
SUPFAM	SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
TIGRFAMs	TIGR02320. PEP_mutase. 1 hit.
PROSITE	PS00161. ISOCITRATE_LYASE. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PEPM_TETPY

Accession

Primary (citable) accession number: P33182

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	April 3, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)