O86937 (PEPM_STRVR) 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:

ppm

Organism

Streptomyces viridochromogenes

Taxonomic identifier

1938 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	313 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Formation of a carbon-phosphorus bond by converting phosphoenolpyruvate (PEP) to phosphonopyruvate (P-Pyr).
Catalytic activity	Phosphoenolpyruvate = 3-phosphonopyruvate.
Pathway	Antibiotic biosynthesis; phosphinothricin biosynthesis.
Sequence similarities	Belongs to the isocitrate lyase/PEP mutase superfamily. PEP mutase family.

Ontologies

Keywords
Biological process	Antibiotic biosynthesis
Molecular function	Isomerase
Gene Ontology (GO)
Biological_process	antibiotic biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
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
	Chain	1 – 313	313	Phosphoenolpyruvate phosphomutase		PRO_0000068826
Sites
	Active site	69	1	Nucleophile By similarity

Sequences

	Sequence		Length	Mass (Da)
	O86937 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 64717D362836E935	FASTA	313	33,477
	10 20 30 40 50 60 MNATERPGSD GTGSPESVGS RLKNLLHGPG TCQLMGVHDG LSARIAVAEG FEALWASGLC 70 80 90 100 110 120 MSTARGVRDS DEASWTELLT LVGTMTEAAP GAPVLVDGDT GYGNFNTARP SPPAPSCLGA 130 140 150 160 170 180 AGVCFEDKVF PKMNSFFGDG HQLAPIGEFS GKIKACKDTQ RDPGFVVVAR TEALISNLPM 190 200 210 220 230 240 EEALTRAHAY VEAVADGLFI HSRMSTPQQI AEFMRQWDGS APILIAPTTY HRPSLDDFAA 250 260 270 280 290 300 LGIAGCIWAN HSMRAAFSAM RDVCQQIRAD RGIFGVEERV APLKEIFGLL DYESLEQDEN 310 RYTQAPDLAP VQG

References

[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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X65195 Genomic DNA. Translation: CAJ14044.1.
3D structure databases
ProteinModelPortal	O86937.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00168.
Family and domain databases
Gene3D	3.20.20.60. 1 hit.
InterPro	IPR012698. PEnolPyrv_PMutase_core. IPR015813. Pyrv/PenolPyrv_Kinase-like_dom. [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_STRVR

Accession

Primary (citable) accession number: O86937
Secondary accession number(s): Q4JFE7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1998
Last modified:	May 29, 2013
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program