Reviewed, UniProtKB/Swiss-Prot O54457 (PPSA_ENTAG)

Names and origin

Protein names

Recommended name:
    Phosphoenolpyruvate synthase
      Short name=PEP synthase
    EC=2.7.9.2
Alternative name(s):
    Pyruvate, water dikinase

Gene names

Name:

ppsA

Organism

Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans)

Taxonomic identifier

549 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Pantoea

Protein attributes

Sequence length	61 AA.
Sequence status	Fragment.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate By similarity.
Catalytic activity	ATP + pyruvate + H2O = AMP + phosphoenolpyruvate + phosphate.
Cofactor	Magnesium By similarity.
Pathway	Carbohydrate biosynthesis; gluconeogenesis.
Domain	The N-terminal domain contains the ATP/Pi binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site By similarity.
Miscellaneous	The reaction takes place in three steps, mediated by a phosphocarrier histidine residue located on the surface of the central domain. The two first partial reactions are catalyzed at an active site located on the N-terminal domain, and the third partial reaction is catalyzed at an active site located on the C-terminal domain. For catalytic turnover, the central domain swivels from the concave surface of the N-terminal domain to that of the C-terminal domain By similarity.
Sequence similarities	Belongs to the PEP-utilizing enzyme family.

Ontologies

Keywords
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	phosphorylation Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW pyruvate, water dikinase 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 – ›61	›61	Phosphoenolpyruvate synthase		PRO_0000147035
Experimental info
	Non-terminal residue	61	1

Sequences

	Sequence		Length	Mass (Da)
	O54457-1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 77AF7475B7A1CAD9	FASTA	61	6,605
	10 20 30 40 50 60 MSSKGEQPLV LWYNQLGMHD VDRVGGKNPS LGEMITNLSS LGVSVPNGFA TTSYAFNLFL D

References

[1]

"Substrate ambiguity of 3-deoxy-D-manno-octulosonate 8-phosphate synthase from Neisseria gonorrhoeae in the context of its membership in a protein family containing a subset of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthases." Subramaniam P.S., Xie G., Xia T., Jensen R.A. J. Bacteriol. 180:119-127(1998) [PubMed: 9422601] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	U93355 Genomic DNA. Translation: AAB96398.1.
3D structure databases
SMR	O54457. Positions 10-60.
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.7.9.2. 3054.
Family and domain databases
InterPro	IPR013815. ATP_grasp_subdomain_1. IPR002192. PPDK_PEP_bd. [Graphical view]
Gene3D	G3DSA:3.30.1490.20. ATP_grasp_subdomain_1. 1 hit.
Pfam	PF01326. PPDK_N. 1 hit. [Graphical view]
PROSITE	PS00742. PEP_ENZYMES_2. Partial match. PS00370. PEP_ENZYMES_PHOS_SITE. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PPSA_ENTAG

Accession

Primary (citable) accession number: O54457

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	June 1, 1998
Last modified:	January 19, 2010
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)