Reviewed, UniProtKB/Swiss-Prot Q5P7N4 (GPMA_AZOSE)

Names and origin

Protein names

Recommended name:
    2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
      Short name=Phosphoglyceromutase
      Short name=PGAM
      Short name=BPG-dependent PGAM
      Short name=dPGM
    EC=5.4.2.1

Gene names

Name:	gpmA
Ordered Locus Names:	AZOSEA05550
ORF Names:	ebA1052

Organism

Azoarcus sp. (strain EbN1) (Aromatoleum aromaticum (strain EbN1)) [Complete proteome] [HAMAP]

Taxonomic identifier

76114 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Rhodocyclales › Rhodocyclaceae › Aromatoleum

Protein attributes

Sequence length	249 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate By similarity.
Catalytic activity	2-phospho-D-glycerate = 3-phospho-D-glycerate. HAMAP MF_01039
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. HAMAP MF_01039
Sequence similarities	Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.

Ontologies

Keywords
Biological process	Glycolysis
Molecular function	Isomerase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: HAMAP
Molecular function	2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 249	249	2,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP MF_01039		PRO_0000229101
Sites
	Active site	9	1	Tele-phosphohistidine intermediate By similarity
	Active site	182	1	By similarity
	Site	60	1	Interaction with carboxyl group of phosphoglycerates By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5P7N4-1 [UniParc]. Last modified January 4, 2005. Version 1. Checksum: 9A40D38022F47E3E	FASTA	249	28,045
	10 20 30 40 50 60 MYKIVLLRHG ESTWNKDNRF TGWTDVDLTE KGVEEARGAG HLLKREGYTF DLAYTSVLKR 70 80 90 100 110 120 ANKTLNIVLE ELDSLWLPVE HSWRLNERHY GDLQGLNKAE TAAKFGDDQV LVWRRSYDTP 130 140 150 160 170 180 PPPLPEGDER LTSGDPRYAS LPRAQFPRTE CLKDTVARFV PYWETVIVPN ILAGRRILIA 190 200 210 220 230 240 AHGNSLRALI KYLDNISDSE IVGLNIPTAQ PLVYELDANL RPIRSYYLAD ADTIRAAEAA VAGQGKAKG

References

[1]	"The genome sequence of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1." Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., Reinhardt R. Arch. Microbiol. 183:27-36(2005) [PubMed: 15551059] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR555306 Genomic DNA. Translation: CAI06677.1.
RefSeq	YP_157578.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q5P7N4.
Genome annotation databases
GeneID	3179830.
GenomeReviews	Gene locus AZOSEA05550 in contig CR555306_GR.
KEGG	eba:ebA1052.
NMPDR	fig|76114.4.peg.1576.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q5P7N4.
OMA	FMLWRRS.
Enzyme and pathway databases
BioCyc	ASP76114:EBA1052-MON.
Family and domain databases
HAMAP	MF_01039. [Tree]
InterPro	IPR001345. PG/BPGM_mutase_AC. IPR013078. PG_mutase. IPR005952. Phosphogly_mut1. [Graphical view]
PANTHER	PTHR11931. Phosphogly_mut1. 1 hit.
Pfam	PF00300. PGAM. 1 hit. [Graphical view]
TIGRFAMs	TIGR01258. pgm_1. 1 hit.
PROSITE	PS00175. PG_MUTASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GPMA_AZOSE

Accession

Primary (citable) accession number: Q5P7N4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 4, 2006
Last sequence update:	January 4, 2005
Last modified:	November 3, 2009
This is version 31 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)