Reviewed, UniProtKB/Swiss-Prot A6VLV0 (GPMA_ACTSZ)

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:	Asuc_0572

Organism

Actinobacillus succinogenes (strain ATCC 55618 / 130Z) [Complete proteome] [HAMAP]

Taxonomic identifier

339671 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Actinobacillus

Protein attributes

Sequence length	227 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 – 227	227	2,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP MF_01039		PRO_1000072984
Sites
	Active site	8	1	Tele-phosphohistidine intermediate By similarity
	Active site	181	1	By similarity
	Site	59	1	Interaction with carboxyl group of phosphoglycerates By similarity

Sequences

	Sequence		Length	Mass (Da)
	A6VLV0-1 [UniParc]. Last modified August 21, 2007. Version 1. Checksum: 68C543ABC0DBB284	FASTA	227	25,667
	10 20 30 40 50 60 MQLVFIRHGL SEWNALNLFT GWRDVNLSEK GVEEAKEAGR KLKAAGFEFD IAFTSVLTRA 70 80 90 100 110 120 IKTCNLVLEE SDQLWVPQIK TWRLNERHYG GLQGLNKAEA AAEHGDEQVR IWRRSYDVLP 130 140 150 160 170 180 PVLDPKDPNS AHNDRRYAHL PADVVPDCEN LKVTLDRVLP FWEDQIAPAI KAGKRVLVAA 190 200 210 220 HGNSLRALAK HIEGISDEDI MGLEIPTGQP LVYELDDNLK VLSKRYL

References

[1]

"Complete sequence of Actinobacillus succinogenes 130Z." Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Vieille C., Richardson P. Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000746 Genomic DNA. Translation: ABR73947.1.
RefSeq	YP_001343882.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A6VLV0.
Genome annotation databases
GeneID	5348190.
GenomeReviews	Gene locus Asuc_0572 in contig CP000746_GR.
KEGG	asu:Asuc_0572.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	FMLWRRS.
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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GPMA_ACTSZ

Accession

Primary (citable) accession number: A6VLV0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	August 21, 2007
Last modified:	November 3, 2009
This is version 16 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)