Reviewed, UniProtKB/Swiss-Prot Q7NJF7 (GPMA2_GLOVI)

Names and origin

Protein names

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

Gene names

Name:	gpmA2
Ordered Locus Names:	gll1875

Organism

Gloeobacter violaceus [Complete proteome] [HAMAP]

Taxonomic identifier

33072 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Gloeobacteria › Gloeobacterales › Gloeobacter

Protein attributes

Sequence length	219 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate By similarity. HAMAP MF_01039
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 – 219	219	2,3-bisphosphoglycerate-dependent phosphoglycerate mutase 2 HAMAP MF_01039		PRO_0000179880
Sites
	Active site	9	1	Tele-phosphohistidine intermediate By similarity
	Active site	155	1	By similarity
	Site	58	1	Interaction with carboxyl group of phosphoglycerates By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7NJF7-1 [UniParc]. Last modified December 15, 2003. Version 1. Checksum: C5FEA80461A5F5DC	FASTA	219	24,664
	10 20 30 40 50 60 MALLVMVRHG QSIWNLENRF TGWTDVPLTE KGRAEARACG ELIYCVPFAV AFTSKLTRAQ 70 80 90 100 110 120 DTLRLILEAA DQPDVPVIED QALNERHYGE LQGLNKAETA AKYGEETVRQ WRRSLEGRPP 130 140 150 160 170 180 GGESLKDTAL RSLRYFYEKI VPELEAGKNV LVSAHGNTIR AILMELDHLS PEQVEKVEIE 190 200 210 YCVPVAFEHQ ADGTFSQVLM PRCDIIRPPQ PPARSIARL

References

[1]

"Complete genome structure of Gloeobacter violaceus PCC 7421, a cyanobacterium that lacks thylakoids." Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T., Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M., Tabata S. DNA Res. 10:137-145(2003) [PubMed: 14621292] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PCC 7421.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000045 Genomic DNA. Translation: BAC89816.1.
RefSeq	NP_924821.1.
3D structure databases
SMR	Q7NJF7. Positions 1-195.
ModBase	Search...
Genome annotation databases
GeneID	2600277.
GenomeReviews	Gene locus gll1875 in contig BA000045_GR.
KEGG	gvi:gll1875.
NMPDR	fig|251221.1.peg.1875.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG658938.
OMA	TAKKFGE.
Enzyme and pathway databases
BioCyc	GVIO251221:GLL1875-MONOMER.
BRENDA	5.4.2.1. 276183.
Family and domain databases
HAMAP	MF_01039. PGAM_GpmA. [Tree]
InterPro	IPR001345. PG/BPGM_mutase_AS. IPR013078. PG_mutase. IPR005952. Phosphogly_mut1. [Graphical view]
PANTHER	PTHR11931. Phosphogly_mut1. 1 hit.
Pfam	PF00300. PGAM. 1 hit. [Graphical view]
SMART	SM00855. 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

GPMA2_GLOVI

Accession

Primary (citable) accession number: Q7NJF7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	December 15, 2003
Last modified:	February 9, 2010
This is version 37 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)