Reviewed, UniProtKB/Swiss-Prot Q732Z5 (GPMA2_BACC1)

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:	BCE_3765

Organism

Bacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP]

Taxonomic identifier

222523 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	240 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 – 240	240	2,3-bisphosphoglycerate-dependent phosphoglycerate mutase 2 HAMAP MF_01039		PRO_0000179844
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)
	Q732Z5-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: F59901F112313FB0	FASTA	240	27,968
	10 20 30 40 50 60 MVKLVLIRHG QSEWNVENRF TGWTDVDLSS KGLEEAREAG VMLKASGFSF DIAYTSVLRR 70 80 90 100 110 120 AMRTLWITLE EMDLMWIPVY KTWKLNERHY GALQGLNKEE TARKYGDEQV TLWRRSTNVR 130 140 150 160 170 180 PPALTKDDER YEAAHPKYRD IKDYEFPLTE DLEDTEKRVV SYWNEEIAPN VKAGKQVIIA 190 200 210 220 230 240 AHGNTIRALV KHLDQISDKD IENVNIPTGT PLVYELDNDL KPIGHYYLNR EIETLEEKQV

References

[1]

"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1." Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D. Nucleic Acids Res. 32:977-988(2004) [PubMed: 14960714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE017194 Genomic DNA. Translation: AAS42670.1.
RefSeq	NP_980062.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q732Z5.
Genome annotation databases
GeneID	2752317.
GenomeReviews	Gene locus BCE_3765 in contig AE017194_GR.
KEGG	bca:BCE_3765.
NMPDR	fig|222523.1.peg.3734.
TIGR	BCE_3765.
Phylogenomic databases
HOGENOM	Q732Z5.
OMA	PMRFLGD.
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

GPMA2_BACC1

Accession

Primary (citable) accession number: Q732Z5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	July 5, 2004
Last modified:	November 3, 2009
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)