Q63XU7 (GPMA_BURPS) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	gpmA
Ordered Locus Names:	BPSL0443

Organism

Burkholderia pseudomallei (strain K96243) [Reference proteome] [HAMAP]

Taxonomic identifier

272560 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group › Burkholderia pseudomallei

Protein attributes

Sequence length	249 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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

Ontologies

Keywords
Biological process	Glycolysis
Molecular function	Isomerase
Technical term	3D-structure Complete proteome Reference 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-Rule MF_01039

PRO_0000229112

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

Secondary structure

1

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249

Helix Strand Turn

Details...

Beta strand

2 – 8

7

Helix

13 – 16

4

Helix

30 – 45

16

Beta strand

51 – 55

5

Helix

59 – 72

14

Beta strand

79 – 81

3

Helix

83 – 85

3

Helix

91 – 93

3

Helix

98 – 105

8

Helix

107 – 115

9

Helix

136 – 138

3

Helix

143 – 145

3

Helix

152 – 165

14

Helix

167 – 172

6

Beta strand

177 – 181

5

Helix

183 – 194

12

Helix

198 – 201

4

Beta strand

212 – 216

5

Beta strand

222 – 227

6

Sequences

	Sequence		Length	Mass (Da)
	Q63XU7 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: E51933D372E4896E	FASTA	249	27,893
	10 20 30 40 50 60 MYKLVLIRHG ESTWNKENRF TGWVDVDLTE QGNREARQAG QLLKEAGYTF DIAYTSVLKR 70 80 90 100 110 120 AIRTLWHVQD QMDLMYVPVV HSWRLNERHY GALSGLNKAE TAAKYGDEQV LVWRRSYDTP 130 140 150 160 170 180 PPALEPGDER APYADPRYAK VPREQLPLTE CLKDTVARVL PLWNESIAPA VKAGKQVLIA 190 200 210 220 230 240 AHGNSLRALI KYLDGISDAD IVGLNIPNGV PLVYELDESL TPIRHYYLGD QEAIAKAQAA VAQQGKSAA

References

[1]

"Genomic plasticity of the causative agent of melioidosis, Burkholderia pseudomallei." Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M., Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F., Challis G.L. , Cherevach I., Chillingworth T., Cronin A., Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J. Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K96243.

+

Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BX571965 Genomic DNA. Translation: CAH34431.1.

RefSeq

YP_107068.1. NC_006350.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3GW8	X-ray	1.93	A/B	1-249	[»]

ProteinModelPortal

Q63XU7.

SMR

Q63XU7. Positions 2-236.

ModBase

Search...

Protein-protein interaction databases

STRING

272560.BPSL0443.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

3093540.

KEGG

bps:BPSL0443.

PATRIC

19260531. VBIBurPse99623_0497.

Phylogenomic databases

eggNOG

COG0588.

HOGENOM

HOG000221682.

KO

K01834.

OMA

GQSDWNL.

ProtClustDB

PRK14115.

Enzyme and pathway databases

BioCyc

BPSE272560:GJNI-450-MONOMER.

UniPathway

UPA00109; UER00186.

Family and domain databases

HAMAP

MF_01039. PGAM_GpmA.

InterPro

IPR013078. His_Pase_superF_clade-1.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]

PANTHER

PTHR11931. PTHR11931. 1 hit.

Pfam

PF00300. His_Phos_1. 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...

Other

EvolutionaryTrace

Q63XU7.

Entry information

Entry name

GPMA_BURPS

Accession

Primary (citable) accession number: Q63XU7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 4, 2006
Last sequence update:	October 25, 2004
Last modified:	May 1, 2013
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program