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Protein

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase

Gene

gpmA

Organism
Burkholderia pseudomallei (strain K96243)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.UniRule annotation

Catalytic activityi

2-phospho-D-glycerate = 3-phospho-D-glycerate.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei9 – 91Tele-phosphohistidine intermediateUniRule annotation
Binding sitei15 – 1512-phospho-D-glycerateUniRule annotation
Binding sitei60 – 6012-phospho-D-glycerateUniRule annotation
Binding sitei98 – 9812-phospho-D-glycerateUniRule annotation
Active sitei182 – 1821UniRule annotation
Binding sitei184 – 18412-phospho-D-glycerateUniRule annotation

GO - Molecular functioni

  1. 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. glycolytic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Glycolysis

Enzyme and pathway databases

BioCyciBPSE272560:GJNI-450-MONOMER.
UniPathwayiUPA00109; UER00186.

Names & Taxonomyi

Protein namesi
Recommended name:
2,3-bisphosphoglycerate-dependent phosphoglycerate mutaseUniRule annotation (EC:5.4.2.11UniRule annotation)
Short name:
BPG-dependent PGAMUniRule annotation
Short name:
PGAMUniRule annotation
Short name:
PhosphoglyceromutaseUniRule annotation
Short name:
dPGMUniRule annotation
Gene namesi
Name:gpmAUniRule annotation
Ordered Locus Names:BPSL0443
OrganismiBurkholderia pseudomallei (strain K96243)
Taxonomic identifieri272560 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
ProteomesiUP000000605: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2492492,3-bisphosphoglycerate-dependent phosphoglycerate mutasePRO_0000229112Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi272560.BPSL0443.

Structurei

Secondary structure

1
249
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 87Combined sources
Helixi13 – 164Combined sources
Helixi30 – 4516Combined sources
Beta strandi51 – 555Combined sources
Helixi59 – 7214Combined sources
Beta strandi79 – 813Combined sources
Helixi83 – 853Combined sources
Helixi91 – 933Combined sources
Helixi98 – 1058Combined sources
Helixi107 – 1159Combined sources
Helixi136 – 1383Combined sources
Helixi143 – 1453Combined sources
Helixi152 – 16514Combined sources
Helixi167 – 1726Combined sources
Beta strandi177 – 1815Combined sources
Helixi183 – 19412Combined sources
Helixi198 – 2014Combined sources
Beta strandi212 – 2165Combined sources
Beta strandi222 – 2276Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GW8X-ray1.93A/B1-249[»]
ProteinModelPortaliQ63XU7.
SMRiQ63XU7. Positions 2-236.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ63XU7.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni21 – 2222-phospho-D-glycerate bindingUniRule annotation
Regioni87 – 9042-phospho-D-glycerate bindingUniRule annotation
Regioni114 – 11522-phospho-D-glycerate bindingUniRule annotation

Sequence similaritiesi

Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0588.
HOGENOMiHOG000221682.
KOiK01834.
OMAiDRVLPYW.
OrthoDBiEOG6C8N1H.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
HAMAPiMF_01039. PGAM_GpmA.
InterProiIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]
PANTHERiPTHR11931. PTHR11931. 1 hit.
PfamiPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 1 hit.
TIGRFAMsiTIGR01258. pgm_1. 1 hit.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q63XU7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MYKLVLIRHG ESTWNKENRF TGWVDVDLTE QGNREARQAG QLLKEAGYTF
60 70 80 90 100
DIAYTSVLKR AIRTLWHVQD QMDLMYVPVV HSWRLNERHY GALSGLNKAE
110 120 130 140 150
TAAKYGDEQV LVWRRSYDTP PPALEPGDER APYADPRYAK VPREQLPLTE
160 170 180 190 200
CLKDTVARVL PLWNESIAPA VKAGKQVLIA AHGNSLRALI KYLDGISDAD
210 220 230 240
IVGLNIPNGV PLVYELDESL TPIRHYYLGD QEAIAKAQAA VAQQGKSAA
Length:249
Mass (Da):27,893
Last modified:October 25, 2004 - v1
Checksum:iE51933D372E4896E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX571965 Genomic DNA. Translation: CAH34431.1.
RefSeqiYP_107068.1. NC_006350.1.

Genome annotation databases

EnsemblBacteriaiCAH34431; CAH34431; BPSL0443.
GeneIDi3093540.
KEGGibps:BPSL0443.
PATRICi19260531. VBIBurPse99623_0497.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX571965 Genomic DNA. Translation: CAH34431.1.
RefSeqiYP_107068.1. NC_006350.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GW8X-ray1.93A/B1-249[»]
ProteinModelPortaliQ63XU7.
SMRiQ63XU7. Positions 2-236.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272560.BPSL0443.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAH34431; CAH34431; BPSL0443.
GeneIDi3093540.
KEGGibps:BPSL0443.
PATRICi19260531. VBIBurPse99623_0497.

Phylogenomic databases

eggNOGiCOG0588.
HOGENOMiHOG000221682.
KOiK01834.
OMAiDRVLPYW.
OrthoDBiEOG6C8N1H.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00186.
BioCyciBPSE272560:GJNI-450-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ63XU7.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
HAMAPiMF_01039. PGAM_GpmA.
InterProiIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]
PANTHERiPTHR11931. PTHR11931. 1 hit.
PfamiPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 1 hit.
TIGRFAMsiTIGR01258. pgm_1. 1 hit.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K96243.

Entry informationi

Entry nameiGPMA_BURPS
AccessioniPrimary (citable) accession number: Q63XU7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: October 25, 2004
Last modified: January 7, 2015
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.