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Protein

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase

Gene

gpmA

Organism
Burkholderia mallei (strain NCTC 10247)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

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

BioCyciBMAL320389:GH97-2828-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:BMA10247_2838
OrganismiBurkholderia mallei (strain NCTC 10247)
Taxonomic identifieri320389 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
ProteomesiUP000002284: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2492492,3-bisphosphoglycerate-dependent phosphoglycerate mutasePRO_1000064039Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi320389.BMA10247_2838.

Structurei

3D structure databases

ProteinModelPortaliA3MQ23.
SMRiA3MQ23. Positions 2-236.
ModBaseiSearch...
MobiDBiSearch...

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.

A3MQ23-1 [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:April 3, 2007 - v1
Checksum:iE51933D372E4896E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000548 Genomic DNA. Translation: ABO06642.1.
RefSeqiYP_001082359.1. NC_009080.1.

Genome annotation databases

EnsemblBacteriaiABO06642; ABO06642; BMA10247_2838.
GeneIDi4893664.
KEGGibmn:BMA10247_2838.
PATRICi19148020. VBIBurMal96640_5042.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000548 Genomic DNA. Translation: ABO06642.1.
RefSeqiYP_001082359.1. NC_009080.1.

3D structure databases

ProteinModelPortaliA3MQ23.
SMRiA3MQ23. Positions 2-236.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi320389.BMA10247_2838.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABO06642; ABO06642; BMA10247_2838.
GeneIDi4893664.
KEGGibmn:BMA10247_2838.
PATRICi19148020. VBIBurMal96640_5042.

Phylogenomic databases

eggNOGiCOG0588.
HOGENOMiHOG000221682.
KOiK01834.
OMAiDRVLPYW.
OrthoDBiEOG6C8N1H.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00186.
BioCyciBMAL320389:GH97-2828-MONOMER.

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. DeShazer D., Woods D.E., Nierman W.C.
    Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NCTC 10247.

Entry informationi

Entry nameiGPMA_BURM7
AccessioniPrimary (citable) accession number: A3MQ23
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: April 3, 2007
Last modified: January 7, 2015
This is version 52 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

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.