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Protein

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase

Gene

gpmA

Organism
Acidovorax ebreus (strain TPSY) (Diaphorobacter sp. (strain TPSY))
Status
Reviewed-Annotation score: Annotation score: 3 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

Pathway: glycolysis

This protein is involved in step 3 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.UniRule annotation
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Phosphoglycerate kinase (pgk)
  3. 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA)
  4. Enolase (eno)
  5. Pyruvate kinase (Dtpsy_3305)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei9 – 91Tele-phosphohistidine intermediateUniRule annotation
Binding sitei60 – 601SubstrateUniRule annotation
Binding sitei98 – 981SubstrateUniRule annotation
Active sitei182 – 1821UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Gluconeogenesis, Glycolysis

Enzyme and pathway databases

BioCyciAEBR535289:GHOO-2873-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:Dtpsy_2828
OrganismiAcidovorax ebreus (strain TPSY) (Diaphorobacter sp. (strain TPSY))
Taxonomic identifieri535289 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeAcidovorax
ProteomesiUP000000450 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2472472,3-bisphosphoglycerate-dependent phosphoglycerate mutasePRO_1000149510Add
BLAST

Proteomic databases

PRIDEiB9MEZ2.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi535289.Dtpsy_2828.

Structurei

3D structure databases

ProteinModelPortaliB9MEZ2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni8 – 158Substrate bindingUniRule annotation
Regioni21 – 222Substrate bindingUniRule annotation
Regioni87 – 904Substrate bindingUniRule annotation
Regioni114 – 1152Substrate bindingUniRule annotation
Regioni183 – 1842Substrate 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.

B9MEZ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHKLVLIRHG ESTWNLENRF TGWTDVDLTP TGIEQAKNAG RLLKAEGYEF
60 70 80 90 100
DLAYTSVLKR ATRTLWHCLD EMDRTWLPVE HSWRLNERHY GALQGLNKAD
110 120 130 140 150
MAKQYGDAQV LVWRRSYDTP PPALETTDPR SERGDLRYAG LQAGEVPLTE
160 170 180 190 200
CLKDTVARVL PYWNESIAPA IRSGKRVLIA AHGNSIRALV KYLDNISDQD
210 220 230 240
IVGLNIPNGI PLVYELDADL KPLRHYYLGD AEAAAKAAAA VASQGKA
Length:247
Mass (Da):27,648
Last modified:March 24, 2009 - v1
Checksum:i32A61BED9F3EC44D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001392 Genomic DNA. Translation: ACM34262.1.
RefSeqiWP_015914139.1. NC_011992.1.
YP_002554262.1. NC_011992.1.

Genome annotation databases

EnsemblBacteriaiACM34262; ACM34262; Dtpsy_2828.
KEGGidia:Dtpsy_2828.
PATRICi21782797. VBIDiaSp55748_2870.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001392 Genomic DNA. Translation: ACM34262.1.
RefSeqiWP_015914139.1. NC_011992.1.
YP_002554262.1. NC_011992.1.

3D structure databases

ProteinModelPortaliB9MEZ2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi535289.Dtpsy_2828.

Proteomic databases

PRIDEiB9MEZ2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACM34262; ACM34262; Dtpsy_2828.
KEGGidia:Dtpsy_2828.
PATRICi21782797. VBIDiaSp55748_2870.

Phylogenomic databases

eggNOGiCOG0588.
HOGENOMiHOG000221682.
KOiK01834.
OMAiDRVLPYW.
OrthoDBiEOG6C8N1H.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00186.
BioCyciAEBR535289:GHOO-2873-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: TPSY.

Entry informationi

Entry nameiGPMA_ACIET
AccessioniPrimary (citable) accession number: B9MEZ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: June 24, 2015
This is version 45 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.