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Protein

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase

Gene

gpmA

Organism
Polynucleobacter necessarius subsp. asymbioticus (strain DSM 18221 / CIP 109841 / QLW-P1DMWA-1)
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

BioCyciPNEC312153:GH50-1991-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:Pnuc_1948
OrganismiPolynucleobacter necessarius subsp. asymbioticus (strain DSM 18221 / CIP 109841 / QLW-P1DMWA-1)
Taxonomic identifieri312153 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaePolynucleobacter
ProteomesiUP000000231: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2292292,3-bisphosphoglycerate-dependent phosphoglycerate mutasePRO_1000084327Add
BLAST

Proteomic databases

PRIDEiA4T096.

Interactioni

Protein-protein interaction databases

STRINGi312153.Pnuc_1948.

Structurei

3D structure databases

ProteinModelPortaliA4T096.
SMRiA4T096. Positions 3-228.
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.

A4T096-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKQLVLIRHG ESAWNLENRF TGWADVDLTP KGAEQALAAG EHLRKAGYEF
60 70 80 90 100
DVAYTSVLRR AIRTLWHVQD AMDLMWLPVV HSWRLNERHY GALTGLNKAE
110 120 130 140 150
TAAQYGDEQV HIWRRSYDIR PPLLEADDER NPKNDSRYAK LNESDIPLGE
160 170 180 190 200
CLKDNVERVL PLWNESIAPA LKANKRVLLV AHGNSIRSLI KYLDQMSDEA
210 220
IMEVNVPNGI PLVYELDDNL KPIQHFYLD
Length:229
Mass (Da):26,322
Last modified:May 15, 2007 - v1
Checksum:iE946BD6C41659698
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000655 Genomic DNA. Translation: ABP35160.1.
RefSeqiYP_001156724.1. NC_009379.1.

Genome annotation databases

EnsemblBacteriaiABP35160; ABP35160; Pnuc_1948.
GeneIDi5053013.
KEGGipnu:Pnuc_1948.
PATRICi22968421. VBIPolNec12025_2014.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000655 Genomic DNA. Translation: ABP35160.1.
RefSeqiYP_001156724.1. NC_009379.1.

3D structure databases

ProteinModelPortaliA4T096.
SMRiA4T096. Positions 3-228.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi312153.Pnuc_1948.

Proteomic databases

PRIDEiA4T096.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABP35160; ABP35160; Pnuc_1948.
GeneIDi5053013.
KEGGipnu:Pnuc_1948.
PATRICi22968421. VBIPolNec12025_2014.

Phylogenomic databases

eggNOGiCOG0588.
HOGENOMiHOG000221682.
KOiK01834.
OMAiDRVLPYW.
OrthoDBiEOG6C8N1H.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00186.
BioCyciPNEC312153:GH50-1991-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: DSM 18221 / CIP 109841 / QLW-P1DMWA-1.

Entry informationi

Entry nameiGPMA_POLSQ
AccessioniPrimary (citable) accession number: A4T096
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 15, 2007
Last modified: January 7, 2015
This is version 57 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, Reference 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.