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A4T096

- GPMA_POLSQ

UniProt

A4T096 - GPMA_POLSQ

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Protein

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase

Gene
gpmA, Pnuc_1948
Organism
Polynucleobacter necessarius subsp. asymbioticus (strain DSM 18221 / CIP 109841 / QLW-P1DMWA-1)
Status
Reviewed - Annotation score: 2 out of 5 - Protein inferred from homologyi

Functioni

Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate By similarity.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 intermediate By similarity
Binding sitei15 – 1512-phospho-D-glycerate By similarity
Binding sitei60 – 6012-phospho-D-glycerate By similarity
Binding sitei98 – 9812-phospho-D-glycerate By similarity
Active sitei182 – 1821 By similarity
Binding sitei184 – 18412-phospho-D-glycerate By similarity

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 mutase (EC:5.4.2.11)
Short name:
BPG-dependent PGAM
Short name:
PGAM
Short name:
Phosphoglyceromutase
Short name:
dPGM
Gene namesi
Name:gpmA
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 mutaseUniRule annotationPRO_1000084327Add
BLAST

Proteomic databases

PRIDEiA4T096.

Interactioni

Protein-protein interaction databases

STRINGi312153.Pnuc_1948.

Structurei

3D structure databases

ProteinModelPortaliA4T096.
SMRiA4T096. Positions 3-228.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni21 – 2222-phospho-D-glycerate binding By similarity
Regioni87 – 9042-phospho-D-glycerate binding By similarity
Regioni114 – 11522-phospho-D-glycerate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0588.
HOGENOMiHOG000221682.
KOiK01834.
OMAiKDDERFP.
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

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MKQLVLIRHG ESAWNLENRF TGWADVDLTP KGAEQALAAG EHLRKAGYEF    50
DVAYTSVLRR AIRTLWHVQD AMDLMWLPVV HSWRLNERHY GALTGLNKAE 100
TAAQYGDEQV HIWRRSYDIR PPLLEADDER NPKNDSRYAK LNESDIPLGE 150
CLKDNVERVL PLWNESIAPA LKANKRVLLV AHGNSIRSLI KYLDQMSDEA 200
IMEVNVPNGI PLVYELDDNL KPIQHFYLD 229
Length:229
Mass (Da):26,322
Last modified:May 15, 2007 - v1
Checksum:iE946BD6C41659698
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
CP000655 Genomic DNA. Translation: ABP35160.1 .
RefSeqi YP_001156724.1. NC_009379.1.

3D structure databases

ProteinModelPortali A4T096.
SMRi A4T096. Positions 3-228.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 312153.Pnuc_1948.

Proteomic databases

PRIDEi A4T096.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABP35160 ; ABP35160 ; Pnuc_1948 .
GeneIDi 5053013.
KEGGi pnu:Pnuc_1948.
PATRICi 22968421. VBIPolNec12025_2014.

Phylogenomic databases

eggNOGi COG0588.
HOGENOMi HOG000221682.
KOi K01834.
OMAi KDDERFP.
OrthoDBi EOG6C8N1H.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00186 .
BioCyci PNEC312153:GH50-1991-MONOMER.

Family and domain databases

Gene3Di 3.40.50.1240. 1 hit.
HAMAPi MF_01039. PGAM_GpmA.
InterProi IPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view ]
PANTHERi PTHR11931. PTHR11931. 1 hit.
Pfami PF00300. His_Phos_1. 1 hit.
[Graphical view ]
SMARTi SM00855. PGAM. 1 hit.
[Graphical view ]
SUPFAMi SSF53254. SSF53254. 1 hit.
TIGRFAMsi TIGR01258. pgm_1. 1 hit.
PROSITEi PS00175. PG_MUTASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: June 11, 2014
This is version 55 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

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