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Protein

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase

Gene

gpmA

Organism
Pantoea vagans (strain C9-1) (Pantoea agglomerans (strain C9-1))
Status
Unreviewed-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 annotationSAAS annotation

Pathway:iglycolysis

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), Phosphoglycerate kinase (pgk)
  3. Probable phosphoglycerate mutase GpmB (gpmB), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpma3)
  4. Enolase (eno), Enolase (eno)
  5. Pyruvate kinase (pykA), Pyruvate kinase (pykF)
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 sitei11 – 111Tele-phosphohistidine intermediateUniRule annotation
Binding sitei62 – 621SubstrateUniRule annotation
Binding sitei100 – 1001SubstrateUniRule annotation
Active sitei184 – 1841UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

IsomeraseUniRule annotationSAAS annotation

Keywords - Biological processi

GluconeogenesisUniRule annotation, GlycolysisUniRule annotationSAAS annotation

Enzyme and pathway databases

BioCyciPVAG712898:GHQ2-576-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
Synonyms:gpma1Imported
Ordered Locus Names:Pvag_0576Imported
OrganismiPantoea vagans (strain C9-1) (Pantoea agglomerans (strain C9-1))Imported
Taxonomic identifieri712898 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePantoea
ProteomesiUP000006631 Componenti: Chromosome

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi712898.Pvag_0576.

Structurei

3D structure databases

ProteinModelPortaliE1SH37.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni10 – 178Substrate bindingUniRule annotation
Regioni23 – 242Substrate bindingUniRule annotation
Regioni89 – 924Substrate bindingUniRule annotation
Regioni116 – 1172Substrate bindingUniRule annotation
Regioni185 – 1862Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000221682.
KOiK01834.
OMAiPIKRYYL.

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.

E1SH37-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVTKLVLVR HGESQWNNEN RFTGWYDVDL SEKGRGEAKS AGQLLKKEGF
60 70 80 90 100
VFDFAYTSVL KRAIHTLWNV LDELDQAWLP VEKTWRLNER HYGALQGLDK
110 120 130 140 150
AETAAKYGDE QVKQWRRGFA VTPPELDRSD ERFPGHDPRY AKLTPEQLPT
160 170 180 190 200
TESLALTIDR VIPYWNDTIL PRIKSGEKVI IAAHGNSLRA LVKYLDNLSE
210 220 230 240 250
DEILELNIPT GVPLVYEFDE NFKPLKRYYL GDQDEIAAKA AAVANQGKAK
Length:250
Mass (Da):28,499
Last modified:November 30, 2010 - v1
Checksum:iDD803BFE07E7E5C7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002206 Genomic DNA. Translation: ADO08778.1.
RefSeqiWP_003851893.1. NC_014562.1.

Genome annotation databases

EnsemblBacteriaiADO08778; ADO08778; Pvag_0576.
KEGGipva:Pvag_0576.
PATRICi42417205. VBIPanVag152020_0724.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002206 Genomic DNA. Translation: ADO08778.1.
RefSeqiWP_003851893.1. NC_014562.1.

3D structure databases

ProteinModelPortaliE1SH37.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi712898.Pvag_0576.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADO08778; ADO08778; Pvag_0576.
KEGGipva:Pvag_0576.
PATRICi42417205. VBIPanVag152020_0724.

Phylogenomic databases

HOGENOMiHOG000221682.
KOiK01834.
OMAiPIKRYYL.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00186.
BioCyciPVAG712898:GHQ2-576-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. "The genome sequence of the biocontrol agent Pantoea vagans strain C9-1."
    Smits T.H., Rezzonico F., Kamber T., Goesmann A., Ishimaru C.A., Stockwell V.O., Frey J.E., Duffy B.
    J. Bacteriol. 192:6486-6487(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C9-1Imported.

Entry informationi

Entry nameiE1SH37_PANVC
AccessioniPrimary (citable) accession number: E1SH37
Entry historyi
Integrated into UniProtKB/TrEMBL: November 30, 2010
Last sequence update: November 30, 2010
Last modified: July 22, 2015
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

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.