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G4Q0P7 (G4Q0P7_ECOLX) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 14. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP-Rule MF_01039

Short name=BPG-dependent PGAM HAMAP-Rule MF_01039
Short name=PGAM HAMAP-Rule MF_01039
Short name=Phosphoglyceromutase HAMAP-Rule MF_01039
Short name=dPGM HAMAP-Rule MF_01039
EC=5.4.2.11 HAMAP-Rule MF_01039
Gene names
Name:gpmA HAMAP-Rule MF_01039 EMBL AEQ11584.1
ORF Names:CE10_0759 EMBL AEQ11584.1
OrganismEscherichia coli O7:K1 str. CE10 [Complete proteome] EMBL AEQ11584.1
Taxonomic identifier1072459 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length250 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate By similarity. RuleBase RU004512 HAMAP-Rule MF_01039

Catalytic activity

2-phospho-D-glycerate = 3-phospho-D-glycerate. SAAS SAAS001345 RuleBase RU004512 HAMAP-Rule MF_01039

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. RuleBase RU004512 HAMAP-Rule MF_01039

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01039

Sequence similarities

Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily. HAMAP-Rule MF_01039

Ontologies

Keywords
   Biological processGlycolysis SAAS SAAS001345 HAMAP-Rule MF_01039
   Molecular functionIsomerase SAAS SAAS001345 HAMAP-Rule MF_01039
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_function2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region23 – 2422-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region89 – 9242-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region116 – 11722-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039

Sites

Active site111Tele-phosphohistidine intermediate By similarity HAMAP-Rule MF_01039
Active site1841 By similarity HAMAP-Rule MF_01039
Binding site1712-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site6212-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site10012-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site18612-phospho-D-glycerate By similarity HAMAP-Rule MF_01039

Sequences

Sequence LengthMass (Da)Tools
G4Q0P7 [UniParc].

Last modified December 14, 2011. Version 1.
Checksum: A6E0A49406F8482A

FASTA25028,556
        10         20         30         40         50         60 
MAVTKLVLVR HGESQWNKEN RFTGWYDVDL SEKGVSEAKA AGKLLKEEGY SFDFAYTSVL 

        70         80         90        100        110        120 
KRAIHTLWNV LDELDQAWLP VEKSWKLNER HYGALQGLNK AETAEKYGDE QVKQWRRGFA 

       130        140        150        160        170        180 
VTPPELTKDD ERYPGHDPRY AKLSEKELPL TESLALTIDR VIPYWNETIL PRMKSGERVI 

       190        200        210        220        230        240 
IAAHGNSLRA LVKYLDNMSE EEILELNIPT GVPLVYEFDE NFKPLKRYYL GNADEIAAKA 

       250 
AAVANQGKAK 

« Hide

References

[1]"Complete Genome Sequence of the Neonatal-Meningitis-Associated Escherichia coli Strain CE10."
Lu S., Zhang X., Zhu Y., Kim K.S., Yang J., Jin Q.
J. Bacteriol. 193:7005-7005(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: CE10 EMBL AEQ11584.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP003034 Genomic DNA. Translation: AEQ11584.1.
RefSeqYP_006142868.1. NC_017646.1.

3D structure databases

ProteinModelPortalG4Q0P7.
SMRG4Q0P7. Positions 2-248.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEG4Q0P7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEQ11584; AEQ11584; CE10_0759.
GeneID12673564.
KEGGeoc:CE10_0759.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01834.
OMASYYLGDQ.

Enzyme and pathway databases

BioCycECOL1072459:GLD5-759-MONOMER.
UniPathwayUPA00109; UER00186.

Family and domain databases

HAMAPMF_01039. PGAM_GpmA.
InterProIPR013078. His_Pase_superF_clade-1.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]
PANTHERPTHR11931. PTHR11931. 1 hit.
PfamPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTSM00855. PGAM. 1 hit.
[Graphical view]
TIGRFAMsTIGR01258. pgm_1. 1 hit.
PROSITEPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameG4Q0P7_ECOLX
AccessionPrimary (citable) accession number: G4Q0P7
Entry history
Integrated into UniProtKB/TrEMBL: December 14, 2011
Last sequence update: December 14, 2011
Last modified: February 19, 2014
This is version 14 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)