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Q0I4D8 (GPMA_HISS1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

Short name=BPG-dependent PGAM
Short name=PGAM
Short name=Phosphoglyceromutase
Short name=dPGM
EC=5.4.2.11
Gene names
Name:gpmA
Ordered Locus Names:HS_1445
OrganismHistophilus somni (strain 129Pt) (Haemophilus somnus) [Complete proteome] [HAMAP]
Taxonomic identifier205914 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHistophilus

Protein attributes

Sequence length227 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

Catalytic activity

2-phospho-D-glycerate = 3-phospho-D-glycerate. HAMAP-Rule MF_01039

Pathway

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

Sequence similarities

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

Ontologies

Keywords
   Biological processGlycolysis
   Molecular functionIsomerase
   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

Molecule processing

Chain1 – 2272272,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP-Rule MF_01039
PRO_1000064064

Regions

Region20 – 2122-phospho-D-glycerate binding By similarity
Region86 – 8942-phospho-D-glycerate binding By similarity
Region113 – 11422-phospho-D-glycerate binding By similarity

Sites

Active site81Tele-phosphohistidine intermediate By similarity
Active site1811 By similarity
Binding site1412-phospho-D-glycerate By similarity
Binding site5912-phospho-D-glycerate By similarity
Binding site9712-phospho-D-glycerate By similarity
Binding site18312-phospho-D-glycerate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0I4D8 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: FFC3CC21130086FA

FASTA22726,015
        10         20         30         40         50         60 
MELVFIRHGF SEWNAKNLFT GWRDVNLTER GIEEAKAAGK KLLEAGYEFD IAFTSVLTRA 

        70         80         90        100        110        120 
IKTCNIVLEE SNQLWIPQVK HWRLNERHYG ALQGLDKKAT AEQYGDEQVH IWRRSYDVSP 

       130        140        150        160        170        180 
PDLDPQDPNS AHNDRRYALL PKDVVPNAEN LKITLERVLP FWEDQIAPAL LSGKRVLVTA 

       190        200        210        220 
HGNSLRALAK HIIGISDEEI MAFEIPTGQP LVLKLDEQLN FVEKFYL 

« Hide

References

[1]"Complete genome sequence of Haemophilus somnus (Histophilus somni) strain 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus influenzae Rd."
Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O., Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N., Xie G., Inzana T.J.
J. Bacteriol. 189:1890-1898(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 129Pt.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000436 Genomic DNA. Translation: ABI25720.1.
RefSeqYP_719657.1. NC_008309.1.

3D structure databases

ProteinModelPortalQ0I4D8.
SMRQ0I4D8. Positions 2-227.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING205914.HS_1445.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI25720; ABI25720; HS_1445.
GeneID4240961.
KEGGhso:HS_1445.
PATRIC20283009. VBIHaeSom53361_1520.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0588.
HOGENOMHOG000221682.
KOK01834.
OMASYYLGDQ.
OrthoDBEOG6C8N1H.
ProtClustDBPRK14118.

Enzyme and pathway databases

BioCycHSOM205914:GJ7V-1505-MONOMER.
UniPathwayUPA00109; UER00186.

Family and domain databases

HAMAPMF_01039. PGAM_GpmA.
InterProIPR013078. His_Pase_superF_clade-1.
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.
ProtoNetSearch...

Entry information

Entry nameGPMA_HISS1
AccessionPrimary (citable) accession number: Q0I4D8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 3, 2006
Last modified: February 19, 2014
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways