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P44865 (GPMA_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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=5.4.2.1
Gene names
Name:gpmA
Synonyms:gpm
Ordered Locus Names:HI_0757
OrganismHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]
Taxonomic identifier71421 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

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
Reference proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: HAMAP

   Molecular_function2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity

Inferred from electronic annotation. Source: 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_0000179882

Sites

Active site81Tele-phosphohistidine intermediate By similarity
Active site1811 By similarity
Site591Interaction with carboxyl group of phosphoglycerates By similarity

Sequences

Sequence LengthMass (Da)Tools
P44865 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 3B846676BDFB561E

FASTA22726,049
        10         20         30         40         50         60 
MELVFIRHGF SEWNAKNLFT GWRDVNLTER GVEEAKTAGK KLLDKGYEFD IAFTSVLTRA 

        70         80         90        100        110        120 
IKTCNIVLEE SHQLWIPQVK NWRLNERHYG ALQGLDKKAT AEQYGDEQVH IWRRSYDISP 

       130        140        150        160        170        180 
PDLDPQDPNS AHNDRRYANI PSDVVPNAEN LKLTLERALP FWEDQIAPAM LSGKRVLVVA 

       190        200        210        220 
HGNSLRALAK HIIGISDAEI MDFEIPTGQP LVLKLDDKLN YVEHYYL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L42023 Genomic DNA. Translation: AAC22416.1.
PIRA64091.
RefSeqNP_438916.1. NC_000907.1.

3D structure databases

ProteinModelPortalP44865.
SMRP44865. Positions 2-227.
ModBaseSearch...

Protein-protein interaction databases

STRING71421.HI0757.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC22416; AAC22416; HI_0757.
GeneID949776.
KEGGhin:HI0757.
PATRIC20190159. VBIHaeInf48452_0795.

Phylogenomic databases

eggNOGCOG0588.
KOK01834.
OMAGQSDWNL.
ProtClustDBPRK14118.

Enzyme and pathway databases

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.
PROSITEPS00175. PG_MUTASE. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGPMA_HAEIN
AccessionPrimary (citable) accession number: P44865
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 1, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families