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C9R7A9 (C9R7A9_AGGAD) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 29. 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
Ordered Locus Names:D11S_0142 EMBL ACX81561.1
OrganismAggregatibacter actinomycetemcomitans serotype C (strain D11S-1) (Actinobacillus actinomycetemcomitans) [Complete proteome] [HAMAP] EMBL ACX81561.1
Taxonomic identifier668336 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeAggregatibacter

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 SAAS SAAS013078

Catalytic activity

2-phospho-D-glycerate = 3-phospho-D-glycerate. HAMAP-Rule MF_01039 SAAS SAAS013078

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. HAMAP-Rule MF_01039 SAAS SAAS013078

Sequence similarities

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

Ontologies

Keywords
   Biological processGlycolysis HAMAP-Rule MF_01039 SAAS SAAS013078
   Molecular functionIsomerase HAMAP-Rule MF_01039 SAAS SAAS013078
   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

Region20 – 2122-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region86 – 8942-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region113 – 11422-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039

Sites

Active site81Tele-phosphohistidine intermediate By similarity HAMAP-Rule MF_01039
Active site1811 By similarity HAMAP-Rule MF_01039
Binding site1412-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site5912-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site9712-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site18312-phospho-D-glycerate By similarity HAMAP-Rule MF_01039

Sequences

Sequence LengthMass (Da)Tools
C9R7A9 [UniParc].

Last modified November 24, 2009. Version 1.
Checksum: BEEF0F54726272FB

FASTA22725,969
        10         20         30         40         50         60 
MELVFIRHGF SEWNAKNLFT GWRDVNLTER GVEEAKAAGK KLLDAGFEFD IAFTSVLTRA 

        70         80         90        100        110        120 
IKTCNIVLEE SHQLWIPQVK NWRLNERHYG ELQGLDKKAT AEKYGDEQVH IWRRSYDTLP 

       130        140        150        160        170        180 
PLLDPKDPNS AHNDRRYAHL PDDVIPDGEN LKVTLARVLP FWDDQIALAL LSGKRVLVVA 

       190        200        210        220 
HGNSLRALAK HIEGISDADI MDLEIPTGQP LVYKLDDNLK MVEKFYL 

« Hide

References

[1]"Genome sequence of Aggregatibacter actinomycetemcomitans serotype c strain D11S-1."
Chen C., Kittichotirat W., Si Y., Bumgarner R.
J. Bacteriol. 191:7378-7379(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: D11S-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001733 Genomic DNA. Translation: ACX81561.1.
RefSeqYP_003254780.1. NC_013416.1.

3D structure databases

ProteinModelPortalC9R7A9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING668336.D11S_0142.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACX81561; ACX81561; D11S_0142.
GeneID8535861.
KEGGaat:D11S_0142.
PATRIC31911086. VBIAggAct139153_0132.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0588.
HOGENOMHOG000221682.
KOK01834.
OMASYYLGDQ.
OrthoDBEOG6C8N1H.

Enzyme and pathway databases

BioCycAACT668336:GJBF-142-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 nameC9R7A9_AGGAD
AccessionPrimary (citable) accession number: C9R7A9
Entry history
Integrated into UniProtKB/TrEMBL: November 24, 2009
Last sequence update: November 24, 2009
Last modified: February 19, 2014
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)