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H2H2H1 (H2H2H1_CORDD) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 15. 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 AEX71341.1
Ordered Locus Names:CDCE8392_0339 EMBL AEX71341.1
OrganismCorynebacterium diphtheriae (strain CDCE 8392) [Complete proteome] [HAMAP] EMBL AEX71341.1
Taxonomic identifier698965 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length248 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. RuleBase RU004512 HAMAP-Rule MF_01039 SAAS SAAS001345

Pathway

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

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 SAAS001345
   Molecular functionIsomerase HAMAP-Rule MF_01039 SAAS SAAS001345 EMBL AEX71341.1
   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 site1821 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 site18412-phospho-D-glycerate By similarity HAMAP-Rule MF_01039

Sequences

Sequence LengthMass (Da)Tools
H2H2H1 [UniParc].

Last modified March 21, 2012. Version 1.
Checksum: FE74E05C8608052E

FASTA24827,333
        10         20         30         40         50         60 
MTTGKLILLR HGQSEWNASN QFTGWVDVNL TEKGEAEAKR GGELLKAQGV LPSVVYTSLL 

        70         80         90        100        110        120 
RRAIRTANIA LNAADRHWIP VVRDWRLNER HYGALQGLNK AETKEKYGDE QFMAWRRSYG 

       130        140        150        160        170        180 
TPPPELEDSS EFSQANDPRY ANLDVVPRTE CLKDVVERFV PYFKEEILPR VQNGETVLIA 

       190        200        210        220        230        240 
AHGNSLRALV KHLDNISDAD IAELNIPTGI PLVYELDEAG TVLNPGGTYL DPEAAAAGAA 


AVAAQGTK 

« Hide

References

[1]"Pangenomic Study of Corynebacterium diphtheriae That Provides Insights into the Genomic Diversity of Pathogenic Isolates from Cases of Classical Diphtheria, Endocarditis, and Pneumonia."
Trost E., Blom J., de Castro Soares S., Huang I.H., Al-Dilaimi A., Schroder J., Jaenicke S., Dorella F.A., Rocha F.S., Miyoshi A., Azevedo V., Schneider M.P., Silva A., Camello T.C., Sabbadini P.S., Santos C.S., Santos L.S., Hirata R.Jr. expand/collapse author list , Mattos-Guaraldi A.L., Efstratiou A., Schmitt M.P., Ton-That H., Tauch A.
J. Bacteriol. 194:3199-3215(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDCE 8392 EMBL AEX71341.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP003211 Genomic DNA. Translation: AEX71341.1.
RefSeqYP_005132889.1. NC_016785.1.

3D structure databases

ProteinModelPortalH2H2H1.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEX71341; AEX71341; CDCE8392_0339.
GeneID11707718.
KEGGcdd:CDCE8392_0339.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01834.

Enzyme and pathway databases

BioCycCDIP698965:GHJP-353-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 nameH2H2H1_CORDD
AccessionPrimary (citable) accession number: H2H2H1
Entry history
Integrated into UniProtKB/TrEMBL: March 21, 2012
Last sequence update: March 21, 2012
Last modified: April 16, 2014
This is version 15 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)