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Q8NTA5 (GPMA_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 59. 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=5.4.2.1
Gene names
Name:gpmA
Ordered Locus Names:Cgl0402, cg0482
OrganismCorynebacterium glutamicum (Brevibacterium flavum)
Taxonomic identifier1718 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length248 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Pathway

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

   Molecular functionphosphoglycerate mutase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2482482,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP MF_01039
PRO_0000179871

Sites

Active site111Tele-phosphohistidine intermediate By similarity
Active site1821 By similarity
Site621Interaction with carboxyl group of phosphoglycerates By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8NTA5 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 699879F5A008CCB6

FASTA24827,246
        10         20         30         40         50         60 
MTNGKLILLR HGQSEWNASN QFTGWVDVNL TEQGEAEAKR GGELLVEAGV LPGVVYTSLL 

        70         80         90        100        110        120 
RRAIRTANIA LNAADRHWIP VIRDWRLNER HYGALQGLDK AATKEKYGDD QFMEWRRSYD 

       130        140        150        160        170        180 
TPPPELADDA EYSQANDPRY ADLDVVPRTE CLKDVVVRFV PYFEEEILPR AKKGETVLIA 

       190        200        210        220        230        240 
AHGNSLRALV KHLDGISDAD IAELNIPTGI PLVYEIAEDG SVVNPGGTYL DPEAAAAGAA 


AVANQGNK 

« Hide

References

[1]"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."
Nakagawa S.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000036 Genomic DNA. Translation: BAB97795.1.
BX927149 Genomic DNA. Translation: CAF19118.1.
RefSeqNP_599649.1. NC_003450.3.
YP_224704.1. NC_006958.1.

3D structure databases

ProteinModelPortalQ8NTA5.
SMRQ8NTA5. Positions 4-238.
ModBaseSearch...

2D gel databases

World-2DPAGE0001:Q8NTA5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1021136.
3344861.
GenomeReviewsGene locus Cgl0402 in contig BA000036_GR.
Gene locus cg0482 in contig BX927147_GR.
KEGGcgb:cg0482.
cgl:NCgl0390.
PATRIC21492862. VBICorGlu203724_0402.

Phylogenomic databases

HOGENOMHBG658938.
OMAEWNALNL.
PhylomeDBQ8NTA5.
ProtClustDBPRK14120.

Enzyme and pathway databases

BioCycCGLU196627:CG0482-MONOMER.

Family and domain databases

HAMAPMF_01039. PGAM_GpmA.
[Tree]
InterProIPR013078. His_Pase_superF_clade-1.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]
KOK01834.
PANTHERPTHR11931. Phosphogly_mut1. 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 nameGPMA_CORGL
AccessionPrimary (citable) accession number: Q8NTA5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 13, 2002
Last sequence update: October 1, 2002
Last modified: January 25, 2012
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families