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Q4JSW4 (GPMA_CORJK) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 55. 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:jk1912
OrganismCorynebacterium jeikeium (strain K411) [Complete proteome] [HAMAP]
Taxonomic identifier306537 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length254 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 – 2542542,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP-Rule MF_01039
PRO_0000229118

Regions

Region28 – 2922-phospho-D-glycerate binding By similarity
Region94 – 9742-phospho-D-glycerate binding By similarity
Region121 – 12222-phospho-D-glycerate binding By similarity

Sites

Active site161Tele-phosphohistidine intermediate By similarity
Active site1871 By similarity
Binding site2212-phospho-D-glycerate By similarity
Binding site6712-phospho-D-glycerate By similarity
Binding site10512-phospho-D-glycerate By similarity
Binding site18912-phospho-D-glycerate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4JSW4 [UniParc].

Last modified August 2, 2005. Version 1.
Checksum: 98AD302DAB1A7BFF

FASTA25428,076
        10         20         30         40         50         60 
MSEQNNSHGN LILLRHGQSE WNASNQFTGW VDVRLTEKGR AEAVRGGEMI KEAGLEPTIL 

        70         80         90        100        110        120 
YTSLLRRAIT TANIALDAAD RHWIPVVRDW RLNERHYGAL QGLNKAETKD KYGEEQFMAW 

       130        140        150        160        170        180 
RRSYDTPPPA IDADNEYAQT NDPRYADLSE IPATECLLDV VKRFIPYYEE EIEPRVKNGE 

       190        200        210        220        230        240 
TVLVAAHGNS LRALVKHLDK ISDEDIAGLN IPTGIPLVYN IDADGKVLNP GGDYLDPEAA 

       250 
AAGAAAVAAQ GQAK 

« Hide

References

[1]"Complete genome sequence and analysis of the multiresistant nosocomial pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the human skin flora."
Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A., Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F., Rupp O., Schneiker S., Viehoever P., Puehler A.
J. Bacteriol. 187:4671-4682(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K411.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR931997 Genomic DNA. Translation: CAI38093.1.
RefSeqYP_251711.1. NC_007164.1.

3D structure databases

ProteinModelPortalQ4JSW4.
SMRQ4JSW4. Positions 9-243.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING306537.jk1912.

Proteomic databases

PRIDEQ4JSW4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAI38093; CAI38093; jk1912.
GeneID3433787.
KEGGcjk:jk1912.
PATRIC21514796. VBICorJei31838_1940.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0588.
HOGENOMHOG000221682.
KOK01834.
OMASYYLGDQ.
OrthoDBEOG6C8N1H.

Enzyme and pathway databases

BioCycCJEI306537:GJ8V-1965-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 nameGPMA_CORJK
AccessionPrimary (citable) accession number: Q4JSW4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: August 2, 2005
Last modified: February 19, 2014
This is version 55 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