Glucose-6-phosphate isomerase structure
P06744
G6PI_HUMAN
GPI

Glucose-6-phosphate isomerase

Homo sapiensTaxon: 9606

3D-structureAcetylationAlternative splicingCytokineCytoplasmDirect protein sequencingDisease variantGluconeogenesisGlycolysisGrowth factorHereditary hemolytic anemiaHydroxylation+6
Sequence Length

558

amino acids

Molecular Weight

63.1 kDa

theoretical

Experimental Structures

13

PDB entries

Related Diseases

1

recorded

Function

Isomerase that catalyzes the conversion of alpha-D-glucose-6-phosphate to beta-D-fructose-6-phosphate, the second step in glycolysis, and the reverse reaction in gluconeogenesis, within the cytoplasm (PubMed:28803808). Also shows C2-epimerase activity, interconverting D-glucose-6-phosphate (G6P) and D-mannose-6-phosphate (M6P) (By similarity). Also displays anomerase activity, interconverting alpha and beta-anomeric forms of G6P, D-fructose-6-phosphate and M6P (By similarity). In addition to its metabolic role, this enzyme functions extracellularly as a cytokine: acts as autocrine motility factor (AMF), a secreted angiogenic factor that enhances endothelial cell motility (PubMed:11437381). Functions as neuroleukin, a neurotrophic factor supporting the survival of spinal and sensory neurons (PubMed:11004567, PubMed:3352745). Released by lectin-stimulated T-cells to induce immunoglobulin secretion (PubMed:11004567, PubMed:3352745)

Related Diseases

Anemia, congenital, non-spherocytic hemolytic, 4

An autosomal recessive form of anemia in which there is no abnormal hemoglobin or spherocytosis. It is caused by glucose phosphate isomerase deficiency.

Amino Acid Sequence

MAALTRDPQFQKLQQWYREHRSELNLRRLFDANKDRFNHFSLTLNTNHGHILVDYSKNLV
TEDVMRMLVDLAKSRGVEAARERMFNGEKINYTEGRAVLHVALRNRSNTPILVDGKDVMP
EVNKVLDKMKSFCQRVRSGDWKGYTGKTITDVINIGIGGSDLGPLMVTEALKPYSSGGPR
VWYVSNIDGTHIAKTLAQLNPESSLFIIASKTFTTQETITNAETAKEWFLQAAKDPSAVA

FASTA format · 558 amino acids · mass 63.1 kDa

Experimental Structures

13 PDB entries
1IAT1IRI1JIQ1JLH1NUH6XUH6XUI8BBH8P2K9FCW9FHF9FKC9FKF

Post-Translational Modifications

  • Phosphorylation at Ser-185 by CK2 has been shown to decrease enzymatic activity and may contribute to secretion by a non-classical secretory pathway
  • ISGylated