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Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in Catalysis by Triosephosphate Isomerase

Source organism: Trypanosoma brucei brucei
Biochemical function: isomerase activity
Biological process: glyceraldehyde-3-phosphate biosynthetic process
Cellular component: glycosome

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EC 5.3.1.1: Triose-phosphate isomerase

Reaction catalysed:
D-glyceraldehyde 3-phosphate = glycerone phosphate
Systematic name:
D-glyceraldehyde-3-phosphate aldose-ketose-isomerase
Alternative Name(s):
  • D-glyceraldehyde-3-phosphate ketol-isomerase
  • Phosphotriose isomerase
  • Triose phosphate mutase
  • Triose phosphoisomerase
  • Triosephosphate isomerase
  • Triosephosphate mutase

GO terms

Sequence family

Pfam Protein family (Pfam)
PF00121
Domain description: Triosephosphate isomerase
Occurring in:
  1. Triosephosphate isomerase, glycosomal
The deposited structure of PDB entry 5i3j contains 2 copies of Pfam domain PF00121 (Triosephosphate isomerase) in Triosephosphate isomerase, glycosomal. Showing 1 copy in chain A.

InterPro InterPro annotations
IPR000652
Domain description: Triosephosphate isomerase
Occurring in:
  1. Triosephosphate isomerase, glycosomal
IPR020861
Domain description: Triosephosphate isomerase, active site
Occurring in:
  1. Triosephosphate isomerase, glycosomal
IPR035990
Domain description: Triosephosphate isomerase superfamily
Occurring in:
  1. Triosephosphate isomerase, glycosomal
IPR022896
Domain description: Triosephosphate isomerase, bacterial/eukaryotic
Occurring in:
  1. Triosephosphate isomerase, glycosomal
IPR013785
Domain description: Aldolase-type TIM barrel
Occurring in:
  1. Triosephosphate isomerase, glycosomal

Structure domain

CATH CATH domain
3.20.20.70
Class: Alpha Beta
Architecture: Alpha-Beta Barrel
Topology: TIM Barrel
Homology: Aldolase class I
Occurring in:
  1. Triosephosphate isomerase, glycosomal
The deposited structure of PDB entry 5i3j contains 2 copies of CATH domain 3.20.20.70 (TIM Barrel) in Triosephosphate isomerase, glycosomal. Showing 1 copy in chain A.

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