CATH Classification
Level | CATH Code | Description |
---|---|---|
3 | Alpha Beta | |
3.20 | Alpha-Beta Barrel | |
3.20.20 | TIM Barrel | |
3.20.20.390 | FMN-linked oxidoreductases |
Domain Context
CATH Clusters
Superfamily | FMN-linked oxidoreductases |
Functional Family |
Enzyme Information
2.5.1.41 |
Phosphoglycerol geranylgeranyltransferase.
based on mapping to UniProt A5FJK8
Geranylgeranyl diphosphate + sn-glycerol 1-phosphate = diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate.
-!- Catalyzes the first pathway-specific step in the biosynthesis of the core membrane diether lipids in archaebacteria. -!- It catalyzes the alkylation of the primary hydroxy group in sn-glycerol 1-phosphate by geranylgeranyl diphosphate (GGPP) in a prenyltransfer reaction where a hydroxy group is the nucleophile in the acceptor substrate. -!- The other enzymes involved in the biosynthesis of polar lipids in archaea are EC 1.1.1.261, EC 2.5.1.42 and EC 2.7.7.67, which lead to the formation of CDP-unsaturated archaeol. -!- The final step in the pathway involves the addition of L-serine, with concomitant removal of CMP, leading to the production of unsaturated archaetidylserine.
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UniProtKB Entries (1)
A5FJK8 |
GGGPS_FLAJ1
Flavobacterium johnsoniae UW101
Geranylgeranylglyceryl phosphate synthase
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PDB Structure
PDB | 4JEJ |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
A comprehensive analysis of the geranylgeranylglyceryl phosphate synthase enzyme family identifies novel members and reveals mechanisms of substrate specificity and quaternary structure organization.
Mol.Microbiol.
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