1rtz A: PDB entry domain

SCOP classification

• Root: SCOP hierarchy in SUPERFAMILY [ 0] (11)
• Class: Alpha and beta proteins (a+b) [ 53931] (376)
• Fold: Ferredoxin-like [ 54861] (59)
• Superfamily: 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, HPPK [ 55083]
• Family: 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, HPPK [ 55084]
• Protein:
  • 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, HPPK [55085]
• PDB Entry Domain:
  • 1rtz A: [ 97831]
  • SUPERFAMILY domain annotation for 1rtza
  • PDB structure summary for 1rtz

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InterPro annotation

• Cross references: IPR000550 SSF55083 Protein matches
• Abstract: All organisms require reduced folate cofactors for the synthesis of a variety of metabolites. Most microorganisms must synthesise folate de novo because they lack the active transport system of higher vertebrate cells which allows these organisms to use dietary folates. Enzymes involved in folate biosynthesis are therefore targets for a variety of antimicrobial agents such as trimethoprim or sulphonamides. 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase (HPPK) catalyzes the attachment of pyrophosphate to 6-hydroxymethyl-7,8-dihydropterin to form 6-hydroxymethyl-7,8-dihydropteridine pyrophosphate. This is the first step in a three-step pathway leading to 7,8 dihydrofolate. Bacterial HPPK (gene folK or sulD) [1325970] is a protein of 160 to 270 amino acids. In the lower eukaryote Pneumocystis carinii, HPPK is the central domain of a multifunctional folate synthesis enzyme (gene fas) [1313386].

InterPro database

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