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InterPro: IPR000550 7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase, HPPK

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1785 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Architectures
Accession List
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Accession

IPR000550 Hppk

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:3.30.70.560	Hppk	1728
Pfam	PF01288	HPPK	1731
PROSITE pattern	PS00794	HPPK	1245
SuperFamily	SSF55083	Hppk	1774
TIGRFAMs	TIGR01498	folK	1707
Signatures in BioMart

InterPro Relationships Help

Found in

IPR016261 Folic acid synthesis protein

GO Term annotation Help

Process

GO:0009396 folic acid and derivative biosynthetic process

Function

GO:0003848 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity

InterPro annotation

Entry Details in BioMart

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 (EC:2.7.6.3) (HPPK) catalyses 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) [1] 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) [2].

Structural links Help

PDB - click here

SCOP: d.58.30.1

CATH: 3.30.70.560

Database links Help

PDBe-motif: PS00794

Enzyme: EC:2.7.6.3

PROSITE doc: PDOC00631

PANDIT: PF01288

Blocks: IPB000550

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR000550

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P26281 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase

P29251 Folic acid synthesis protein fol1

P53848 Folic acid synthesis protein FOL1

P72736 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase

Q54YD9 Folic acid synthesis protein FOL1

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR006390	Dihydropteroate synthase
IPR011005	Dihydropteroate synthase-like
IPR000489	Dihydropteroate synthase, DHPS
IPR016261	Folic acid synthesis protein
IPR000550	7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase, HPPK
IPR006157	Dihydroneopterin aldolase
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Talarico TL, Ray PH, Dev IK, Merrill BM, Dallas WS. Cloning, sequence analysis, and overexpression of Escherichia coli folK, the gene coding for 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase. J. Bacteriol. 174 5971-7 1992 [PubMed: 1325970] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=1325970
2.	Volpe F, Dyer M, Scaife JG, Darby G, Stammers DK, Delves CJ. The multifunctional folic acid synthesis fas gene of Pneumocystis carinii appears to encode dihydropteroate synthase and hydroxymethyldihydropterin pyrophosphokinase. Gene 112 213-8 1992 [PubMed: 1313386] http://dx.doi.org/10.1016/0378-1119(92)90378-3

Additional Reading Open in usermanual
	Blaszczyk J, Li Y, Wu Y, Shi G, Ji X, Yan H. Essential roles of a dynamic loop in the catalysis of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase. Biochemistry 43 2004 1469-77 [PubMed: 14769023] http://dx.doi.org/10.1021/bi036053l
	Blaszczyk J, Li Y, Cherry S, Alexandratos J, Wu Y, Shaw G, Tropea JE, Waugh DS, Yan H, Ji X. Structure and activity of Yersinia pestis 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase as a novel target for the development of antiplague therapeutics. Acta Crystallogr. D Biol. Crystallogr. 63 2007 1169-77 [PubMed: 18007032] http://dx.doi.org/10.1107/S0907444907047452
	Li Y, Blaszczyk J, Wu Y, Shi G, Ji X, Yan H. Is the critical role of loop 3 of Escherichia coli 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase in catalysis due to loop-3 residues arginine-84 and tryptophan-89? Site-directed mutagenesis, biochemical, and crystallographic studies. Biochemistry 44 2005 8590-9 [PubMed: 15952765] http://dx.doi.org/10.1021/bi0503495
	Blaszczyk J, Shi G, Li Y, Yan H, Ji X. Reaction trajectory of pyrophosphoryl transfer catalyzed by 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase. Structure 12 2004 467-75 [PubMed: 15016362] http://dx.doi.org/10.1016/j.str.2004.02.003
	Blaszczyk J, Li Y, Shi G, Yan H, Ji X. Dynamic roles of arginine residues 82 and 92 of Escherichia coli 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase: crystallographic studies. Biochemistry 42 2003 1573-80 [PubMed: 12578370] http://dx.doi.org/10.1021/bi0267994

InterPro 23.1