SMART: Pfam domain PTPS

The domain within your query sequence starts at position 12 and ends at position 144; the E-value for the PTPS domain shown below is 2.5e-38.

RLSRLVSFSASHRLHSPSLSDEENLRVFGKCNNPNGHGHNYKVVVTVHGEIDPVTGMVMN
LTDLKEYMEEAIMKPLDHKNLDLDVPYFADAVSTTENVAVYIWESLQKLLPVGALYKVKV
FETDNNIVVYKGE

PTPS

PFAM accession number:	PF01242
Interpro abstract (IPR007115):	6-Pyruvoyl tetrahydrobiopterin synthase (PTPS) catalyses the conversion of dihydroneopterin triphosphate to 6-pyruvoyl tetrahydropterin, the second of three enzymatic steps in the synthesis of tetrahydrobiopterin from GTP [ (PUBMED:8137809) ]. The functional enzyme is a hexamer of identical subunits. A transition metal binding site formed by the three histidine residues 23, 48 and 50 is present in each subunit, and bound Zn(II) is responsible for the enzymatic activity. Site-directed mutagenesis of each of these three histidine residues results in a complete loss of metal binding and enzymatic activity [ (PUBMED:7563095) (PUBMED:9165069) ]. The function of the bacterial branch of the family had been thought to be the same, but many are now taken to be QueD, and enzyme of queuosine biosynthesis. Queuosine is a hypermodified base in the wobble position of some tRNAs in most species [ (PUBMED:14660578) ].

PFAM accession number:

PF01242

Interpro abstract (IPR007115):

6-Pyruvoyl tetrahydrobiopterin synthase (PTPS) catalyses the conversion of dihydroneopterin triphosphate to 6-pyruvoyl tetrahydropterin, the second of three enzymatic steps in the synthesis of tetrahydrobiopterin from GTP [ (PUBMED:8137809) ]. The functional enzyme is a hexamer of identical subunits. A transition metal binding site formed by the three histidine residues 23, 48 and 50 is present in each subunit, and bound Zn(II) is responsible for the enzymatic activity. Site-directed mutagenesis of each of these three histidine residues results in a complete loss of metal binding and enzymatic activity [ (PUBMED:7563095) (PUBMED:9165069) ].

The function of the bacterial branch of the family had been thought to be the same, but many are now taken to be QueD, and enzyme of queuosine biosynthesis. Queuosine is a hypermodified base in the wobble position of some tRNAs in most species [ (PUBMED:14660578) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry PTPS