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0PTPS_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NamePTS
Description6-pyruvoyl tetrahydrobiopterin synthase (ec 4.2.3.12) (ptps) (ptp synthase).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0003874 6-pyruvoyltetrahydropterin synthase activity (TAS)
0006520 amino acid metabolism (TAS)
0007417 central nervous system development (TAS)
0006729 tetrahydrobiopterin biosynthesis (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
The complex organic chemistry involved in the transformation of GTP to tetrahydrobiopterin is catalysed by only three enzymes: GTP cyclohydrolase I.-pyruvoyltetrahydropterin synthase and sepiapterin reductase. Tetrahydrobiopterin is the cofactor for several aromatic amino acid monooxygenases and the nitric oxide synthases. 6-Pyruvoyl tetrahydropterin synthase (PTPS) is a Zn-dependent metalloprotein.ransforms dihydroneopterin triphosphate into 6-pyruvoyltetrahydropterin in the presence of Mg(II) and for which the crystal structure is known.The enzyme is a homohexameric.omposed of a dimer of trimers. A transition metal binding site formed by the three histidine residues 23.8 and 50 is present in each subunit.nd 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 . The function of the bacterial branch of the sequence lineage appears not to have been established.
  IPR007115:6-pyruvoyl tetrahydropterin synthase and hypothetical protein
The complex organic chemistry involved in the transformation of GTP to tetrahydrobiopterin is catalysed by only three enzymes: GTP cyclohydrolase I.-pyruvoyltetrahydropterin synthase and sepiapterin reductase. Tetrahydrobiopterin is the cofactor for several aromatic amino acid monooxygenases and the nitric oxide synthases. 6-Pyruvoyl tetrahydropterin synthase (PTPS) is a Zn-dependent metalloprotein.ransforms dihydroneopterin triphosphate into 6-pyruvoyltetrahydropterin in the presence of Mg(II) and for which the crystal structure is known.The enzyme is a homohexameric.omposed of a dimer of trimers. A transition metal binding site formed by the three histidine residues 23.8 and 50 is present in each subunit.nd 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 . The function of the bacterial branch of the sequence lineage appears not to have been established.
  IPR007116:6-pyruvoyl tetrahydropterin synthase
IPR007115:PTPS 
Evalue:-115.30980682373 
Location:3-145
SequencesProtein: PTPS_HUMAN (145 aa)
mRNA: NM_000317
Local Annotation
Synapse Ontology
Typical ecretory organelles, some 50 nm in diameter, of presynaptic nerve terminals; accumulate high concentrations of nonpeptide neurotransmitters and secrete these into the synaptic cleft by fusion with the 'active zone' of the presynaptic plasma membrane.
sdb:0094 typical synaptic vesicle  (Evidence:keywords)
?
sdb:0328 transmitters release and endocytosis  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 51 residues, 111602308-111602459Exon2: 28 residues, 111604526-111604606Exon3: 9 residues, 111606140-111606163Exon4: 21 residues, 111606558-111606615Exon5: 25 residues, 111609095-111609166Exon6: 181 residues, 111609364-111609903Exon7: 2 residues, -Jump to PTPS_HUMAN  
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Loci Cluster (Details)Loci: 3990 111102849-111142313 ~-39K 7727(PPP2R1B)(-)Loci: 2704 111462831-111471727 ~-9K 7743(SDHD)(+)Loci: 2705 111602308-111609903 ~-8K 7753(PTS)(+)Loci: 2703 110978379-111102840 ~-124K 7726(SNF1LK2)(+)Link out to UCSC