PTPS_PONAB
ID PTPS_PONAB Reviewed; 145 AA.
AC Q5REZ5;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=6-pyruvoyl tetrahydrobiopterin synthase;
DE Short=PTP synthase;
DE Short=PTPS;
DE EC=4.2.3.12;
GN Name=PTS;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the biosynthesis of tetrahydrobiopterin, an
CC essential cofactor of aromatic amino acid hydroxylases. Catalyzes the
CC transformation of 7,8-dihydroneopterin triphosphate into 6-pyruvoyl
CC tetrahydropterin (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7,8-dihydroneopterin 3'-triphosphate = 6-pyruvoyl-5,6,7,8-
CC tetrahydropterin + H(+) + triphosphate; Xref=Rhea:RHEA:22048,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18036, ChEBI:CHEBI:58462,
CC ChEBI:CHEBI:136564; EC=4.2.3.12;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrobiopterin biosynthesis;
CC tetrahydrobiopterin from 7,8-dihydroneopterin triphosphate: step 1/3.
CC -!- SUBUNIT: Homohexamer formed of two homotrimers in a head to head
CC fashion. {ECO:0000250}.
CC -!- PTM: Phosphorylation of Ser-19 is required for maximal enzyme activity.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: The active site is at the interface between 2 subunits.
CC The proton acceptor Cys is on one subunit, and the charge relay system
CC is on the other subunit.
CC -!- SIMILARITY: Belongs to the PTPS family. {ECO:0000305}.
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DR EMBL; CR857367; CAH89662.1; -; mRNA.
DR RefSeq; NP_001124750.1; NM_001131278.1.
DR AlphaFoldDB; Q5REZ5; -.
DR SMR; Q5REZ5; -.
DR STRING; 9601.ENSPPYP00000004445; -.
DR Ensembl; ENSPPYT00000058588; ENSPPYP00000029489; ENSPPYG00000003880.
DR GeneID; 100171600; -.
DR KEGG; pon:100171600; -.
DR CTD; 5805; -.
DR eggNOG; KOG4105; Eukaryota.
DR GeneTree; ENSGT00390000002752; -.
DR InParanoid; Q5REZ5; -.
DR OrthoDB; 1502673at2759; -.
DR UniPathway; UPA00849; UER00819.
DR Proteomes; UP000001595; Chromosome 11.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0003874; F:6-pyruvoyltetrahydropterin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.479.10; -; 1.
DR InterPro; IPR007115; 6-PTP_synth/QueD.
DR InterPro; IPR038418; 6-PTP_synth/QueD_sf.
DR InterPro; IPR022469; PTPS_His_AS.
DR PANTHER; PTHR12589; PTHR12589; 1.
DR Pfam; PF01242; PTPS; 1.
DR PIRSF; PIRSF006113; PTP_synth; 1.
DR TIGRFAMs; TIGR00039; 6PTHBS; 1.
DR PROSITE; PS00988; PTPS_2; 1.
PE 2: Evidence at transcript level;
KW Lyase; Metal-binding; Phosphoprotein; Reference proteome;
KW Tetrahydrobiopterin biosynthesis; Zinc.
FT CHAIN 1..145
FT /note="6-pyruvoyl tetrahydrobiopterin synthase"
FT /id="PRO_0000260520"
FT ACT_SITE 43
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 90
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10124"
FT ACT_SITE 134
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10124"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03393"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R1Z7"
FT MOD_RES 128
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q03393"
SQ SEQUENCE 145 AA; 16315 MW; 3625AF542CFFF2C5 CRC64;
MSTAGGGRRC QAQVSRRISF SASHRLYSKF LSDEENLKLF GKCSNPNGHG HNYKVVVTVH
GEIDPATGMV MNLADLKKYM EEAIMQPLDH KNLDMDVPYF ADVVSTTENV AVYIWDNLQK
VLPVGVLYKV KLYETDNNIV VYKGE
