ID   PTPS_POERE              Reviewed;         147 AA.
AC   Q90W95; Q90W94;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=6-pyruvoyl tetrahydrobiopterin synthase;
DE            Short=PTP synthase;
DE            Short=PTPS;
DE            EC=4.2.3.12;
GN   Name=pts;
OS   Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=8081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Caudal fin;
RA   Ben J., Lim T.-M., Chan W.-K., Phang V.P.E.;
RT   "Molecular cloning of 6-pyruvoyl tetrahydropterin synthase genes from
RT   guppies.";
RL   Submitted (MAY-2001) 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.
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q90W95-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q90W95-2; Sequence=VSP_005511;
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; AY034101; AAK59697.1; -; mRNA.
DR   EMBL; AY034102; AAK59698.1; -; mRNA.
DR   RefSeq; NP_001284375.1; NM_001297446.1. [Q90W95-2]
DR   AlphaFoldDB; Q90W95; -.
DR   SMR; Q90W95; -.
DR   STRING; 8081.XP_008435972.1; -.
DR   GeneID; 103481923; -.
DR   KEGG; pret:103481923; -.
DR   CTD; 5805; -.
DR   UniPathway; UPA00849; UER00819.
DR   Proteomes; UP000242638; Unassembled WGS sequence.
DR   GO; GO:0003874; F:6-pyruvoyltetrahydropterin synthase activity; IEA:UniProtKB-EC.
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; IPR022470; PTPS_Cys_AS.
DR   InterPro; IPR022469; PTPS_His_AS.
DR   PANTHER; PTHR12589; PTHR12589; 1.
DR   Pfam; PF01242; PTPS; 1.
DR   TIGRFAMs; TIGR00039; 6PTHBS; 1.
DR   PROSITE; PS00987; PTPS_1; 1.
DR   PROSITE; PS00988; PTPS_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Lyase; Metal-binding; Reference proteome;
KW   Tetrahydrobiopterin biosynthesis; Zinc.
FT   CHAIN           1..147
FT                   /note="6-pyruvoyl tetrahydrobiopterin synthase"
FT                   /id="PRO_0000057916"
FT   ACT_SITE        45
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10123"
FT   ACT_SITE        92
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10124"
FT   ACT_SITE        136
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10124"
FT   BINDING         26
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10123"
FT   BINDING         51
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10123"
FT   BINDING         53
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10123"
FT   VAR_SEQ         84..106
FT                   /note="EVIMIPLDHKNLDKDVPYFADVV -> IRTFHQTFLLSLT (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_005511"
SQ   SEQUENCE   147 AA;  16679 MW;  D26FA34DD907B2A2 CRC64;
     MAESSGNPPA ERIGYITRVQ SFSACHRLHS LRLSDEENKE VYGKCNNPYG HGHNYKVEVT
     VRGKIDPVTG MVMNLTDLKK CIEEVIMIPL DHKNLDKDVP YFADVVSTTE NLAVYIWDNM
     AKALPASLPY EIRIHETDKN IVVYRGE