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Database: UniProt
Entry: G3P7E1_GASAC
LinkDB: G3P7E1_GASAC
Original site: G3P7E1_GASAC 
ID   G3P7E1_GASAC            Unreviewed;       144 AA.
AC   G3P7E1;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=6-pyruvoyl tetrahydrobiopterin synthase {ECO:0000256|ARBA:ARBA00015587, ECO:0000256|PIRNR:PIRNR006113};
DE            Short=PTP synthase {ECO:0000256|PIRNR:PIRNR006113};
DE            Short=PTPS {ECO:0000256|PIRNR:PIRNR006113};
DE            EC=4.2.3.12 {ECO:0000256|ARBA:ARBA00013100, ECO:0000256|PIRNR:PIRNR006113};
GN   Name=PTS {ECO:0000313|Ensembl:ENSGACP00000013515.1};
OS   Gasterosteus aculeatus (Three-spined stickleback).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC   Gasterosteus.
OX   NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000013515.1, ECO:0000313|Proteomes:UP000007635};
RN   [1] {ECO:0000313|Ensembl:ENSGACP00000013515.1, ECO:0000313|Proteomes:UP000007635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGACP00000013515.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00025266}.
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         Evidence={ECO:0000256|PIRNR:PIRNR006113};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRNR:PIRNR006113,
CC         ECO:0000256|PIRSR:PIRSR006113-2};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR006113,
CC       ECO:0000256|PIRSR:PIRSR006113-2};
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrobiopterin biosynthesis;
CC       tetrahydrobiopterin from 7,8-dihydroneopterin triphosphate: step 1/3.
CC       {ECO:0000256|ARBA:ARBA00005126, ECO:0000256|PIRNR:PIRNR006113}.
CC   -!- SIMILARITY: Belongs to the PTPS family. {ECO:0000256|ARBA:ARBA00009164,
CC       ECO:0000256|PIRNR:PIRNR006113}.
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DR   AlphaFoldDB; G3P7E1; -.
DR   STRING; 69293.ENSGACP00000013515; -.
DR   Ensembl; ENSGACT00000013540.1; ENSGACP00000013515.1; ENSGACG00000010227.1.
DR   eggNOG; KOG4105; Eukaryota.
DR   GeneTree; ENSGT00390000002752; -.
DR   InParanoid; G3P7E1; -.
DR   OMA; HFNAAHK; -.
DR   TreeFam; TF105796; -.
DR   UniPathway; UPA00849; UER00819.
DR   Proteomes; UP000007635; Unassembled WGS sequence.
DR   Bgee; ENSGACG00000010227; Expressed in embryo and 13 other cell types or tissues.
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   CDD; cd00470; PTPS; 1.
DR   Gene3D; 3.30.479.10; 6-pyruvoyl tetrahydropterin synthase/QueD; 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   NCBIfam; TIGR00039; 6PTHBS; 1.
DR   PANTHER; PTHR12589:SF7; 6-PYRUVOYL TETRAHYDROBIOPTERIN SYNTHASE; 1.
DR   PANTHER; PTHR12589; PYRUVOYL TETRAHYDROBIOPTERIN SYNTHASE; 1.
DR   Pfam; PF01242; PTPS; 1.
DR   PIRSF; PIRSF006113; PTP_synth; 1.
DR   SUPFAM; SSF55620; Tetrahydrobiopterin biosynthesis enzymes-like; 1.
DR   PROSITE; PS00987; PTPS_1; 1.
DR   PROSITE; PS00988; PTPS_2; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR006113};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR006113};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW   Tetrahydrobiopterin biosynthesis {ECO:0000256|ARBA:ARBA00023007,
KW   ECO:0000256|PIRNR:PIRNR006113};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR006113}.
FT   ACT_SITE        42
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006113-1"
FT   ACT_SITE        89
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006113-1"
FT   ACT_SITE        133
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006113-1"
FT   BINDING         23
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006113-2"
FT   BINDING         48
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006113-2"
FT   BINDING         50
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006113-2"
SQ   SEQUENCE   144 AA;  16190 MW;  E1307B024C9E997A CRC64;
     SSGSGAAEPV GYITRVQSFS ACHRLHSVHL SEDDNKAVYG KCNNPNGHGH NYKVEVTVRG
     KIDRVTGMVM NLTDLKKCIE DVIMTPLDHK NLDQDVPYFR SVVSTTENVA VHIWNEMIKV
     LPPNLLHEIK IHETDKNIVI YRGE
//
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