ID A0A1X7U3C7_AMPQE Unreviewed; 147 AA.
AC A0A1X7U3C7;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=6-pyruvoyl tetrahydrobiopterin synthase {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|PIRNR:PIRNR006113};
GN Name=100633397 {ECO:0000313|EnsemblMetazoa:Aqu2.1.22044_001};
OS Amphimedon queenslandica (Sponge).
OC Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha;
OC Haplosclerida; Niphatidae; Amphimedon.
OX NCBI_TaxID=400682 {ECO:0000313|EnsemblMetazoa:Aqu2.1.22044_001, ECO:0000313|Proteomes:UP000007879};
RN [1] {ECO:0000313|Proteomes:UP000007879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20686567; DOI=10.1038/nature09201;
RA Srivastava M., Simakov O., Chapman J., Fahey B., Gauthier M.E., Mitros T.,
RA Richards G.S., Conaco C., Dacre M., Hellsten U., Larroux C., Putnam N.H.,
RA Stanke M., Adamska M., Darling A., Degnan S.M., Oakley T.H.,
RA Plachetzki D.C., Zhai Y., Adamski M., Calcino A., Cummins S.F.,
RA Goodstein D.M., Harris C., Jackson D.J., Leys S.P., Shu S., Woodcroft B.J.,
RA Vervoort M., Kosik K.S., Manning G., Degnan B.M., Rokhsar D.S.;
RT "The Amphimedon queenslandica genome and the evolution of animal
RT complexity.";
RL Nature 466:720-726(2010).
RN [2] {ECO:0000313|Proteomes:UP000007879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lucas S., Shapiro H., Lindquist E., Tice H., Dalin E., Glavina del Rio T.,
RA Bruce D., Barry K., Pitluck S., Srivastava M., Simakov O., Chapman J.,
RA Mitros T., Hellsten U., Putnam N.H., Fahey B., Gauthier M., Larroux C.,
RA Richards G.S., Stanke M., Adamska M., Darling A., Dacre M., Degnan S.M.,
RA Zhai Y., Adamski M., Calcino A., Cummins S.F., Goodstein D.M., Harris C.,
RA Shu S., Woodcroft B., Leys S.P., Manning G., Degnan B.M., Rokhsar D.S.;
RT "The genome of the haplosclerid demosponge Amphimedon queenslandica and the
RT evolution of animal complexity.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:Aqu2.1.22044_001}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (MAY-2017) to UniProtKB.
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 RefSeq; XP_011406178.1; XM_011407876.2.
DR AlphaFoldDB; A0A1X7U3C7; -.
DR STRING; 400682.A0A1X7U3C7; -.
DR EnsemblMetazoa; Aqu2.1.22044_001; Aqu2.1.22044_001; Aqu2.1.22044.
DR GeneID; 100633397; -.
DR KEGG; aqu:100633397; -.
DR eggNOG; KOG4105; Eukaryota.
DR InParanoid; A0A1X7U3C7; -.
DR OMA; YETERNF; -.
DR OrthoDB; 5539at2759; -.
DR UniPathway; UPA00849; UER00819.
DR Proteomes; UP000007879; 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; 6-pyruvoyl tetrahydropterin synthase/QueD; 1.
DR InterPro; IPR007115; 6-PTP_synth/QueD.
DR InterPro; IPR038418; 6-PTP_synth/QueD_sf.
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.
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:UP000007879};
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 38
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006113-1"
FT ACT_SITE 85
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 19
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR006113-2"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR006113-2"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR006113-2"
SQ SEQUENCE 147 AA; 16755 MW; 38F1ED13C8E64817 CRC64;
MIRCPVAYLS RSLSVSAAHR LCSSHLTEEE NISLYGKCYN PNGHGHNYTV EVTVKGKVDP
STGMVMDLQE LKKAMDVAVT AQLDHKNIDL DVPYFRDQRI VSTTENVTVF IWKEMTKSLG
SNKHLLYKVV VWETDKNKFT YKGEEEI
//
