PTPS_DROME
ID PTPS_DROME Reviewed; 168 AA.
AC P48611; A4V0X1; Q9VIP5;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=6-pyruvoyl tetrahydrobiopterin synthase;
DE Short=PTP synthase;
DE Short=PTPS;
DE EC=4.2.3.12;
DE AltName: Full=Protein purple;
DE AltName: Full=Sepiapterin synthase A;
GN Name=pr; ORFNames=CG16784;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=8846895; DOI=10.1093/genetics/142.4.1157;
RA Kim N., Kim J., Park D., Rosen C., Dorsett D., Yim J.;
RT "Structure and expression of wild-type and suppressible alleles of the
RT Drosophila purple gene.";
RL Genetics 142:1157-1168(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159; THR-161; SER-164;
RP SER-165 AND SER-167, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Required for pigment and biopterin synthesis.
CC {ECO:0000269|PubMed:8846895}.
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 -!- INTERACTION:
CC P48611; P48611: pr; NbExp=3; IntAct=EBI-128080, EBI-128080;
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; U36232; AAC47269.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN11065.1; -; Genomic_DNA.
DR EMBL; AY061078; AAL28626.1; -; mRNA.
DR PIR; S68127; S68127.
DR RefSeq; NP_724244.1; NM_165319.3.
DR AlphaFoldDB; P48611; -.
DR SMR; P48611; -.
DR BioGRID; 61262; 15.
DR DIP; DIP-22470N; -.
DR IntAct; P48611; 1.
DR STRING; 7227.FBpp0088417; -.
DR iPTMnet; P48611; -.
DR PaxDb; P48611; -.
DR PRIDE; P48611; -.
DR DNASU; 35292; -.
DR EnsemblMetazoa; FBtr0089395; FBpp0088417; FBgn0003141.
DR GeneID; 35292; -.
DR KEGG; dme:Dmel_CG16784; -.
DR UCSC; CG16784-RB; d. melanogaster.
DR CTD; 19066; -.
DR FlyBase; FBgn0003141; pr.
DR VEuPathDB; VectorBase:FBgn0003141; -.
DR eggNOG; KOG4105; Eukaryota.
DR GeneTree; ENSGT00390000002752; -.
DR HOGENOM; CLU_111016_2_0_1; -.
DR InParanoid; P48611; -.
DR OMA; NVAIFIW; -.
DR OrthoDB; 1502673at2759; -.
DR PhylomeDB; P48611; -.
DR BioCyc; MetaCyc:MON-18456; -.
DR Reactome; R-DME-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
DR SignaLink; P48611; -.
DR UniPathway; UPA00849; UER00819.
DR BioGRID-ORCS; 35292; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 35292; -.
DR PRO; PR:P48611; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0003141; Expressed in capitellum (Drosophila) and 28 other tissues.
DR Genevisible; P48611; DM.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0003874; F:6-pyruvoyltetrahydropterin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006728; P:pteridine biosynthetic process; IDA:FlyBase.
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 1: Evidence at protein level;
KW Lyase; Metal-binding; Phosphoprotein; Reference proteome;
KW Tetrahydrobiopterin biosynthesis; Zinc.
FT CHAIN 1..168
FT /note="6-pyruvoyl tetrahydrobiopterin synthase"
FT /id="PRO_0000057918"
FT ACT_SITE 38
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10123"
FT ACT_SITE 85
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10124"
FT ACT_SITE 130
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10124"
FT BINDING 19
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10123"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10123"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10123"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 161
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 168 AA; 19337 MW; BEBB45B046421B84 CRC64;
MSQQPVAFLT RRETFSACHR LHSPQLSDAE NLEVFGKCNN FHGHGHNYTV EITVRGPIDR
RTGMVLNITE LKEAIETVIM KRLDHKNLDK DVEYFANTPS TTENLAVYIW DNIRLQLKKP
ELLYEVKIHE TPKNIISYRG PYPLNGIYNP INKRIAHDSC TNISSDSD
