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PHS_DROME
ID   PHS_DROME               Reviewed;         192 AA.
AC   O76454; C6SV03;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Pterin-4-alpha-carbinolamine dehydratase;
DE            Short=PHS;
DE            EC=4.2.1.96;
DE   AltName: Full=4-alpha-hydroxy-tetrahydropterin dehydratase;
DE   AltName: Full=Pterin carbinolamine dehydratase;
DE            Short=PCD;
GN   Name=Pcd; ORFNames=CG1963;
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 CATALYTIC ACTIVITY.
RC   TISSUE=Head;
RX   PubMed=9774744; DOI=10.1016/s0167-4838(98)00203-9;
RA   Seong C., Jeong S., Park D., Yoon J., Oh Y., Yim J., Han K., Baek K.;
RT   "Molecular characterization of the Drosophila melanogaster gene encoding
RT   the pterin 4alpha-carbinolamine dehydratase.";
RL   Biochim. Biophys. Acta 1388:273-278(1998).
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=Head;
RA   Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 37-192.
RC   STRAIN=Berkeley; TISSUE=Larva, and Pupae;
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).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin =
CC         (6R)-L-erythro-6,7-dihydrobiopterin + H2O; Xref=Rhea:RHEA:11920,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15642, ChEBI:CHEBI:43120; EC=4.2.1.96;
CC         Evidence={ECO:0000269|PubMed:9774744};
CC   -!- SIMILARITY: Belongs to the pterin-4-alpha-carbinolamine dehydratase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC25196.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAM50917.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF069297; AAC25196.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AE014297; AAF56923.2; -; Genomic_DNA.
DR   EMBL; BT088995; ACT88136.1; -; mRNA.
DR   EMBL; AY119057; AAM50917.1; ALT_INIT; mRNA.
DR   RefSeq; NP_477360.2; NM_058012.4.
DR   AlphaFoldDB; O76454; -.
DR   SMR; O76454; -.
DR   BioGRID; 68363; 4.
DR   DIP; DIP-22629N; -.
DR   IntAct; O76454; 3.
DR   STRING; 7227.FBpp0084824; -.
DR   PaxDb; O76454; -.
DR   PRIDE; O76454; -.
DR   DNASU; 43499; -.
DR   EnsemblMetazoa; FBtr0085458; FBpp0084824; FBgn0024841.
DR   GeneID; 43499; -.
DR   KEGG; dme:Dmel_CG1963; -.
DR   CTD; 43499; -.
DR   FlyBase; FBgn0024841; Pcd.
DR   VEuPathDB; VectorBase:FBgn0024841; -.
DR   eggNOG; KOG4073; Eukaryota.
DR   GeneTree; ENSGT00390000007221; -.
DR   HOGENOM; CLU_123007_0_0_1; -.
DR   InParanoid; O76454; -.
DR   OMA; IYKQFVL; -.
DR   OrthoDB; 1386644at2759; -.
DR   PhylomeDB; O76454; -.
DR   Reactome; R-DME-8964208; Phenylalanine metabolism.
DR   BioGRID-ORCS; 43499; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 43499; -.
DR   PRO; PR:O76454; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0024841; Expressed in mouthpart and 25 other tissues.
DR   Genevisible; O76454; DM.
DR   GO; GO:0008124; F:4-alpha-hydroxytetrahydrobiopterin dehydratase activity; IBA:GO_Central.
DR   GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.30.1360.20; -; 1.
DR   HAMAP; MF_00434; Pterin_4_alpha; 1.
DR   InterPro; IPR036428; PCD_sf.
DR   InterPro; IPR001533; Pterin_deHydtase.
DR   PANTHER; PTHR12599; PTHR12599; 1.
DR   Pfam; PF01329; Pterin_4a; 1.
DR   SUPFAM; SSF55248; SSF55248; 1.
PE   1: Evidence at protein level;
KW   Lyase; Reference proteome.
FT   CHAIN           1..192
FT                   /note="Pterin-4-alpha-carbinolamine dehydratase"
FT                   /id="PRO_0000063061"
SQ   SEQUENCE   192 AA;  21067 MW;  720FC09124A59281 CRC64;
     MLLTIKCAQN VIKPNCQKVA NLLASSRRAG LFPTTATTAT SRSLSQISVL YSPAAREAAR
     AATGGSANLR RIHNTPTTEA TATAITAKKR KMVVRLNEQE RAEKLQPLLD AGWTLVEGRD
     AIFKQFVLKD FNQAFSFMTG VALLAEKINH HPEWFNCYNK VDVTLSTHDV GGLSSQDIRM
     ATHLETTANL LK
 
 
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