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Database: UniProt
Entry: D0MVR8_PHYIT
LinkDB: D0MVR8_PHYIT
Original site: D0MVR8_PHYIT 
ID   D0MVR8_PHYIT            Unreviewed;       374 AA.
AC   D0MVR8;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=phenylalanine 4-monooxygenase {ECO:0000256|ARBA:ARBA00011995};
DE            EC=1.14.16.1 {ECO:0000256|ARBA:ARBA00011995};
GN   ORFNames=PITG_02210 {ECO:0000313|EMBL:EEY63731.1};
OS   Phytophthora infestans (strain T30-4) (Potato late blight agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=403677 {ECO:0000313|EMBL:EEY63731.1, ECO:0000313|Proteomes:UP000006643};
RN   [1] {ECO:0000313|Proteomes:UP000006643}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T30-4 {ECO:0000313|Proteomes:UP000006643};
RX   PubMed=19741609; DOI=10.1038/nature08358;
RG   The Broad Institute Genome Sequencing Platform;
RA   Haas B.J., Kamoun S., Zody M.C., Jiang R.H., Handsaker R.E., Cano L.M.,
RA   Grabherr M., Kodira C.D., Raffaele S., Torto-Alalibo T., Bozkurt T.O.,
RA   Ah-Fong A.M., Alvarado L., Anderson V.L., Armstrong M.R., Avrova A.,
RA   Baxter L., Beynon J., Boevink P.C., Bollmann S.R., Bos J.I., Bulone V.,
RA   Cai G., Cakir C., Carrington J.C., Chawner M., Conti L., Costanzo S.,
RA   Ewan R., Fahlgren N., Fischbach M.A., Fugelstad J., Gilroy E.M., Gnerre S.,
RA   Green P.J., Grenville-Briggs L.J., Griffith J., Grunwald N.J., Horn K.,
RA   Horner N.R., Hu C.H., Huitema E., Jeong D.H., Jones A.M., Jones J.D.,
RA   Jones R.W., Karlsson E.K., Kunjeti S.G., Lamour K., Liu Z., Ma L.,
RA   Maclean D., Chibucos M.C., McDonald H., McWalters J., Meijer H.J.,
RA   Morgan W., Morris P.F., Munro C.A., O'Neill K., Ospina-Giraldo M.,
RA   Pinzon A., Pritchard L., Ramsahoye B., Ren Q., Restrepo S., Roy S.,
RA   Sadanandom A., Savidor A., Schornack S., Schwartz D.C., Schumann U.D.,
RA   Schwessinger B., Seyer L., Sharpe T., Silvar C., Song J., Studholme D.J.,
RA   Sykes S., Thines M., van de Vondervoort P.J., Phuntumart V., Wawra S.,
RA   Weide R., Win J., Young C., Zhou S., Fry W., Meyers B.C., van West P.,
RA   Ristaino J., Govers F., Birch P.R., Whisson S.C., Judelson H.S.,
RA   Nusbaum C.;
RT   "Genome sequence and analysis of the Irish potato famine pathogen
RT   Phytophthora infestans.";
RL   Nature 461:393-398(2009).
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|ARBA:ARBA00001954,
CC         ECO:0000256|PIRSR:PIRSR601273-2};
CC   -!- SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid
CC       hydroxylase family. {ECO:0000256|ARBA:ARBA00009712}.
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DR   EMBL; DS028120; EEY63731.1; -; Genomic_DNA.
DR   RefSeq; XP_002907167.1; XM_002907121.1.
DR   AlphaFoldDB; D0MVR8; -.
DR   STRING; 403677.D0MVR8; -.
DR   EnsemblProtists; PITG_02210T0; PITG_02210T0; PITG_02210.
DR   GeneID; 9469603; -.
DR   KEGG; pif:PITG_02210; -.
DR   VEuPathDB; FungiDB:PITG_02210; -.
DR   eggNOG; KOG3820; Eukaryota.
DR   HOGENOM; CLU_023198_0_1_1; -.
DR   InParanoid; D0MVR8; -.
DR   OMA; FHDEVYR; -.
DR   OrthoDB; 275463at2759; -.
DR   Proteomes; UP000006643; Partially assembled WGS sequence.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016714; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygen; IEA:InterPro.
DR   GO; GO:0004664; F:prephenate dehydratase activity; IEA:InterPro.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:InterPro.
DR   Gene3D; 1.10.800.10; Aromatic amino acid hydroxylase; 1.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR001273; ArAA_hydroxylase.
DR   InterPro; IPR036951; ArAA_hydroxylase_sf.
DR   InterPro; IPR036329; Aro-AA_hydroxylase_C_sf.
DR   InterPro; IPR019774; Aromatic-AA_hydroxylase_C.
DR   InterPro; IPR018528; Preph_deHydtase_CS.
DR   InterPro; IPR019773; Tyrosine_3-monooxygenase-like.
DR   PANTHER; PTHR11473; AROMATIC AMINO ACID HYDROXYLASE; 1.
DR   PANTHER; PTHR11473:SF24; PHENYLALANINE-4-HYDROXYLASE; 1.
DR   Pfam; PF00351; Biopterin_H; 1.
DR   PIRSF; PIRSF000336; TH; 1.
DR   PRINTS; PR00372; FYWHYDRXLASE.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF56534; Aromatic aminoacid monoxygenases, catalytic and oligomerization domains; 1.
DR   PROSITE; PS51410; BH4_AAA_HYDROXYL_2; 1.
DR   PROSITE; PS00858; PREPHENATE_DEHYDR_2; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000336-1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000336-1};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006643}.
FT   DOMAIN          41..374
FT                   /note="Biopterin-dependent aromatic amino acid hydroxylase
FT                   family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51410"
FT   BINDING         220
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000336-1"
FT   BINDING         225
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000336-1"
FT   BINDING         265
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000336-1"
SQ   SEQUENCE   374 AA;  43269 MW;  B151016E28989827 CRC64;
     MTRIESRPAK GHNMNYSFFI DFEGKSGQNK VDDLMTDLEK NCLDVMVLND KKVPWFPRKI
     NELDRSVANI LDAGTDLESD HPGFSDQEYR RRRNMFAEIA QNYRQGDPIP RLDYTQDEIN
     TWGVIYKRMK EMWKQHACDE FNYIIPLLES NCGYAEDNIP QQEDISNFLK ECTGFTLRPV
     GGLLSSRDFL NGLAFRVFFS TQYIRHHSMP LYTPEPDICH ELMGHAPMFA DPDFADFSHE
     VGLASLGASD EEIERLATCY WFSVEFGITK QRGEYKAYGA GLLSSFGEME YACAADRPAG
     SDMPEYRPWD PFSACKQKYP ITTYQPVYYV ADSLFDAKEK MRGFCEDLKK PFQARYDPYS
     QTISIDRAVQ RQEL
//
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