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Database: UniProt
Entry: A0A1S8VPG6_9FUNG
LinkDB: A0A1S8VPG6_9FUNG
Original site: A0A1S8VPG6_9FUNG 
ID   A0A1S8VPG6_9FUNG        Unreviewed;       546 AA.
AC   A0A1S8VPG6;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=phenylalanine 4-monooxygenase {ECO:0000256|ARBA:ARBA00011995};
DE            EC=1.14.16.1 {ECO:0000256|ARBA:ARBA00011995};
GN   ORFNames=BSLG_05587 {ECO:0000313|EMBL:OON04288.1};
OS   Batrachochytrium salamandrivorans.
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC   Rhizophydiales incertae sedis; Batrachochytrium.
OX   NCBI_TaxID=1357716 {ECO:0000313|EMBL:OON04288.1, ECO:0000313|Proteomes:UP000189906};
RN   [1] {ECO:0000313|EMBL:OON04288.1, ECO:0000313|Proteomes:UP000189906}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BS {ECO:0000313|EMBL:OON04288.1,
RC   ECO:0000313|Proteomes:UP000189906};
RA   Lavstsen T., Jespersen J.S.;
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OON04288.1}.
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DR   EMBL; LYON01001091; OON04288.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S8VPG6; -.
DR   STRING; 1357716.A0A1S8VPG6; -.
DR   VEuPathDB; FungiDB:BSLG_05587; -.
DR   OrthoDB; 275463at2759; -.
DR   Proteomes; UP000189906; Unassembled WGS sequence.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004505; F:phenylalanine 4-monooxygenase activity; IEA:UniProt.
DR   GO; GO:0004664; F:prephenate dehydratase activity; IEA:InterPro.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:InterPro.
DR   CDD; cd04880; ACT_AAAH-PDT-like; 1.
DR   Gene3D; 1.10.800.10; Aromatic amino acid hydroxylase; 1.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR001273; ArAA_hydroxylase.
DR   InterPro; IPR018301; ArAA_hydroxylase_Fe/CU_BS.
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; PS51671; ACT; 1.
DR   PROSITE; PS00367; BH4_AAA_HYDROXYL_1; 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:UP000189906}.
FT   DOMAIN          125..201
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   DOMAIN          198..544
FT                   /note="Biopterin-dependent aromatic amino acid hydroxylase
FT                   family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51410"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         377
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000336-1"
FT   BINDING         382
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000336-1"
FT   BINDING         422
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000336-1"
SQ   SEQUENCE   546 AA;  61051 MW;  D325253A1DC4B43D CRC64;
     MLQSRSDPGS LFKTPSPSHF PSHTVTPTPP CVQPQMRFIS RLSTNAALSG TVRPARTLSQ
     WPLAAACSQS RSFILPSTFR TRRPALPVSP VCARPLLAAR GHATSSPMTS TEKTATAAST
     CKPSSIYFTI TDSTDGLDGI LALLRSLNIS LTRIESRPSK TKGDYDFYID FMAKDDAHVS
     AALNSIAKLA KAVKSVSSGT SDTDSADGTV PWFPRKIADL DSFAERVLSY GEELDADHPG
     FTDLVYRERR SAITDSAKRH KHGQPLPRVE YSEKEVKTWG IVFNKLMELY KTHACQEHQY
     IFPLLIQNCG YNEHNIPQID DISKFLKDCT GWTMRPVMGL LSSRDFLNAL AFRVFHSTQY
     IRHHTAPFYT PEPDVCHELL GHVPLYADPD FAAFSQEIGL ASLGASDEDL SKLATIYWFT
     VEFGICRQNG ELKAYGAGLL SSFGELEYSL SNKPKHLPFD CERMGVQKYP ITEYQPVYFV
     ADSFLQMKND VREYTTTLKR PFTVHYNALT ESIEILDNKE HIMRFASGVK SDLTRLISAI
     DKVIRE
//
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