ID   Q2STC0_BURTA            Unreviewed;       297 AA.
AC   Q2STC0;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   08-OCT-2025, entry version 100.
DE   RecName: Full=Phenylalanine-4-hydroxylase {ECO:0000256|ARBA:ARBA00020276};
DE            EC=1.14.16.1 {ECO:0000256|ARBA:ARBA00011995};
DE   AltName: Full=Phe-4-monooxygenase {ECO:0000256|ARBA:ARBA00029922};
GN   Name=phhA {ECO:0000313|EMBL:ABC37990.1};
GN   OrderedLocusNames=BTH_I3337 {ECO:0000313|EMBL:ABC37990.1};
OS   Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CCUG 48851 /
OS   CIP 106301 / E264).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848 {ECO:0000313|EMBL:ABC37990.1, ECO:0000313|Proteomes:UP000001930};
RN   [1] {ECO:0000313|EMBL:ABC37990.1, ECO:0000313|Proteomes:UP000001930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700388 / DSM 13276 / CCUG 48851 / CIP 106301 / E264
RC   {ECO:0000313|Proteomes:UP000001930};
RX   PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA   Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA   DeShazer D.;
RT   "Bacterial genome adaptation to niches: divergence of the potential
RT   virulence genes in three Burkholderia species of different survival
RT   strategies.";
RL   BMC Genomics 6:174-174(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-phenylalanine +
CC         O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + L-
CC         tyrosine; Xref=Rhea:RHEA:20273, ChEBI:CHEBI:15379, ChEBI:CHEBI:15642,
CC         ChEBI:CHEBI:58095, ChEBI:CHEBI:58315, ChEBI:CHEBI:59560;
CC         EC=1.14.16.1; Evidence={ECO:0000256|ARBA:ARBA00001060};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|ARBA:ARBA00001954,
CC         ECO:0000256|PIRSR:PIRSR601273-2};
CC   -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC       acetoacetate and fumarate from L-phenylalanine: step 1/6.
CC       {ECO:0000256|ARBA:ARBA00005088}.
CC   -!- SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid
CC       hydroxylase family. {ECO:0000256|ARBA:ARBA00009712}.
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DR   EMBL; CP000086; ABC37990.1; -; Genomic_DNA.
DR   RefSeq; WP_011402675.1; NC_007651.1.
DR   AlphaFoldDB; Q2STC0; -.
DR   GeneID; 45123004; -.
DR   KEGG; bte:BTH_I3337; -.
DR   HOGENOM; CLU_023198_1_0_4; -.
DR   UniPathway; UPA00139; UER00337.
DR   Proteomes; UP000001930; Chromosome I.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004505; F:phenylalanine 4-monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03348; pro_PheOH; 1.
DR   Gene3D; 1.10.800.10; Aromatic amino acid hydroxylase; 1.
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; IPR005960; Phe-4-hydroxylase_mono.
DR   NCBIfam; TIGR01267; Phe4hydrox_mono; 1.
DR   NCBIfam; NF008877; PRK11913.1-2; 1.
DR   PANTHER; PTHR11473; AROMATIC AMINO ACID HYDROXYLASE; 1.
DR   PANTHER; PTHR11473:SF24; PHENYLALANINE-4-HYDROXYLASE; 1.
DR   Pfam; PF00351; Biopterin_H; 1.
DR   PRINTS; PR00372; FYWHYDRXLASE.
DR   SUPFAM; SSF56534; Aromatic aminoacid monoxygenases, catalytic and oligomerization domains; 1.
DR   PROSITE; PS00367; BH4_AAA_HYDROXYL_1; 1.
DR   PROSITE; PS51410; BH4_AAA_HYDROXYL_2; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR601273-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR601273-2};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ABC37990.1};
KW   Phenylalanine catabolism {ECO:0000256|ARBA:ARBA00023232};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001930}.
FT   DOMAIN          1..297
FT                   /note="Biopterin-dependent aromatic amino acid hydroxylase
FT                   family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51410"
FT   BINDING         134
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
FT   BINDING         139
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
FT   BINDING         181
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
SQ   SEQUENCE   297 AA;  33069 MW;  649B044E294EE0DC CRC64;
     MSTVVTAKLK EQFDAGLETR ADFTIDQPLA RYGDLDHAVW RQLYARQASL LRGRACDAFI
     GGLARIGLAP DRVPSFADVN RRLEPATGWR IVAVPGLVPD AVFFEHLANR RFPVTWWMRR
     PDQLDYLQEP DCFHDLFGHV PLLIDPVFAD YMHAYGRAAL GVADDPRALA LLARLYWYTV
     EFGLIRGARG ENGLRIYGAG IVSSKGETLY SLESASPNRI GFDLERVMRT RYRIDTLQKT
     YFVIDDFAQL FALADIDART LAARLANAPE HAAGAVLDGD HVLTRGTGEG WATDADA
//