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Database: UniProt
Entry: A0A1Q8IRT2_9BURK
LinkDB: A0A1Q8IRT2_9BURK
Original site: A0A1Q8IRT2_9BURK 
ID   A0A1Q8IRT2_9BURK        Unreviewed;       300 AA.
AC   A0A1Q8IRT2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=phenylalanine 4-monooxygenase {ECO:0000256|ARBA:ARBA00011995};
DE            EC=1.14.16.1 {ECO:0000256|ARBA:ARBA00011995};
DE   AltName: Full=Phe-4-monooxygenase {ECO:0000256|ARBA:ARBA00029922};
GN   ORFNames=BTH42_23145 {ECO:0000313|EMBL:OLL29383.1};
OS   Burkholderia sp. SRS-W-2-2016.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=1926878 {ECO:0000313|EMBL:OLL29383.1, ECO:0000313|Proteomes:UP000186182};
RN   [1] {ECO:0000313|Proteomes:UP000186182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRS-W-2-2016 {ECO:0000313|Proteomes:UP000186182};
RA   Chauhan A.;
RL   Submitted (DEC-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   -!- 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}.
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:OLL29383.1}.
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DR   EMBL; MSDV01000052; OLL29383.1; -; Genomic_DNA.
DR   RefSeq; WP_075303489.1; NZ_MSDV01000052.1.
DR   AlphaFoldDB; A0A1Q8IRT2; -.
DR   STRING; 1926878.BTH42_23145; -.
DR   Proteomes; UP000186182; Unassembled WGS sequence.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004505; F:phenylalanine 4-monooxygenase activity; IEA:InterPro.
DR   GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:InterPro.
DR   CDD; cd03348; pro_PheOH; 1.
DR   Gene3D; 1.10.800.10; Aromatic amino acid hydroxylase; 1.
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; IPR005960; Phe-4-hydroxylase_mono.
DR   NCBIfam; TIGR01267; Phe4hydrox_mono; 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; 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, ECO:0000313|EMBL:OLL29383.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186182}.
FT   DOMAIN          1..300
FT                   /note="Biopterin-dependent aromatic amino acid hydroxylase
FT                   family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51410"
FT   BINDING         138
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
FT   BINDING         143
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
FT   BINDING         184
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
SQ   SEQUENCE   300 AA;  33661 MW;  9CDBEA44C5EF2670 CRC64;
     MSTATRTAAT AKLQEQFDAG LETRADFTID QPLERYRAVD HAVWRQLYAR QSALLEGRVC
     DEFLAGLARI GMPSDRVPSF DEINAKLTPA TGWRIVAVPG LVPDQVFFEH LANRRFPVTW
     WMRRPDQLDY LQEPDCFHDL FAHVPLLINP VFADYMHAYG RAALAANDAG ALPLLARLYW
     YTVEFGLIRD AASPNGVKIY GAGIVSSQGE TLYSQQSGSP NRLGFELERV MRTRYRIDTF
     QKSYFVIDDF EQLFGVAQTD FAPLLDRLAT APAFAAGDAL ASDRVLTRGS REGWQDDGDV
//
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