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Database: UniProt
Entry: A0A0J1H8A4_9GAMM
LinkDB: A0A0J1H8A4_9GAMM
Original site: A0A0J1H8A4_9GAMM 
ID   A0A0J1H8A4_9GAMM        Unreviewed;       303 AA.
AC   A0A0J1H8A4;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
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:KLV07949.1};
GN   ORFNames=ABT57_13930 {ECO:0000313|EMBL:KLV07949.1};
OS   Photobacterium ganghwense.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=320778 {ECO:0000313|EMBL:KLV07949.1, ECO:0000313|Proteomes:UP000035909};
RN   [1] {ECO:0000313|EMBL:KLV07949.1, ECO:0000313|Proteomes:UP000035909}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22954 {ECO:0000313|EMBL:KLV07949.1,
RC   ECO:0000313|Proteomes:UP000035909};
RA   Machado H., Gram L.;
RT   "Photobacterium galathea sp. nov.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KLV07949.1}.
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DR   EMBL; LDOU01000015; KLV07949.1; -; Genomic_DNA.
DR   RefSeq; WP_047885842.1; NZ_PYMI01000004.1.
DR   AlphaFoldDB; A0A0J1H8A4; -.
DR   STRING; 320778.ABT57_13930; -.
DR   PATRIC; fig|320778.3.peg.3033; -.
DR   OrthoDB; 9780502at2; -.
DR   UniPathway; UPA00139; UER00337.
DR   Proteomes; UP000035909; Unassembled WGS sequence.
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   PANTHER; PTHR11473; AROMATIC AMINO ACID HYDROXYLASE; 1.
DR   PANTHER; PTHR11473:SF24; PHENYLALANINE-4-HYDROXYLASE; 1.
DR   Pfam; PF00351; Biopterin_H; 1.
DR   SUPFAM; SSF56534; Aromatic aminoacid monoxygenases, catalytic and oligomerization domains; 2.
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, ECO:0000313|EMBL:KLV07949.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:KLV07949.1};
KW   Phenylalanine catabolism {ECO:0000256|ARBA:ARBA00023232};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035909}.
FT   DOMAIN          1..303
FT                   /note="Biopterin-dependent aromatic amino acid hydroxylase
FT                   family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51410"
FT   BINDING         122
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
FT   BINDING         127
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
FT   BINDING         167
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
SQ   SEQUENCE   303 AA;  34690 MW;  A2519AFBC6BD567F CRC64;
     MGSATKYVSK KPDERGFVDW DQSENQIWHD LVTRQLSCVS GRACQAYIDG LKMLNLPIDK
     APQLGDVNRV LKAQTGWECV AVPALINFDR FFELLANKQF PVATFLRSRE EFDYLQEPDF
     FHEIFGHCAM LTNPAFAEFT HTYGKLGFSA SPKDRVYLAR LYWFTVEFGL LQETNGIRIY
     GGGILSSPGE TRFALTGDFE SANDSVNDPE SGLNQQNTEQ IELSQREVKP IYRPFDPIDI
     MRTPYRIDIM QPVYFILDDI QQLFELAQQD IMSMVEQAKA MGLHEPLFPP KNKDEDKKVG
     NYV
//
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