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Database: UniProt
Entry: A0A316F2J7_9BURK
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ID   A0A316F2J7_9BURK        Unreviewed;       296 AA.
AC   A0A316F2J7;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
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   ORFNames=C7419_1012917 {ECO:0000313|EMBL:PWK39014.1};
OS   Cupriavidus plantarum.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=942865 {ECO:0000313|EMBL:PWK39014.1, ECO:0000313|Proteomes:UP000245754};
RN   [1] {ECO:0000313|EMBL:PWK39014.1, ECO:0000313|Proteomes:UP000245754}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SLV-132 {ECO:0000313|EMBL:PWK39014.1,
RC   ECO:0000313|Proteomes:UP000245754};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-V): Genome sequencing
RT   to study the core and pangenomes of soil and plant-associated
RT   prokaryotes.";
RL   Submitted (MAY-2018) 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:PWK39014.1}.
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DR   EMBL; QGGT01000001; PWK39014.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316F2J7; -.
DR   OrthoDB; 9780502at2; -.
DR   UniPathway; UPA00139; UER00337.
DR   Proteomes; UP000245754; 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   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   Phenylalanine catabolism {ECO:0000256|ARBA:ARBA00023232};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245754}.
FT   DOMAIN          1..296
FT                   /note="Biopterin-dependent aromatic amino acid hydroxylase
FT                   family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51410"
FT   BINDING         137
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
FT   BINDING         142
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
FT   BINDING         183
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
SQ   SEQUENCE   296 AA;  33631 MW;  D01DDDA7F05B7A95 CRC64;
     MITLTEKLKE QFDAGLLSGE TLRDDFTIAQ PVHRYTDTDH AMWRTLYERQ AAMLKGRVCN
     EFLEGLDTLG MDKHRVPDFG ALNERLMRAT GWQIVAVPGL VPDEVFFEHL ANRRFPASWW
     MRKPEQLDYL QEPDCFHDVF GHVPLLINPV FADYMEAYGK GGLKAHGLGA LDMLARLYWY
     TVEFGLIRTP EGLRIYGAGI VSSQGESIYS LDAASPNRIG FDVRRIMRTR YRIDTFQKTY
     FVIDSFEQLF EATGPDFTPL YDALRAQPTM GAGDIAEGDT VIHAGTREGW GDSDDI
//
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