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Database: UniProt
Entry: A0A2N7QSZ5_9GAMM
LinkDB: A0A2N7QSZ5_9GAMM
Original site: A0A2N7QSZ5_9GAMM 
ID   A0A2N7QSZ5_9GAMM        Unreviewed;       296 AA.
AC   A0A2N7QSZ5;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 36.
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:PMQ04740.1};
GN   ORFNames=DyAD56_13060 {ECO:0000313|EMBL:PMQ04740.1};
OS   Dyella sp. AD56.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Dyella.
OX   NCBI_TaxID=1528744 {ECO:0000313|EMBL:PMQ04740.1, ECO:0000313|Proteomes:UP000235676};
RN   [1] {ECO:0000313|EMBL:PMQ04740.1, ECO:0000313|Proteomes:UP000235676}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AD56 {ECO:0000313|EMBL:PMQ04740.1,
RC   ECO:0000313|Proteomes:UP000235676};
RA   Schulz-Bohm K., Janssens T.K., De Jager V., Gawehns F., De Boer W.,
RA   Garbeva P.;
RT   "Bacterial performance in fungal presence.";
RL   Submitted (AUG-2017) 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:PMQ04740.1}.
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DR   EMBL; NRDP01000017; PMQ04740.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N7QSZ5; -.
DR   UniPathway; UPA00139; UER00337.
DR   Proteomes; UP000235676; 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   ECO:0000313|EMBL:PMQ04740.1};
KW   Phenylalanine catabolism {ECO:0000256|ARBA:ARBA00023232};
KW   Reference proteome {ECO:0000313|Proteomes:UP000235676}.
FT   DOMAIN          1..296
FT                   /note="Biopterin-dependent aromatic amino acid hydroxylase
FT                   family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51410"
FT   BINDING         135
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
FT   BINDING         140
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;  33592 MW;  81CA37317EFE340C CRC64;
     MSTTPRRVEH QQTDRGYVPV YATGVVDQPW ANYSATDHEV WDTLYKRQRD LLPGRACQEF
     MDGVERFGLG DGGIPKFADL NKVLGATTGW ELVAVEGLLP DEVFFDHLAH RRFPVSWWIR
     KPDQLDYLSE PDLFHDLFGH VPLLLNPVFA DYMQAYGRGG MKAFAIGPEA LMNLTRLYWY
     TVEFGLINTK DGMRIYGAGI VSSKGESIYS LDSASPNRIG FGLERVMSAR YRIDTFQQTY
     FVIDSFEQLF EATRPDFTPI YATLRETTAH AAGDVLDSDR VFTRGNREGW ATNADT
//
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