ID A0A0Q7DKF6_9BURK Unreviewed; 295 AA.
AC A0A0Q7DKF6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=ASC67_19665 {ECO:0000313|EMBL:KQW73696.1};
OS Methylibium sp. Root1272.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Methylibium.
OX NCBI_TaxID=1736441 {ECO:0000313|EMBL:KQW73696.1, ECO:0000313|Proteomes:UP000053968};
RN [1] {ECO:0000313|EMBL:KQW73696.1, ECO:0000313|Proteomes:UP000053968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1272 {ECO:0000313|EMBL:KQW73696.1,
RC ECO:0000313|Proteomes:UP000053968};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW73696.1, ECO:0000313|Proteomes:UP000053968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1272 {ECO:0000313|EMBL:KQW73696.1,
RC ECO:0000313|Proteomes:UP000053968};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQW73696.1}.
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DR EMBL; LMDY01000005; KQW73696.1; -; Genomic_DNA.
DR RefSeq; WP_056316147.1; NZ_LMDY01000005.1.
DR AlphaFoldDB; A0A0Q7DKF6; -.
DR STRING; 1736441.ASC67_19665; -.
DR OrthoDB; 9780502at2; -.
DR UniPathway; UPA00139; UER00337.
DR Proteomes; UP000053968; 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, ECO:0000313|EMBL:KQW73696.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phenylalanine catabolism {ECO:0000256|ARBA:ARBA00023232}.
FT DOMAIN 1..295
FT /note="Biopterin-dependent aromatic amino acid hydroxylase
FT family profile"
FT /evidence="ECO:0000259|PROSITE:PS51410"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 146
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
FT BINDING 151
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
FT BINDING 192
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
SQ SEQUENCE 295 AA; 33196 MW; 1B8AAC36904E5106 CRC64;
MKNDFHDGVN KGVAPVTYGQ GDRPPRGDYS RARADYSCEQ DMARYTEADH ETYRRLYARQ
LRQLPGLACQ EFIDAVEQLG APDRIPRFTD ISARLSKATG WQVVGVPGLI PEEAFFALLA
ERKFPVTDWI RTPEEFDYVV EPDVFHDLFG HVPLLFNPVF ADYMQAYGAG GLKASRLDAC
ELLARLYWYT VEFGLIDTPQ GLRAYGAGIL SSAGELRHAV TSPEPQRIAF DLQRLMRTLY
KIDSYQAGYF VIDSFRQLFD ATAPDFTPVY AAVRRQPLVE AGVVLDGERC FTPAG
//