ID A0A031JWX3_9SPHN Unreviewed; 284 AA.
AC A0A031JWX3;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
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=BES08_10050 {ECO:0000313|EMBL:AOR77055.1}, BV97_02637
GN {ECO:0000313|EMBL:EZP81420.1};
OS Novosphingobium resinovorum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=158500 {ECO:0000313|EMBL:EZP81420.1, ECO:0000313|Proteomes:UP000024329};
RN [1] {ECO:0000313|EMBL:EZP81420.1, ECO:0000313|Proteomes:UP000024329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KF1 {ECO:0000313|EMBL:EZP81420.1,
RC ECO:0000313|Proteomes:UP000024329};
RA Gan H.M., Gan H.Y., Chew T.H., Savka M.A.;
RT "Whole genome sequence of Novosphingobium resinovorum KF1.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AOR77055.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA1 {ECO:0000313|EMBL:AOR77055.1};
RA Seilhamer J.J.;
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000094626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA1 {ECO:0000313|Proteomes:UP000094626};
RX PubMed=27851894; DOI=10.1016/j.jbiotec.2016.11.013;
RA Hegedus B., Kos P.B., Balint B., Maroti G., Gan H.M., Perei K., Rakhely G.;
RT "Complete genome sequence of Novosphingobium resinovorum SA1, a versatile
RT xenobiotic-degrading bacterium capable of utilizing sulfanilic acid.";
RL J. Biotechnol. 241:76-80(2017).
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}.
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DR EMBL; CP017075; AOR77055.1; -; Genomic_DNA.
DR EMBL; JFYZ01000012; EZP81420.1; -; Genomic_DNA.
DR RefSeq; WP_036526326.1; NZ_JFYZ01000012.1.
DR AlphaFoldDB; A0A031JWX3; -.
DR STRING; 158500.BES08_10050; -.
DR KEGG; nre:BES08_10050; -.
DR PATRIC; fig|158500.4.peg.2696; -.
DR eggNOG; COG3186; Bacteria.
DR OrthoDB; 9780502at2; -.
DR UniPathway; UPA00139; UER00337.
DR Proteomes; UP000024329; Unassembled WGS sequence.
DR Proteomes; UP000094626; Chromosome.
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:EZP81420.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phenylalanine catabolism {ECO:0000256|ARBA:ARBA00023232}.
FT DOMAIN 1..284
FT /note="Biopterin-dependent aromatic amino acid hydroxylase
FT family profile"
FT /evidence="ECO:0000259|PROSITE:PS51410"
FT BINDING 134
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
FT BINDING 139
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
FT BINDING 180
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
SQ SEQUENCE 284 AA; 32212 MW; AF949F5B95D19E4B CRC64;
MKKPSTITSN SGLRGEYDRA ADDYTVAQDW HAYTPEMHAR WRRLYARQSA LVRTHACASF
REGLARLDCA EGIPRFADAN RVLQAATGWR LVAVPGFIPD AVFFDHLAHR RFPVTRWLRE
EHELDYLAEP DVFHDFFGHV PMLLDPTIAD FLELYGKAGA RAMAMGALDM LARIYWYTIE
FGLVREDGAL KVFGAGIISS AGETRFSIED REVLRLPFDP VRVMRTSYMI DSFQKTYFVL
ESLPQLIEAL VSLDFGPVYE TWRHEPPLPA GEALPEETPI GALA
//
