ID A0A1G5Y4I9_9BACT Unreviewed; 263 AA.
AC A0A1G5Y4I9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=phenylalanine 4-monooxygenase {ECO:0000256|ARBA:ARBA00011995};
DE EC=1.14.16.1 {ECO:0000256|ARBA:ARBA00011995};
DE AltName: Full=Phe-4-monooxygenase {ECO:0000256|ARBA:ARBA00029922};
GN ORFNames=SAMN03080617_02220 {ECO:0000313|EMBL:SDA76905.1};
OS Algoriphagus alkaliphilus.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Algoriphagus.
OX NCBI_TaxID=279824 {ECO:0000313|EMBL:SDA76905.1, ECO:0000313|Proteomes:UP000198756};
RN [1] {ECO:0000313|EMBL:SDA76905.1, ECO:0000313|Proteomes:UP000198756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22703 {ECO:0000313|EMBL:SDA76905.1,
RC ECO:0000313|Proteomes:UP000198756};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FMXE01000013; SDA76905.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5Y4I9; -.
DR STRING; 279824.SAMN03080617_02220; -.
DR OrthoDB; 9780502at2; -.
DR Proteomes; UP000198756; Unassembled WGS sequence.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004505; F:phenylalanine 4-monooxygenase activity; IEA:InterPro.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:InterPro.
DR CDD; cd00361; arom_aa_hydroxylase; 1.
DR Gene3D; 1.10.800.10; Aromatic amino acid hydroxylase; 1.
DR InterPro; IPR001273; ArAA_hydroxylase.
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; 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}.
FT DOMAIN 1..263
FT /note="Biopterin-dependent aromatic amino acid hydroxylase
FT family profile"
FT /evidence="ECO:0000259|PROSITE:PS51410"
FT BINDING 127
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
FT BINDING 132
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
FT BINDING 174
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
SQ SEQUENCE 263 AA; 31167 MW; 818B475565FCF1A3 CRC64;
MTDKPKDWVF TDPRLIELKQ DYAAYTEEDF KVWRILFERQ MPNLPKAASQ AYLEGVEKVR
FTADRIANFE ELNEILETQT GWKVQVVPGL IDDDLFFGLL NNKRFPSSTW LRKMEQLDYL
EEPDMFHDAF AHMPLLVNQH YVDFLENLSG IALKHIQNPW AIQLLSRIYW FTIEFGLIRE
NGKLKVYGAG ILSSAGETKF SLSDEPKHFP YDVRQIMSTE YWKDRFQDKY WVIDSYEQLF
ESLPEIEEVL EEMLANKTQD ARQ
//
