ID A0A0Q4LEU2_9SPHI Unreviewed; 592 AA.
AC A0A0Q4LEU2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Phenylalanine 4-monooxygenase {ECO:0000313|EMBL:KQN33422.1};
GN ORFNames=ASE92_16640 {ECO:0000313|EMBL:KQN33422.1};
OS Pedobacter sp. Leaf41.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1736218 {ECO:0000313|EMBL:KQN33422.1, ECO:0000313|Proteomes:UP000051488};
RN [1] {ECO:0000313|Proteomes:UP000051488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf41 {ECO:0000313|Proteomes:UP000051488};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000051488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf41 {ECO:0000313|Proteomes:UP000051488};
RA Vorholt J.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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 -!- 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:KQN33422.1}.
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DR EMBL; LMLE01000010; KQN33422.1; -; Genomic_DNA.
DR RefSeq; WP_056851372.1; NZ_LMLE01000010.1.
DR AlphaFoldDB; A0A0Q4LEU2; -.
DR STRING; 1736218.ASE92_16640; -.
DR OrthoDB; 9780502at2; -.
DR Proteomes; UP000051488; Unassembled WGS sequence.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016714; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygen; IEA:InterPro.
DR GO; GO:0009072; P:aromatic amino acid metabolic process; IEA:InterPro.
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 PANTHER; PTHR11473; AROMATIC AMINO ACID HYDROXYLASE; 1.
DR PANTHER; PTHR11473:SF24; PHENYLALANINE-4-HYDROXYLASE; 1.
DR Pfam; PF00351; Biopterin_H; 2.
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, ECO:0000313|EMBL:KQN33422.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 1..343
FT /note="Biopterin-dependent aromatic amino acid hydroxylase
FT family profile"
FT /evidence="ECO:0000259|PROSITE:PS51410"
FT BINDING 132
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
FT BINDING 137
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
FT BINDING 222
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
SQ SEQUENCE 592 AA; 66894 MW; 9A08C3F249AA2130 CRC64;
MSHFNDFNNA QVAKLPKHLK QFIVDQNYEK YTPIDQAVWR YVMRQNYSYL KNVAYYPYIK
GLQRAGLSIE HIPDLQTMND NLGKIGWGAV TVDGFIPPAA FMEYQAYRVL VIAADIRQIN
HIEYTPAPDI IHESAGHAPI IADTDYNNYL SYFGSIGAKA MFSAKDFELY EAIRKLSILK
EAVDANDSEI AKSEKELRYI NENMGEPSEM ALLGRLHWWT VEYGLIGTLE NPKIYGAGLL
SSIGESASCM QRHVEKIWYN MDTINYAYDI TKPQPQLFVT ETFQNLIDVL ETFANTMAFR
VGGAESVMKA IDCKNVATAV YSSGLQVSGI FTDIGLNADD EVTFIKTTGV SALAFAGKQL
ENHGKDYHKD GFSSPVGRLK SSLKPLENSS DEEMELAGLY LGNKTNLTFE SGITVAGKVN
NILKRAEKII LITFEECTVT EGNGNVLFKP EWGIYDMAVG DKIVSVFNGA ADKDAFEEIT
LVSLEKTQQI VYDDKTLKLH QFYKTVREIR ESGDHLAKLP DIFDQLRTNH RQDWLCALEI
LELVYHKKIY HQLERDVLIY LELKAAREAD HRKLINDGLH VIKNPVSQLV VE
//
