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Database: UniProt
Entry: A0A1G0SIE2_9BACT
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Original site: A0A1G0SIE2_9BACT 
ID   A0A1G0SIE2_9BACT        Unreviewed;       272 AA.
AC   A0A1G0SIE2;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Phenylalanine 4-monooxygenase {ECO:0000313|EMBL:OGU72151.1};
GN   ORFNames=A2V93_08635 {ECO:0000313|EMBL:OGU72151.1};
OS   Ignavibacteria bacterium RBG_16_34_14.
OC   Bacteria; Ignavibacteriota; Ignavibacteria.
OX   NCBI_TaxID=1798433 {ECO:0000313|EMBL:OGU72151.1, ECO:0000313|Proteomes:UP000176348};
RN   [1] {ECO:0000313|EMBL:OGU72151.1, ECO:0000313|Proteomes:UP000176348}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGU72151.1}.
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DR   EMBL; MHAF01000135; OGU72151.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G0SIE2; -.
DR   STRING; 1798433.A2V93_08635; -.
DR   Proteomes; UP000176348; 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   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   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, ECO:0000313|EMBL:OGU72151.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          1..272
FT                   /note="Biopterin-dependent aromatic amino acid hydroxylase
FT                   family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51410"
FT   BINDING         148
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
FT   BINDING         153
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
FT   BINDING         193
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
SQ   SEQUENCE   272 AA;  31793 MW;  AC639FF343AFAB66 CRC64;
     MQNKKEEKEF KSAYEKAAEK GIDPRCIPQR LTGPVPVDDK IEYPDYPESD NETWKFLYDR
     QMKNLPGRVC QEYLDGVDIL NFTRDKIPAL KDLSAVFKKT TGWMIARVPG LIHEQNFFEL
     LRERIFPSTD YIRGKGELDY TPAPDCFHDM FGHMPLLTNK NFASFYQMFG EAALNAKGEN
     RKFLETFHWF TVEFGLIRQK EGMRIYGAGI ISSKEEVNHA LSNEVEVKDF IPGKLVQQQY
     DVWHLQPILF TINSFKQLEE GFKEWTKKRG LL
//
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