ID   W1SNG6_9BACI            Unreviewed;       579 AA.
AC   W1SNG6;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Phenylalanine 4-monooxygenase {ECO:0000313|EMBL:ETI70630.1};
DE            EC=1.14.16.1 {ECO:0000313|EMBL:ETI70630.1};
GN   ORFNames=BAVI_01620 {ECO:0000313|EMBL:ETI70630.1};
OS   Neobacillus vireti LMG 21834.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX   NCBI_TaxID=1131730 {ECO:0000313|EMBL:ETI70630.1, ECO:0000313|Proteomes:UP000018877};
RN   [1] {ECO:0000313|EMBL:ETI70630.1, ECO:0000313|Proteomes:UP000018877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21834 {ECO:0000313|EMBL:ETI70630.1,
RC   ECO:0000313|Proteomes:UP000018877};
RX   PubMed=24708037; DOI=10.1111/1462-2920.12478;
RA   Mania D., Heylen K., van Spanning R.J., Frostegard A.;
RT   "The nitrate-ammonifying and nosZ-carrying bacterium Bacillus vireti is a
RT   potent source and sink for nitric and nitrous oxide under high nitrate
RT   conditions.";
RL   Environ. Microbiol. 16:3196-3210(2014).
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:ETI70630.1}.
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DR   EMBL; ALAN01000012; ETI70630.1; -; Genomic_DNA.
DR   RefSeq; WP_024026544.1; NZ_ALAN01000012.1.
DR   AlphaFoldDB; W1SNG6; -.
DR   STRING; 220686.AA980_24310; -.
DR   PATRIC; fig|1131730.3.peg.343; -.
DR   eggNOG; COG3186; Bacteria.
DR   OrthoDB; 9780502at2; -.
DR   Proteomes; UP000018877; 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   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:ETI70630.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ETI70630.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018877}.
FT   DOMAIN          1..338
FT                   /note="Biopterin-dependent aromatic amino acid hydroxylase
FT                   family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51410"
FT   BINDING         126
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
FT   BINDING         131
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
FT   BINDING         216
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
SQ   SEQUENCE   579 AA;  64213 MW;  AEF9B8CDEB811AEA CRC64;
     MIGNVVKKIP VQLKQFISKQ YYDSYSPIDH AVWRFVMKQN HYFLKGIAHP YYVNGLKDSG
     IKTESIPKVD DMNTSLAKVG WGAVTIDGLI PGSAFYGFLA NGILPIATEI RKIENIAYTP
     APDMIHEAAG HAPILLDESY RGFVKKIGEM GSKAISSKEK LEVFKAVRHL TIVAEDPHST
     EEQVKEAERQ VAEARTKVKG ISEADQVSRL FWWTVEYGLI GELSDPKIYG AGLLSSVGES
     QSCLADDVQK IPFTVEECVR TPYDVTKPQP QLFVCKNFGE LVSAIDQFAA TMAFRKGGTE
     GLEKALQSDS VATICFSSGL QVTGTVATIL KDDDGEAVYL WTKGPTALSF ENKQLTGHGI
     ETHRKGFGTP IGLLDAGIAL EECSEDQVRD LGISEGKAAL LHFESGVIVK GTVTGILSSG
     AKPILISFKD CTVTYEDQVL FEPDWGTFDM AVGAGIPSVF AGAADPDAYY QFKPAEEIEE
     SAVQRSWNEL ETLYEEVRNI REGSNWNEQS LSQVDRILAV LEDKYQREWL LRLELLEIYQ
     KHNPSHPTVT QLVEKLQNTD WDPSVQQMIQ RGLTLFYYN
//