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Database: UniProt
Entry: A0A1G9V0N2_9BACT
LinkDB: A0A1G9V0N2_9BACT
Original site: A0A1G9V0N2_9BACT 
ID   A0A1G9V0N2_9BACT        Unreviewed;       256 AA.
AC   A0A1G9V0N2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Phenylalanine 4-hydroxylase {ECO:0000313|EMBL:SDM65566.1};
GN   ORFNames=SAMN04488090_3912 {ECO:0000313|EMBL:SDM65566.1};
OS   Siphonobacter aquaeclarae.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae;
OC   Siphonobacter.
OX   NCBI_TaxID=563176 {ECO:0000313|EMBL:SDM65566.1, ECO:0000313|Proteomes:UP000198901};
RN   [1] {ECO:0000313|EMBL:SDM65566.1, ECO:0000313|Proteomes:UP000198901}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21668 {ECO:0000313|EMBL:SDM65566.1,
RC   ECO:0000313|Proteomes:UP000198901};
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   -!- SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid
CC       hydroxylase family. {ECO:0000256|ARBA:ARBA00009712}.
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DR   EMBL; FNGS01000008; SDM65566.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9V0N2; -.
DR   STRING; 563176.SAMN04488090_3912; -.
DR   Proteomes; UP000198901; Unassembled WGS sequence.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004505; F:phenylalanine 4-monooxygenase activity; IEA:UniProt.
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; 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   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};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198901}.
FT   DOMAIN          1..256
FT                   /note="Biopterin-dependent aromatic amino acid hydroxylase
FT                   family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51410"
FT   BINDING         121
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
FT   BINDING         126
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
FT   BINDING         168
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
SQ   SEQUENCE   256 AA;  29731 MW;  643201CE1708616A CRC64;
     MSSPYAFVPY SLKQEYARYT SDDQDVWKIL FERQLALLPG RASEAYFEGL RLTGLTAEAI
     PRYEEVSDRL RELTGWAIHV VPGLIANRPF FELMRDKQFC ASTWLRSREQ LDYLEEPDMF
     HDIFGHVPML SKKAVCHFLE ELARIALRFV DIPEAIEYIA RLYWYTIEFG LVREKGELRI
     YGAGILSSTG ESQYCLGGSV ATFPYDIRMI FQTPYIKEHY QDQYFVIDSY DQLFHSIPAI
     ETELEHLLGA AVVLAH
//
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