ID A0A1Y2SJY3_9GAMM Unreviewed; 272 AA.
AC A0A1Y2SJY3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Phenylalanine-4-hydroxylase {ECO:0000313|EMBL:OTA18205.1};
DE EC=1.14.16.1 {ECO:0000313|EMBL:OTA18205.1};
GN Name=phhA {ECO:0000313|EMBL:OTA18205.1};
GN ORFNames=Xvie_00019 {ECO:0000313|EMBL:OTA18205.1};
OS Xenorhabdus vietnamensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=351656 {ECO:0000313|EMBL:OTA18205.1, ECO:0000313|Proteomes:UP000194350};
RN [1] {ECO:0000313|EMBL:OTA18205.1, ECO:0000313|Proteomes:UP000194350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22392 {ECO:0000313|EMBL:OTA18205.1,
RC ECO:0000313|Proteomes:UP000194350};
RA Tobias N.J., Wolff H., Djahanschiri B., Pidot S.J., Stinear T.P.,
RA Ebersberger I., Bode H.B.;
RT "Systematic genetic and metabolomic analysis of Xenorhabdus and
RT Photorhabdus spp., highlights the requirements for a dual symbiotic and
RT pathogenic life style.";
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}.
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:OTA18205.1}.
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DR EMBL; MUBJ01000001; OTA18205.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2SJY3; -.
DR STRING; 351656.Xvie_00019; -.
DR OrthoDB; 9780502at2; -.
DR Proteomes; UP000194350; 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 GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-KW.
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 ECO:0000313|EMBL:OTA18205.1};
KW Phenylalanine catabolism {ECO:0000256|ARBA:ARBA00023232}.
FT DOMAIN 1..272
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 172
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
SQ SEQUENCE 272 AA; 31559 MW; F594364156F49728 CRC64;
MGNSSSVSKF GYVAKQPDSN GEIYFSISEH EIWNKLYSRQ INLIQEHAFY QYLEGIKHLN
LDDNGIPRLS KINSILLKST GWQLQPVDCT ISFDYFFHLL SNKKFPAAAF IRRSEDFDFV
PVPDIFHEIF GHCPLLLNKE YANLSYKIGK LGVKMSKEDQ KYLARIYWFT IETGLIKSNK
NIEIYGGSIL SSYSEYNYAT TSELPLRLPF NLLDILRTPY RVDVLPNVYF NISSFEQLQE
ITEEIIIEYI EKAKVLGDFR SLYPPRDIAK IA
//
