ID   PH4H_RHILO              Reviewed;         275 AA.
AC   Q98D72;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Phenylalanine-4-hydroxylase;
DE            Short=PAH;
DE            EC=1.14.16.1;
DE   AltName: Full=Phe-4-monooxygenase;
GN   Name=phhA; OrderedLocusNames=mlr4831;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-phenylalanine +
CC         O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + L-
CC         tyrosine; Xref=Rhea:RHEA:20273, ChEBI:CHEBI:15379, ChEBI:CHEBI:15642,
CC         ChEBI:CHEBI:58095, ChEBI:CHEBI:58315, ChEBI:CHEBI:59560;
CC         EC=1.14.16.1;
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe(2+) ion. {ECO:0000250};
CC   -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC       acetoacetate and fumarate from L-phenylalanine: step 1/6.
CC   -!- SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid
CC       hydroxylase family. {ECO:0000305}.
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DR   EMBL; BA000012; BAB51399.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q98D72; -.
DR   SMR; Q98D72; -.
DR   STRING; 266835.14024797; -.
DR   EnsemblBacteria; BAB51399; BAB51399; BAB51399.
DR   KEGG; mlo:mlr4831; -.
DR   eggNOG; COG3186; Bacteria.
DR   HOGENOM; CLU_023198_1_0_5; -.
DR   OMA; KQFPVAT; -.
DR   UniPathway; UPA00139; UER00337.
DR   Proteomes; UP000000552; Chromosome.
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-UniPathway.
DR   CDD; cd03348; pro_PheOH; 1.
DR   Gene3D; 1.10.800.10; -; 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   InterPro; IPR005960; Phe-4-hydroxylase_mono.
DR   PANTHER; PTHR11473; PTHR11473; 1.
DR   Pfam; PF00351; Biopterin_H; 1.
DR   PRINTS; PR00372; FYWHYDRXLASE.
DR   SUPFAM; SSF56534; SSF56534; 1.
DR   TIGRFAMs; TIGR01267; Phe4hydrox_mono; 1.
DR   PROSITE; PS00367; BH4_AAA_HYDROXYL_1; 1.
DR   PROSITE; PS51410; BH4_AAA_HYDROXYL_2; 1.
PE   3: Inferred from homology;
KW   Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Phenylalanine catabolism.
FT   CHAIN           1..275
FT                   /note="Phenylalanine-4-hydroxylase"
FT                   /id="PRO_0000205557"
FT   BINDING         135
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255"
FT   BINDING         140
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255"
FT   BINDING         181
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   275 AA;  31348 MW;  BC29D255534BC215 CRC64;
     MSVAEYARDC AAQGLRGDYS VCRADFTVAQ DYDYSDEEQA VWRTLCDRQT KLTRKLAHHS
     YLDGVEKLGL LDRIPDFEDV STKLRKLTGW EIIAVPGLIP AAPFFDHLAN RRFPVTNWLR
     TRQELDYIVE PDMFHDFFGH VPVLSQPVFA DFMQMYGKKA GDIIALGGDE MITRLYWYTA
     EYGLVQEAGQ PLKAFGAGLM SSFTELQFAV EGKDAHHVPF DLETVMRTGY EIDKFQRAYF
     VLPSFDALRD AFQTADFEAI VARRKDQKAL DPATV