ID   PH4H_PSEAE              Reviewed;         262 AA.
AC   P43334;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   08-DEC-2000, sequence version 2.
DT   10-JUN-2026, entry version 146.
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=PA0872;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pseudomonadales; Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC   1C / PRS 101 / PAO1;
RX   PubMed=8108417; DOI=10.1073/pnas.91.4.1366;
RA   Zhao G., Xia T., Song J., Roy R.A.;
RT   "Pseudomonas aeruginosa possesses homologues of mammalian phenylalanine
RT   hydroxylase and 4 alpha-carbinolamine dehydratase/DCoH as part of a three-
RT   component gene cluster.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:1366-1370(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC   1C / PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(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;
CC       Note=Binds 1 Fe(2+) ion.;
CC   -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC       acetoacetate and fumarate from L-phenylalanine: step 1/6.
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid
CC       hydroxylase family. {ECO:0000305}.
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DR   EMBL; M88627; AAA25936.1; -; Genomic_DNA.
DR   EMBL; AE004091; AAG04261.1; -; Genomic_DNA.
DR   PIR; A53452; A53452.
DR   PIR; F83535; F83535.
DR   RefSeq; NP_249563.1; NC_002516.2.
DR   RefSeq; WP_003114241.1; NC_002516.2.
DR   AlphaFoldDB; P43334; -.
DR   SMR; P43334; -.
DR   STRING; 208964.PA0872; -.
DR   PaxDb; 208964-PA0872; -.
DR   DNASU; 879709; -.
DR   GeneID; 879709; -.
DR   KEGG; pae:PA0872; -.
DR   PATRIC; fig|208964.12.peg.906; -.
DR   PseudoCAP; PA0872; -.
DR   HOGENOM; CLU_023198_1_1_6; -.
DR   InParanoid; P43334; -.
DR   OrthoDB; 9780502at2; -.
DR   PhylomeDB; P43334; -.
DR   BioCyc; PAER208964:G1FZ6-887-MONOMER; -.
DR   UniPathway; UPA00139; UER00337.
DR   Proteomes; UP000002438; Chromosome.
DR   AbasyAtlas; P43334; -.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IBA:GO_Central.
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; 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   InterPro; IPR005960; Phe-4-hydroxylase_mono.
DR   NCBIfam; TIGR01267; Phe4hydrox_mono; 1.
DR   NCBIfam; NF008877; PRK11913.1-2; 1.
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; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Phenylalanine catabolism; Reference proteome.
FT   CHAIN           1..262
FT                   /note="Phenylalanine-4-hydroxylase"
FT                   /id="PRO_0000205555"
FT   BINDING         121
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         126
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         166
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        135
FT                   /note="F -> L (in Ref. 1; AAA25936)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   262 AA;  30322 MW;  A5665839C5961A45 CRC64;
     MKTTQYVARQ PDDNGFIHYP ETEHQVWNTL ITRQLKVIEG RACQEYLDGI EQLGLPHERI
     PQLDEINRVL QATTGWRVAR VPALIPFQTF FELLASQQFP VATFIRTPEE LDYLQEPDIF
     HEIFGHCPLL TNPWFAEFTH TYGKLGLKAS KEERVFLARL YWMTIEFGLV ETDQGKRIYG
     GGILSSPKET VYSLSDEPLH QAFNPLEAMR TPYRIDILQP LYFVLPDLKR LFQLAQEDIM
     ALVHEAMRLG LHAPLFPPKQ AA
//