PH4H_PSEAE
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 03-AUG-2022, entry version 135.
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; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC 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 / 1C /
RC 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 / 1C /
RC 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; NZ_QZGE01000007.1.
DR AlphaFoldDB; P43334; -.
DR SMR; P43334; -.
DR STRING; 287.DR97_1071; -.
DR PaxDb; P43334; -.
DR PRIDE; P43334; -.
DR DNASU; 879709; -.
DR EnsemblBacteria; AAG04261; AAG04261; PA0872.
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 OMA; KQFPVAT; -.
DR PhylomeDB; P43334; -.
DR BioCyc; PAER208964:G1FZ6-887-MON; -.
DR UniPathway; UPA00139; UER00337.
DR Proteomes; UP000002438; 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; 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
