ID   PH4H_VIBCH              Reviewed;         289 AA.
AC   Q9KLB8;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 112.
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=VC_A0828;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(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; AE003853; AAF96726.1; -; Genomic_DNA.
DR   PIR; D82413; D82413.
DR   AlphaFoldDB; Q9KLB8; -.
DR   SMR; Q9KLB8; -.
DR   STRING; 243277.VC_A0828; -.
DR   PRIDE; Q9KLB8; -.
DR   DNASU; 2612712; -.
DR   EnsemblBacteria; AAF96726; AAF96726; VC_A0828.
DR   KEGG; vch:VC_A0828; -.
DR   eggNOG; COG3186; Bacteria.
DR   HOGENOM; CLU_023198_1_1_6; -.
DR   OMA; KQFPVAT; -.
DR   BioCyc; VCHO:VCA0828-MON; -.
DR   UniPathway; UPA00139; UER00337.
DR   Proteomes; UP000000584; Chromosome 2.
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..289
FT                   /note="Phenylalanine-4-hydroxylase"
FT                   /id="PRO_0000205558"
FT   BINDING         144
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255"
FT   BINDING         149
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255"
FT   BINDING         189
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   289 AA;  33445 MW;  2D68B31C6E31D521 CRC64;
     MSKIPLAVRI GLGRLNVTNL LRSRAMTQYH SKPVSEHGHI DWDQDEHAVW HELITRQQEV
     VKTRACQAYL DGLNMLNLPT DRLPQLPEIN RVLQRETGWQ VEPVPALISF DRFFALLADK
     KFPVATFLRR REEFDYLQEP DFFHEVYGHC AMLTHPDFAA FTHVYGQLGA KATPKERSYL
     ARLYWFTVEF GLVQEQGQTK IYGGGILSSP GETLYASEST IPKREPFDIM QVLRTPYRID
     IMQPIYYVLP DLSQLYQLSQ RDVMALVWQA MQDGLLPPLF QPKEQQHAG