PH4H_CAUVC
ID PH4H_CAUVC Reviewed; 294 AA.
AC Q9A7V7;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=CC_1612;
OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=190650;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=11259647; DOI=10.1073/pnas.061029298;
RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT "Complete genome sequence of Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
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; AE005673; AAK23591.1; -; Genomic_DNA.
DR PIR; C87449; C87449.
DR RefSeq; NP_420423.1; NC_002696.2.
DR RefSeq; WP_010919486.1; NC_002696.2.
DR AlphaFoldDB; Q9A7V7; -.
DR SMR; Q9A7V7; -.
DR STRING; 190650.CC_1612; -.
DR EnsemblBacteria; AAK23591; AAK23591; CC_1612.
DR KEGG; ccr:CC_1612; -.
DR PATRIC; fig|190650.5.peg.1639; -.
DR eggNOG; COG3186; Bacteria.
DR HOGENOM; CLU_023198_1_0_5; -.
DR OMA; KQFPVAT; -.
DR BioCyc; CAULO:CC1612-MON; -.
DR UniPathway; UPA00139; UER00337.
DR Proteomes; UP000001816; 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..294
FT /note="Phenylalanine-4-hydroxylase"
FT /id="PRO_0000205554"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 129
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 134
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 175
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
SQ SEQUENCE 294 AA; 32761 MW; A623276FD0506720 CRC64;
MSGDGLSNGP PPGARPDWTI DQGWETYTQA EHDVWITLYE RQTDMLHGRA CDEFMRGLDA
LDLHRSGIPD FARINEELKR LTGWTVVAVP GLVPDDVFFD HLANRRFPAG QFIRKPHELD
YLQEPDIFHD VFGHVPMLTD PVFADYMQAY GEGGRRALGL GRLANLARLY WYTVEFGLMN
TPAGLRIYGA GIVSSRTESI FALDDPSPNR IGFDLERVMR TLYRIDDFQQ VYFVIDSIQT
LQEVTLRDFG AIYERLASVS DIGVAEIVPG DAVLTRGTQA YATAGGRLAG AAAG
