PH4H_RALSO
ID PH4H_RALSO Reviewed; 313 AA.
AC Q8XU39;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 119.
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=RSc3355; ORFNames=RS02630;
OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=267608;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GMI1000;
RX PubMed=11823852; DOI=10.1038/415497a;
RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL Nature 415:497-502(2002).
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; AL646052; CAD17143.1; -; Genomic_DNA.
DR RefSeq; WP_011003237.1; NC_003295.1.
DR AlphaFoldDB; Q8XU39; -.
DR SMR; Q8XU39; -.
DR STRING; 267608.RSc3355; -.
DR EnsemblBacteria; CAD17143; CAD17143; RSc3355.
DR GeneID; 60502867; -.
DR KEGG; rso:RSc3355; -.
DR PATRIC; fig|267608.8.peg.3406; -.
DR eggNOG; COG3186; Bacteria.
DR HOGENOM; CLU_023198_1_0_4; -.
DR OMA; KQFPVAT; -.
DR UniPathway; UPA00139; UER00337.
DR Proteomes; UP000001436; 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..313
FT /note="Phenylalanine-4-hydroxylase"
FT /id="PRO_0000205556"
FT BINDING 154
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 159
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 200
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
SQ SEQUENCE 313 AA; 34901 MW; 2EBA9E216476371B CRC64;
MAIATPTSAA PTPAPAGFTG TLTDKLREQF AEGLDGQTLR PDFTMEQPVH RYTAADHATW
RTLYDRQEAL LPGRACDEFL QGLSTLGMSR EGVPSFDRLN ETLMRATGWQ IVAVPGLVPD
EVFFEHLANR RFPASWWMRR PDQLDYLQEP DGFHDIFGHV PLLINPVFAD YMQAYGQGGL
KAARLGALDM LARLYWYTVE FGLIRTPAGL RIYGAGIVSS KSESVYALDS ASPNRIGFDV
HRIMRTRYRI DTFQKTYFVI DSFEQLFDAT RPDFTPLYEA LGTLPTFGAG DVVDGDAVLN
AGTREGWADT ADI