位置:首页 > 蛋白库 > PH4H_RALSO
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024