ID Q6EMJ5_PSEPU Unreviewed; 262 AA. AC Q6EMJ5; DT 16-AUG-2004, integrated into UniProtKB/TrEMBL. DT 16-AUG-2004, sequence version 1. DT 12-AUG-2020, entry version 56. DE RecName: Full=Phe-4-monooxygenase {ECO:0000256|ARBA:ARBA00020694}; DE EC=1.14.16.1 {ECO:0000256|ARBA:ARBA00011995}; DE AltName: Full=Phenylalanine-4-hydroxylase {ECO:0000256|ARBA:ARBA00020276}; GN Name=phhA {ECO:0000313|EMBL:AAO12521.1}; GN ORFNames=B7H18_23855 {ECO:0000313|EMBL:ORL49141.1}, B8W72_13760 GN {ECO:0000313|EMBL:OUM32681.1}; OS Pseudomonas putida (Arthrobacter siderocapsulatus). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=303 {ECO:0000313|EMBL:AAO12521.1}; RN [1] {ECO:0000313|EMBL:AAO12521.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=U {ECO:0000313|EMBL:AAO12521.1}; RX PubMed=15262943; DOI=10.1128/JB.186.15.5062-5077.2004; RA Arias-Barrau E., Olivera E.R., Luengo J.M., Fernandez C., Galan B., RA Garcia J.L., Diaz E., Minambres B.; RT "The homogentisate pathway: a central catabolic pathway involved in the RT degradation of L-phenylalanine, L-tyrosine, and 3-hydroxyphenylacetate in RT Pseudomonas putida."; RL J. Bacteriol. 186:5062-5077(2004). RN [2] {ECO:0000313|EMBL:ORL49141.1, ECO:0000313|Proteomes:UP000193308} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DZ-C20 {ECO:0000313|EMBL:ORL49141.1, RC ECO:0000313|Proteomes:UP000193308}; RA Zhang R.; RT "Presence of VIM-2 positive Pseudomonas species in chickens and their RT surrounding environment."; RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:OUM32681.1, ECO:0000313|Proteomes:UP000196082} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1312 {ECO:0000313|EMBL:OUM32681.1, RC ECO:0000313|Proteomes:UP000196082}; RA Crovadore J., Blanc P., Chablais R., Cochard B., Grizard D., Lefort F.; RT "Whole genome sequence of Pseudomonas putida isolate 1312 commercialized as RT a biostimulant."; RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases. 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; Evidence={ECO:0000256|ARBA:ARBA00001060}; CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000256|ARBA:ARBA00001954}; CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation; CC acetoacetate and fumarate from L-phenylalanine: step 1/6. CC {ECO:0000256|ARBA:ARBA00005088}. CC -!- SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid CC hydroxylase family. {ECO:0000256|ARBA:ARBA00009712}. 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; AY168852; AAO12521.1; -; Genomic_DNA. DR EMBL; NBWB01000030; ORL49141.1; -; Genomic_DNA. DR EMBL; NFSB01000075; OUM32681.1; -; Genomic_DNA. DR RefSeq; WP_016498483.1; NZ_WOWR01000001.1. DR GeneID; 45522860; -. DR BioCyc; PPUT1211579:G1HI6-1382-MONOMER; -. DR UniPathway; UPA00139; UER00337. DR Proteomes; UP000193308; Unassembled WGS sequence. DR Proteomes; UP000196082; Unassembled WGS sequence. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0004505; F:phenylalanine 4-monooxygenase activity; IEA:InterPro. DR GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:InterPro. 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 {ECO:0000256|ARBA:ARBA00023004}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000313|EMBL:ORL49141.1}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Phenylalanine catabolism {ECO:0000256|ARBA:ARBA00023232}. FT DOMAIN 1..262 FT /note="BH4_AAA_HYDROXYL_2" FT /evidence="ECO:0000259|PROSITE:PS51410" SQ SEQUENCE 262 AA; 30067 MW; 177EB13CFFF27AA2 CRC64; MKQTQYVARE PDAHGFIDYP QQEHAVWNTL ITRQLKVIEG RACQEYLDGI DQLKLPHDRI PQLGEVNKVL GATTGWQVAR VPALIPFQTF FELLASKRFP VATFIRTPEE LDYLQEPDIF HEIFGHCPLL TNPWFAEFTH TYGKLGLAAT KEQRVYLARL YWMTIEFGLM ETPQGRKIYG GGILSSPKET VYSLSGEPEH QAFDPIEAMR TPYRIDILQP LYFVLPNMKR LFDLAHEDIM GMVHKAMQLG LHAPKFPPKV AA //