ID PH4H_CAEEL Reviewed; 457 AA. AC P90925; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 03-APR-2007, entry version 54. DE Probable phenylalanine-4-hydroxylase 1 (EC 1.14.16.1) (PAH) (Phe-4- DE monooxygenase) (Biogenic amine synthesis protein 2). GN Name=pah-1; Synonyms=bas-2; ORFNames=K08F8.4; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for RT investigating biology."; RL Science 282:2012-2018(1998). RN [2] RP SEQUENCE REVISION. RG WormBase consortium; RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: L-phenylalanine + tetrahydrobiopterin + O(2) = CC L-tyrosine + 4a-hydroxytetrahydrobiopterin. CC -!- COFACTOR: Fe(2+) ion (By similarity). CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation; CC acetoacetate and fumarate from L-phenylalanine: step 1/6. CC -!- INTERACTION: CC P34371:C50C3.8; NbExp=1; IntAct=EBI-318020, EBI-315422; CC Q9U2U6:Y116A8C.26; NbExp=1; IntAct=EBI-318020, EBI-329992; CC Q9XX47:Y38H6C.14; NbExp=1; IntAct=EBI-318020, EBI-330289; CC -!- SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid CC hydroxylase family. CC -!- SIMILARITY: Contains 1 ACT domain. 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; Z66497; CAA91286.1; -; Genomic_DNA. DR PIR; T23494; T23494. DR UniGene; Cel.19578; -. DR HSSP; P04176; 1PHZ. DR DIP; DIP:25264N; -. DR IntAct; P90925; -. DR Ensembl; K08F8.4; Caenorhabditis elegans. DR KEGG; cel:K08F8.4; -. DR WormBase; WBGene00000240; pah-1. DR WormPep; K08F8.4; CE21050. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR InterPro; IPR001273; Aaa_hydroxylase. DR InterPro; IPR002912; ACT_bd. DR InterPro; IPR005961; Phe4hydrxlaseTet. DR Gene3D; G3DSA:1.10.800.10; Aaa_hydroxylase; 1. DR Pfam; PF01842; ACT; 1. DR Pfam; PF00351; Biopterin_H; 1. DR PRINTS; PR00372; FYWHYDRXLASE. DR ProDom; PD002559; Aaa_hydroxylase; 1. DR TIGRFAMs; TIGR01268; Phe4hydrox_tetr; 1. DR PROSITE; PS00367; BIOPTERIN_HYDROXYL; 1. KW Complete proteome; Iron; Metal-binding; Monooxygenase; Oxidoreductase; KW Phenylalanine catabolism. FT CHAIN 1 457 Probable phenylalanine-4-hydroxylase 1. FT /FTId=PRO_0000205551. FT DOMAIN 30 107 ACT. FT METAL 285 285 Iron (By similarity). FT METAL 290 290 Iron (By similarity). FT METAL 330 330 Iron (By similarity). SQ SEQUENCE 457 AA; 52129 MW; 68365836DFEC8D4F CRC64; MPPAGQDDLD FLKYAMESYV ADVNADIGKT TIVFTLREKA GALAETLKLF QAHDVNLSHI ESRPSKTHEG CYEVLVEFAE AEDHRKIEGV IEHFQQKAEK KVLVQDWNTK NKQNKDSVPW FPQKINDIDQ FANRILSYGA ELDADHPGFK DMTYRERRKF FADIAFNFKH GDKIPTITYT DEEIATWRTV YNELTVMYPK NACQEFNYIF PLLQQNCGFG PDRIPQLQDV SDFLKDCTGY TIRPVAGLLS SRDFLAGLAF RVFHSTQYIR HHSAPKYTPE PDICHELLGH VPLFADVEFA QFSQEIGLAS LGAPDDVIEK LATLYWFTIE FGICQQDGEK KAYGAGLLSS FGELQYALSD KPEVVDFDPA VCCVTKYPIT EYQPKYFLAE SFASAKNKLK SWAATINRPF QIRYNAYTQR VEILDKVAAL QRLARDIRSD ISTLEEALGK VNNLKMK //