ID PH4H_CAEEL STANDARD; PRT; 466 AA. AC P90925; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE PUTATIVE PHENYLALANINE-4-HYDROXYLASE (EC 1.14.16.1) (PAH) (PHE-4- DE MONOOXYGENASE). GN K08F8.4. OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Secernentea; Rhabditia; Rhabditida; OC Rhabditina; Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=BRISTOL N2; RA SMYE R.; RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: L-PHENYLALANINE + TETRAHYDROBIOPTERIN + CC O(2) = L-TYROSINE + DIHYDROBIOPTERIN + H(2)O. CC -!- COFACTOR: FERROUS ION (BY SIMILARITY). CC -!- PATHWAY: RATE-LIMITING STEP IN PHENYLALANINE CATABOLISM. CC -!- SIMILARITY: BELONGS TO THE BIOPTERIN-DEPENDENT AROMATIC AMINO ACID CC HYDROXYLASES FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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; E284944; -. DR HSSP; P04177; 1TOH. DR WORMPEP; K08F8.4; CE11934. DR PFAM; PF00351; biopterin_H; 1. DR PROSITE; PS00367; BIOPTERIN_HYDROXYL; 1. KW Hypothetical protein; Oxidoreductase; Monooxygenase; KW Phenylalanine catabolism; Iron. FT METAL 285 285 IRON (BY SIMILARITY). FT METAL 290 290 IRON (BY SIMILARITY). FT METAL 330 330 IRON (BY SIMILARITY). SQ SEQUENCE 466 AA; 53239 MW; 13553736 CRC32; 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 SFASAKNKLN FNCNLDNFRS WAATINRPFQ IRYNAYTQRV EILDKVAALQ RLARDIRSDI STLEEALGKV NNLKMK //