ID PH4H_DROME STANDARD; PRT; 453 AA. AC P17276; DT 01-AUG-1990 (Rel. 15, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE HENNA PROTEIN [INCLUDES: PHENYLALANINE-4-HYDROXYLASE (EC 1.14.16.1) DE (PAH) (PHE-4-MONOOXYGENASE); TRYPTOPHAN 5-MONOOXYGENASE (EC 1.14.16.4) DE (TRH) (TRYPTOPHAN 5-HYDROXYLASE)]. GN HN OR TPH OR PAH. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CANTON-S, AND OREGON-R; TISSUE=EMBRYO, AND HEAD; RX MEDLINE; 92156168. RA NECKAMEYER W.S., WHITE K.; RT "A single locus encodes both phenylalanine hydroxylase and tryptophan RT hydroxylase activities in Drosophila."; RL J. Biol. Chem. 267:4199-4206(1992). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE; 91033030. RA MORALES G., REQUENA J.M., JIMENEZ-RUIZ A., LOPEZ M.C., UGARTE M., RA ALONSO C.; RT "Sequence and expression of the Drosophila phenylalanine hydroxylase RT mRNA."; RL Gene 93:213-219(1990). CC -!- CATALYTIC ACTIVITY: L-PHENYLALANINE + TETRAHYDROBIOPTERIN + CC O(2) = L-TYROSINE + DIHYDROBIOPTERIN + H(2)O. CC -!- CATALYTIC ACTIVITY: L-TRYPTOPHAN + TETRAHYDROPTERIDINE + O(2) = CC 5-HYDROXY-L-TRYPTOPHAN + DIHYDROPTERIDINE + H(2)O. CC -!- COFACTOR: FERROUS ION. CC -!- ENZYME REGULATION: N-TERMINAL REGION OF PAH IS THOUGHT TO CONTAIN CC ALLOSTERIC BINDING SITES FOR PHENYLALANINE AND TO CONSTITUTE AN CC "INHIBITORY" DOMAIN THAT REGULATES THE ACTIVITY OF A CATALYTIC CC DOMAIN IN THE C-TERMINAL PORTION OF THE MOLECULE. CC -!- PATHWAY: RATE-LIMITING STEP IN PHENYLALANINE CATABOLISM. CC -!- TISSUE SPECIFICITY: PHENYLALANINE HYDROLASE ACTIVITY IS FOUND IN CC YOLK GRANULES OF EMBRYOS, AND FEMALE ABDOMEN AND FAT BODY TISSUES. CC TRYPTOPHAN HYDROXYLASE IS EXPRESSED IN SEROTONERGIC NEURONS. CC BOTH ENZYMES ARE PRESENT IN CUTICULAR TISSUES. CC -!- MISCELLANEOUS: IN DROSOPHILA, THE 2 ENZYMES, PAH AND TRH ARE FOUND CC TO BE ENCODED BY THE SAME GENE. PREFERENCE FOR THE SUBSTRATE IS CC PROBABLY DUE TO POST-TRANSLATIONAL MODIFICATIONS SUCH AS CC PHOSPHORYLATION, OR BY CHANGES IN THE N-TERMINAL REGULATORY CC DOMAIN. 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; M81833; -; NOT_ANNOTATED_CDS. DR EMBL; M32802; AAA69513.1; -. DR PIR; JQ0766; JQ0766. DR PIR; A42271; A42271. DR HSSP; P04177; 1TOH. DR FLYBASE; FBgn0001208; Hn. DR PFAM; PF00351; biopterin_H; 1. DR PROSITE; PS00367; BIOPTERIN_HYDROXYL; 1. KW Oxidoreductase; Monooxygenase; Phenylalanine catabolism; Iron; KW Serotonin biosynthesis; Phosphorylation. FT MOD_RES 272 272 PHOSPHORYLATION (BY CAM-KINASE II) FT (BY SIMILARITY). FT METAL 284 284 IRON (BY SIMILARITY). FT METAL 289 289 IRON (BY SIMILARITY). FT METAL 329 329 IRON (BY SIMILARITY). FT CONFLICT 28 28 E -> A (IN REF. 2). FT CONFLICT 39 47 KDSSLSSGA -> RIRRCPAEL (IN REF. 2). FT CONFLICT 55 56 FK -> LR (IN REF. 2). FT CONFLICT 63 71 VHIESRSSL -> CILSRILAPWF (IN REF. 2). FT CONFLICT 74 114 PGYEFFVEADGKSGALGKAIEDVKEQCSYFNIISRDYKDNA FT -> SSCFWRRMENRSLGKSHRGCEGAMLATLTSSCRELQGV FT MP (IN REF. 2). FT CONFLICT 154 154 R -> A (IN REF. 2). FT CONFLICT 164 164 A -> G (IN REF. 2). FT CONFLICT 171 171 E -> Q (IN REF. 2). FT CONFLICT 264 264 S -> C (IN REF. 2). FT CONFLICT 297 297 A -> S (IN REF. 2). FT CONFLICT 333 335 CRQ -> LAK (IN REF. 2). FT CONFLICT 370 370 V -> S (IN REF. 2). FT CONFLICT 449 453 NCASE -> KLRV (IN REF. 2). SQ SEQUENCE 453 AA; 51682 MW; 758F7618 CRC32; MYQRQVSFDK PTRVEDSAYI VEGVDIKEAR NTCLLFSPKD SSLSSGALAN ILAIFKKHDI NLVHIESRSS LRVPGYEFFV EADGKSGALG KAIEDVKEQC SYFNIISRDY KDNATAVPWF PRRIRDLDRF ANQILSYGSE LDADHPGFTD PEYRKRRKYF ADIAYNYKHG EPLPHVDYTK EEIETWGIIF RNLTKLYKTH ACREYNHVFP LLVDNCGFRE DNIPQLEDVS NFLRDCTGFT LRPVAGLLSS RDFLAGLAFR VFHSTQYIRH PSKPMYTPEP DVCHELMGHV PLFADPAFAQ FSQEIGLASL GAPDDYIEKL STIFWFTVEY GLCRQEGELK AYGAGLLSSY GELEYCLTDK PQLKDFEPEV TGVTKYPITQ FQPLYYVADS FETAKEKTIK FANSIPRPFG VRYNAYTQSV EVLDSKPQIS NLMDNINSEF QILQNAVANC ASE //