ID PH4H$DROME STANDARD; PRT; 453 AA. AC P17276; DT 01-AUG-1990 (REL. 15, CREATED) DT 01-AUG-1990 (REL. 15, LAST SEQUENCE UPDATE) DT 01-AUG-1990 (REL. 15, LAST ANNOTATION UPDATE) DE PHENYLALANINE-4-HYDROXYLASE (EC 1.14.16.1) (PAH) (PHE-4-MONOOXYGENASE) DE (GENE NAME: PAH). OS FRUIT FLY (DROSOPHILA MELANOGASTER). OC EUKARYOTA; METAZOA; ARTHROPODA; INSECTA. RN [1] (SEQUENCE FROM N.A.) RA MORALES G., REQUENA J.M., JIMENEZ-RUIZ A., LOPEZ M.C., UGARTE M., RA ALONSO C.; RL SUBMITTED (MAY-1990) TO EMBL/GENBANK DATA BANKS. CC -!- CATALYTIC ACTIVITY: L-PHENYLALANINE + TETRAHYDROBIOPTERIN + CC O(2) = L-TYROSINE + DIHYDROBIOPTERIN + H(2)O. CC -!- PATHWAY: RATE-LIMITING STEP IN PHENYLALANINE CATABOLISM. CC -!- COFACTOR: THIS ENZYME REQUIRES A 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 -!- SIMILARITY: TO OTHER BIOPTERIN-DEPENDENT AROMATIC AMINO ACID CC HYDROXYLASES. 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; M23802; M23802. KW OXIDOREDUCTASE; MONOOXYGENASE; PHENYLALANINE CATABOLISM; IRON. SQ SEQUENCE 453 AA; 51907 MW; 1080701 CN; MYQRQVSFDK PTRVEDSAYI VEGVDIKAAR NTCLLFSPRI RRCPAELLAN ILAILRKHDI NLCILSRILA PWFRVSSCFW RRMENRSLGK SHRGCEGAML ATLTSSCREL QGVMPTAVPW FPRRIRDLDR FANQILSYGS ELDADHPGFT DPEYAKRRKY FADIGYNYKH GQPLPHVDYT KEEIETWGII FRNLTKLYKT HACREYNHVF PLLVDNCGFR EDNIPQLEDV SNFLRDCTGF TLRPVAGLLS SRDFLAGLAF RVFHCTQYIR HPSKPMYTPE PDVCHELMGH VPLFADPSFA QFSQEIGLAS LGAPDDYIEK LSTIFWFTVE YGLLAKEGEL KAYGAGLLSS YGELEYCLTD KPQLKDFEPE STGVTKYPIT QFQPLYYVAD SFETAKEKTI KFANSIPRPF GVRYNAYTQS VEVLDSKPQI SNLMDNINSE FQILQNAVAK LRV //