ID DODA_AMAMU Reviewed; 228 AA. AC P87064; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 27-MAR-2024, entry version 78. DE RecName: Full=DOPA 4,5-dioxygenase; DE EC=1.14.99.-; GN Name=DODA; OS Amanita muscaria (Fly agaric) (Agaricus muscarius). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes; OC Agaricomycetidae; Agaricales; Pluteineae; Amanitaceae; Amanita. OX NCBI_TaxID=41956; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 90-103; 140-158; RP 178-188 AND 206-215. RC TISSUE=Cap; RX PubMed=9341673; DOI=10.1007/s004380050539; RA Hinz U.G., Fivaz J., Girod P.-A., Zryd J.-P.; RT "The gene coding for the DOPA dioxygenase involved in betalain biosynthesis RT in Amanita muscaria and its regulation."; RL Mol. Gen. Genet. 256:1-6(1997). RN [2] RP CHARACTERIZATION. RA Mueller L.A., Hinz U.G., Uze M., Sautter C., Zryd J.-P.; RT "Biochemical complementation of the betalain biosynthetic pathway in RT Portulaca grandiflora by a fungal 3,4-dihydroxyphenylalanine dioxygenase."; RL Planta 203:260-263(1997). RN [3] RP CHARACTERIZATION. RA Mueller L.A., Hinz U.G., Zryd J.-P.; RT "The formation of betalamic acid and muscaflavin by recombinant DOPA- RT dioxygenase from amanita."; RL Phytochemistry 44:567-569(1997). CC -!- FUNCTION: Extradiol dioxygenase that opens up the cyclic ring of DOPA CC between carbons 4 and 5 thus producing an unstable seco-DOPA that CC rearranges non-enzymatically to betalamic acid. Can also catalyze the CC formation of muscaflavin (a pigment found in the hygrocybe mushrooms CC family and of some amanita species only) by a 2,3-extradiol cleavage of CC DOPA. CC -!- PATHWAY: Pigment biosynthesis; betalain biosynthesis. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Expressed at high level in coloured cap tissue and CC at least 10 times lower level in the stipe. CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Pretty pigments - Issue 1 of CC September 2000; CC URL="https://web.expasy.org/spotlight/back_issues/001"; 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; Y12886; CAA73387.1; -; Genomic_DNA. DR AlphaFoldDB; P87064; -. DR SMR; P87064; -. DR KEGG; ag:CAA73387; -. DR UniPathway; UPA00278; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW. DR Gene3D; 3.30.70.1240; DOPA-like domains; 1. DR InterPro; IPR023389; DOPA-like_sf. DR InterPro; IPR014980; DOPA_dioxygen. DR PANTHER; PTHR36423; AFR070WP; 1. DR PANTHER; PTHR36423:SF2; DOPA 4,5-DIOXYGENASE; 1. DR Pfam; PF08883; DOPA_dioxygen; 1. DR SUPFAM; SSF143410; DOPA-like; 1. PE 1: Evidence at protein level; KW Cytoplasm; Dioxygenase; Direct protein sequencing; Oxidoreductase. FT CHAIN 1..228 FT /note="DOPA 4,5-dioxygenase" FT /id="PRO_0000079972" SQ SEQUENCE 228 AA; 26176 MW; C03CF0F055026E10 CRC64; MVPSFVVYSS WVNGRQRYIR QAFASILFYI IRDTTLSFPS HTTMSTKPET DLQTVLDSEI KEWHFHIYFH QNNAAEHQAA LELRDAVLRL RQDGAFVAVP LFRVNMDPMG PHPVGSYEIW VPSETFASVF SYLCMNRGRL SILVHPLTRE ELRDHEIRNA WIGPSFPLNL ANLPIKSDEI PLQYPSLKLG YSSTAHKMSL EERRKLGDDI EAVLRGEKEA ARAPHRDA //