DODA_AMAMU
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 25-MAY-2022, entry version 74.
DE RecName: Full=DOPA 4,5-dioxygenase;
DE EC=1.14.99.-;
GN Name=DODA;
OS Amanita muscaria (Fly agaric).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; 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";
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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; -; 1.
DR InterPro; IPR023389; DOPA-like_sf.
DR InterPro; IPR014980; DOPA_dioxygen.
DR PANTHER; PTHR36423; PTHR36423; 1.
DR Pfam; PF08883; DOPA_dioxygen; 1.
DR SUPFAM; SSF143410; SSF143410; 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