ID   DOD1W_BETVU             Reviewed;         275 AA.
AC   I3PFJ9;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2012, sequence version 1.
DT   03-AUG-2022, entry version 26.
DE   RecName: Full=4,5-DOPA dioxygenase extradiol 1 {ECO:0000303|PubMed:22660548};
DE            EC=1.13.11.29 {ECO:0000305};
GN   Name=DODA1 {ECO:0000303|PubMed:22660548};
OS   Beta vulgaris (Sugar beet).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Betoideae; Beta.
OX   NCBI_TaxID=161934 {ECO:0000312|EMBL:AET43293.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=cv. W357B;
RX   PubMed=22660548; DOI=10.1038/ng.2297;
RA   Hatlestad G.J., Sunnadeniya R.M., Akhavan N.A., Gonzalez A., Goldman I.L.,
RA   McGrath J.M., Lloyd A.M.;
RT   "The beet R locus encodes a new cytochrome P450 required for red betalain
RT   production.";
RL   Nat. Genet. 44:816-820(2012).
CC   -!- FUNCTION: Opens the cyclic ring of dihydroxy-phenylalanine (DOPA)
CC       between carbons 4 and 5, thus producing an unstable seco-DOPA that
CC       rearranges nonenzymatically to betalamic acid.
CC       {ECO:0000305|PubMed:22660548}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-dopa + O2 = 4-(L-alanin-3-yl)-2-hydroxy-cis,cis-muconate 6-
CC         semialdehyde + H(+); Xref=Rhea:RHEA:21220, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57504, ChEBI:CHEBI:57639;
CC         EC=1.13.11.29; Evidence={ECO:0000305};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Pigment biosynthesis; betalain biosynthesis. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the DODA-type extradiol aromatic ring-opening
CC       dioxygenase family. {ECO:0000305}.
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DR   EMBL; HQ656027; AET43293.1; -; mRNA.
DR   AlphaFoldDB; I3PFJ9; -.
DR   SMR; I3PFJ9; -.
DR   UniPathway; UPA00278; -.
DR   GO; GO:0008198; F:ferrous iron binding; IEA:InterPro.
DR   GO; GO:0050297; F:stizolobate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006725; P:cellular aromatic compound metabolic process; IEA:InterPro.
DR   CDD; cd07363; 45_DOPA_Dioxygenase; 1.
DR   InterPro; IPR014436; Extradiol_dOase_DODA.
DR   InterPro; IPR004183; Xdiol_dOase_suB.
DR   Pfam; PF02900; LigB; 1.
DR   PIRSF; PIRSF006157; Doxgns_DODA; 1.
PE   2: Evidence at transcript level;
KW   Dioxygenase; Metal-binding; Oxidoreductase; Zinc.
FT   CHAIN           1..275
FT                   /note="4,5-DOPA dioxygenase extradiol 1"
FT                   /id="PRO_0000431982"
FT   BINDING         22
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         182
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         236
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   275 AA;  31161 MW;  04B549828DFC17E7 CRC64;
     MKMMNGEDAN DQMIKESFFI THGNPILTVE DTHPLRPFFE TWREKIFSKK PKAILIISGH
     WETVKPTVNA VHINDTIHDF DDYPAAMYQF KYPAPGEPEL ARKVEEILKK SGFETAETDQ
     KRGLDHGAWV PLMLMYPEAD IPVCQLSVQP HLDGTYHYNL GRALAPLKND GVLIIGSGSA
     THPLDETPHY FDGVAPWAAA FDSWLRKALI NGRFEEVNIY ESKAPNWKLA HPFPEHFYPL
     HVVLGAAGEK WKAELIHSSW DHGTLCHGSY KFTSA