ID   DODA_MIRJA              Reviewed;         267 AA.
AC   B6F0W8;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=4,5-DOPA dioxygenase extradiol;
DE            Short=MjDOD;
DE            EC=1.13.11.29;
DE   AltName: Full=DOPA 4,5-dioxygenase;
GN   Name=DOD;
OS   Mirabilis jalapa (Garden four-o'clock).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Nyctaginaceae; Mirabilis.
OX   NCBI_TaxID=3538;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=19366710; DOI=10.1093/pcp/pcp053;
RA   Sasaki N., Abe Y., Goda Y., Adachi T., Kasahara K., Ozeki Y.;
RT   "Detection of DOPA 4,5-dioxygenase (DOD) activity using recombinant protein
RT   prepared from Escherichia coli cells harboring cDNA encoding DOD from
RT   Mirabilis jalapa.";
RL   Plant Cell Physiol. 50:1012-1016(2009).
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. Produces mainly (S)-
CC       betalamic acid. Required for the coloration of flowers.
CC       {ECO:0000269|PubMed:19366710}.
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:0000269|PubMed:19366710};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000269|PubMed:19366710};
CC   -!- PATHWAY: Pigment biosynthesis; betalain biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in petals. Not detected in leaves, stems
CC       and roots. {ECO:0000269|PubMed:19366710}.
CC   -!- MISCELLANEOUS: Requires ascorbic acid for iron to be in the proper
CC       redox state (PubMed:19366710). For the same enzyme from B. vulgaris (AC
CC       Q70FG7), presence of Fe(2+) is not necessary to detect activity.
CC       {ECO:0000305|PubMed:19366710}.
CC   -!- SIMILARITY: Belongs to the DODA-type extradiol aromatic ring-opening
CC       dioxygenase family. {ECO:0000305}.
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DR   EMBL; AB435372; BAG80686.1; -; mRNA.
DR   AlphaFoldDB; B6F0W8; -.
DR   SMR; B6F0W8; -.
DR   UniPathway; UPA00278; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046566; F:DOPA dioxygenase activity; IDA:UniProtKB.
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; IDA:UniProtKB.
DR   GO; GO:0046148; P:pigment biosynthetic process; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   Cytoplasm; Dioxygenase; Iron; Metal-binding; Oxidoreductase; Zinc.
FT   CHAIN           1..267
FT                   /note="4,5-DOPA dioxygenase extradiol"
FT                   /id="PRO_0000424075"
FT   BINDING         9
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         47
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         168
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         222
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   267 AA;  30171 MW;  07C7C561E3836DB6 CRC64;
     MKGTYYINHG DPLMYLKKHI KLRQFLEGWQ ENVVIEKPKS ILIISAHWDT NVPTVNFVEH
     CDTIHDFDDY PDPLYQIQYR APGAPNLAKK VEELLKESGM ECEIDTKRGL DHAAWFPLMF
     MYPEANIPIC ELSVQPSKDG IHHYNVGKAL SPLLQQGVLI IGSGGTVHPS DDTPHCPNGV
     APWAIEFDNW LEDALLSGRY EDVNNFKKLA PNWEISHPGQ EHLYPLHVAL GAAGKNPKTQ
     LIHRSWAANG VFGYSTYNFT PTTQKTD