ID   DODA_BETVU              Reviewed;         268 AA.
AC   Q70FG7;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=4,5-DOPA dioxygenase extradiol;
DE            EC=1.13.11.29;
GN   Name=DODA;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Bikores Monogerm;
RX   PubMed=14730069; DOI=10.1104/pp.103.031914;
RA   Christinet L., Burdet F.X., Zaiko M., Hinz U.G., Zryd J.-P.;
RT   "Characterization and functional identification of a novel plant 4,5-
RT   extradiol dioxygenase involved in betalain pigment biosynthesis in
RT   Portulaca grandiflora.";
RL   Plant Physiol. 134:265-274(2004).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX   PubMed=22270561; DOI=10.1007/s00425-012-1593-2;
RA   Gandia-Herrero F., Garcia-Carmona F.;
RT   "Characterization of recombinant Beta vulgaris 4,5-DOPA-extradiol-
RT   dioxygenase active in the biosynthesis of betalains.";
RL   Planta 236:91-100(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. Produces mainly (S)-
CC       betalamic acid. {ECO:0000269|PubMed:22270561}.
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:22270561};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=6.9 mM for L-dopa {ECO:0000269|PubMed:22270561};
CC         Vmax=1.2 umol/min/mg enzyme {ECO:0000269|PubMed:22270561};
CC         Note=kcat is 0.095 sec(-1) for L-dopa.;
CC       pH dependence:
CC         Optimum pH is 8.5. {ECO:0000269|PubMed:22270561};
CC   -!- PATHWAY: Pigment biosynthesis; betalain biosynthesis.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:22270561}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- MISCELLANEOUS: Supplementation with Fe(2+) in the reaction medium is
CC       not necessary to detect activity in contrast to the results found for
CC       the M. jalapa enzyme (AC B6F0W8) (PubMed:22270561).
CC       {ECO:0000305|PubMed:22270561}.
CC   -!- SIMILARITY: Belongs to the DODA-type extradiol aromatic ring-opening
CC       dioxygenase family. {ECO:0000305}.
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DR   EMBL; AJ583017; CAE47100.1; -; mRNA.
DR   AlphaFoldDB; Q70FG7; -.
DR   SMR; Q70FG7; -.
DR   BioCyc; MetaCyc:MON-19377; -.
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; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006725; P:cellular aromatic compound metabolic 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; Metal-binding; Oxidoreductase; Zinc.
FT   CHAIN           1..268
FT                   /note="4,5-DOPA dioxygenase extradiol"
FT                   /id="PRO_0000424076"
FT   BINDING         15
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         53
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         175
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         229
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   268 AA;  29616 MW;  D47C6D4466454C63 CRC64;
     MGSEDNIKET FFISHGTPMM AIDDSKPSKK FLESWREKIF SKKPKAILVI SAHWETDQPS
     VNVVDINDTI YDFRGFPARL YQFKYSAPGS PELANRIQDL LAGSGFKSVN TDKKRGLDHG
     AWVPLMLMYP EADIPVCQLS VQSHLDGTHH YKLGQALAPL KDEGVLIIGS GSATHPSNGT
     PPCSDGVAPW AAAFDSWLET ALTNGSYEEV NKYETKAPNW KLAHPWPEHF YPLHVAMGAA
     GENSKAELIH NSWDGGIMSY GSYKFTST