ID   DODA_PORGR              Reviewed;         271 AA.
AC   Q7XA48;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=4,5-DOPA dioxygenase extradiol;
DE            EC=1.13.11.29;
GN   Name=DODA;
OS   Portulaca grandiflora (Rose moss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Cactineae; Portulacaceae; Portulaca.
OX   NCBI_TaxID=3583;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
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).
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:0000269|PubMed:14730069}.
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:14730069};
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; Evidence={ECO:0000305};
CC   -!- PATHWAY: Pigment biosynthesis; betalain biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed only in colored petals and pigmented
CC       tissues, absent from green stems and leaves.
CC       {ECO:0000269|PubMed:14730069}.
CC   -!- DEVELOPMENTAL STAGE: Very high expression in immature colored petals,
CC       then decreases in mature colored petals. {ECO:0000269|PubMed:14730069}.
CC   -!- MISCELLANEOUS: In contrary to the fungal dioxygenase (AC P87064), this
CC       enzyme does not have a significant 2,3-ring-cleaving activity.
CC   -!- SIMILARITY: Belongs to the DODA-type extradiol aromatic ring-opening
CC       dioxygenase family. {ECO:0000305}.
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DR   EMBL; AJ580598; CAE45178.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7XA48; -.
DR   SMR; Q7XA48; -.
DR   BioCyc; MetaCyc:MON-12753; -.
DR   UniPathway; UPA00278; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   1: Evidence at protein level;
KW   Cytoplasm; Dioxygenase; Iron; Metal-binding; Oxidoreductase; Zinc.
FT   CHAIN           1..271
FT                   /note="4,5-DOPA dioxygenase extradiol"
FT                   /id="PRO_0000079973"
FT   BINDING         17
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         55
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         177
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         232
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   271 AA;  29920 MW;  6B1B0A6E60FF4DE1 CRC64;
     MGVGKEVSFK ESFFLSHGNP AMLADESFIA RNFLLGWKKN VFPVKPKSIL VVSAHWETDV
     PCVSAGQYPN VIYDFTEVPA SMFQMKYPAP GCPKLAKRVQ ELLIAGGFKS AKLDEERGFD
     HSSWVPLSMM CPEADIPVCQ LSVQPGLDAT HHFNVGRALA PLKGEGVLFI GSGGAVHPSD
     DTPHWFDGVA PWAAEFDQWL EDALLEGRYE DVNNYQTKAP EGWKLAHPIP EHFLPLHVAM
     GAGGEKSKAE LIYRTWDHGT LGYASYKFTS I