ID K9JXA1_AMAHP Unreviewed; 268 AA.
AC K9JXA1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=stizolobate synthase {ECO:0000256|ARBA:ARBA00013224};
DE EC=1.13.11.29 {ECO:0000256|ARBA:ARBA00013224};
GN Name=doda {ECO:0000313|EMBL:ADZ48644.1};
OS Amaranthus hypochondriacus (Prince-of-Wales feather) (Amaranthus hybridus
OS var. hypochondriacus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Amaranthaceae; Amaranthus.
OX NCBI_TaxID=28502 {ECO:0000313|EMBL:ADZ48644.1};
RN [1] {ECO:0000313|EMBL:ADZ48644.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:ADZ48644.1};
RA Casique G., Frier J.P., Gonzalez L.E.;
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADZ48644.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:ADZ48644.1};
RX PubMed=24896616;
RA Casique-Arroyo G., Martinez-Gallardo N., Gonzalez de la Vara L.,
RA Delano-Frier J.P.;
RT "Betacyanin Biosynthetic Genes and Enzymes Are Differentially Induced by
RT (a)biotic Stress in Amaranthus hypochondriacus.";
RL PLoS ONE 9:E99012-E99012(2014).
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:0000256|ARBA:ARBA00000466};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PATHWAY: Pigment biosynthesis; betalain biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005034}.
CC -!- SIMILARITY: Belongs to the DODA-type extradiol aromatic ring-opening
CC dioxygenase family. {ECO:0000256|ARBA:ARBA00007581}.
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DR EMBL; HQ889614; ADZ48644.1; -; mRNA.
DR AlphaFoldDB; K9JXA1; -.
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 Gene3D; 3.40.830.10; LigB-like; 1.
DR InterPro; IPR014436; Extradiol_dOase_DODA.
DR InterPro; IPR004183; Xdiol_dOase_suB.
DR PANTHER; PTHR30096:SF21; STIZOLOBATE SYNTHASE; 1.
DR PANTHER; PTHR30096; UNCHARACTERIZED; 1.
DR Pfam; PF02900; LigB; 1.
DR PIRSF; PIRSF006157; Doxgns_DODA; 1.
DR SUPFAM; SSF53213; LigB-like; 1.
PE 2: Evidence at transcript level;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000313|EMBL:ADZ48644.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 10..265
FT /note="Extradiol ring-cleavage dioxygenase class III enzyme
FT subunit B"
FT /evidence="ECO:0000259|Pfam:PF02900"
SQ SEQUENCE 268 AA; 30271 MW; 3A9CFBBBACF2DE88 CRC64;
MGSQEIIKET FFISHGTPRM TIEESKPARK FLESWRDKIY CKKPKAILVI SAHWETDFPS
VNAVDINDTI YDFYGFPAPM YQFKYPAPGS PDLAQRVQEL LTASGFKSVN VDKKRGLDHG
AWVPLMLMYP NADIPVCQLS VQSHLDGMYH YKLGRALAPL KEEGVLIIGS GSATHPSNST
PHYYDGVAPW AADFDQWLET ALTNGSYEEV NKCERKAPNW KLAHPWPEHF YPLHVAMGAA
GENWKAELIH NSWDHGTMSY GSYKFVSS
//
