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Database: UniProt
Entry: A0A1R3J4C0_COCAP
LinkDB: A0A1R3J4C0_COCAP
Original site: A0A1R3J4C0_COCAP 
ID   A0A1R3J4C0_COCAP        Unreviewed;       356 AA.
AC   A0A1R3J4C0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=anthocyanidin synthase {ECO:0000256|ARBA:ARBA00039062};
DE            EC=1.14.20.4 {ECO:0000256|ARBA:ARBA00039062};
GN   ORFNames=CCACVL1_07703 {ECO:0000313|EMBL:OMO89673.1};
OS   Corchorus capsularis (Jute).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX   NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO89673.1, ECO:0000313|Proteomes:UP000188268};
RN   [1] {ECO:0000313|EMBL:OMO89673.1, ECO:0000313|Proteomes:UP000188268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC   TISSUE=Whole seedling {ECO:0000313|EMBL:OMO89673.1};
RA   Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA   Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA   Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT   "Corchorus capsularis genome sequencing.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC         Evidence={ECO:0000256|ARBA:ARBA00001961};
CC   -!- PATHWAY: Pigment biosynthesis; anthocyanin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004935}.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00008056, ECO:0000256|RuleBase:RU003682}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OMO89673.1}.
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DR   EMBL; AWWV01008631; OMO89673.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R3J4C0; -.
DR   STRING; 210143.A0A1R3J4C0; -.
DR   EnsemblPlants; OMO89673; OMO89673; CCACVL1_07703.
DR   Gramene; OMO89673; OMO89673; CCACVL1_07703.
DR   OMA; AGMRILH; -.
DR   OrthoDB; 1057251at2759; -.
DR   Proteomes; UP000188268; Unassembled WGS sequence.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR026992; DIOX_N.
DR   InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR   InterPro; IPR027443; IPNS-like_sf.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   PANTHER; PTHR47991:SF200; ANTHOCYANIDIN SYNTHASE; 1.
DR   PANTHER; PTHR47991; OXOGLUTARATE/IRON-DEPENDENT DIOXYGENASE; 1.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   Pfam; PF14226; DIOX_N; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   3: Inferred from homology;
KW   Dioxygenase {ECO:0000313|EMBL:OMO89673.1};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU003682};
KW   Metal-binding {ECO:0000256|RuleBase:RU003682};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003682};
KW   Reference proteome {ECO:0000313|Proteomes:UP000188268}.
FT   DOMAIN          212..311
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   356 AA;  40438 MW;  5CEA7CD49F8D1A72 CRC64;
     MVTSVAPSPR VESLSSSGIQ SIPKEYIRPQ EELTSIGNVF EEEKKEEGPQ VPTIDLKEIE
     SEDPEVREKC RQELKKAAMD WGVMHVVNHG ISDELIQRVK KAGQKFCELP IEEKEKYAND
     QASGKIQGYG SKLANNASGQ LEWEDYFFHL IFPEDKRDLS IWPKIPRDYT EVTSEYAREL
     RGLASKILSA LSICLGLEEG RLEKEVGGME ELLLQMKINY YPKCPQPELA LGVEAHTDVS
     ALTFILHNMV PGLQLFYEGK WVTAKCVPNS IIMHIGDTIE ILSNGKYKSI LHRGLVNKEK
     VRISWAVFCE PPKEKIILKP LPELVSETEP PLFPPRTFDQ HIQHKLFRKT QDGLSN
//
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