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Database: UniProt
Entry: A0A498ITC5_MALDO
LinkDB: A0A498ITC5_MALDO
Original site: A0A498ITC5_MALDO 
ID   A0A498ITC5_MALDO        Unreviewed;       615 AA.
AC   A0A498ITC5;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=9-cis-epoxycarotenoid dioxygenase {ECO:0000256|ARBA:ARBA00039007};
DE            EC=1.13.11.51 {ECO:0000256|ARBA:ARBA00039007};
GN   ORFNames=DVH24_021792 {ECO:0000313|EMBL:RXH86519.1};
OS   Malus domestica (Apple) (Pyrus malus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX   NCBI_TaxID=3750 {ECO:0000313|EMBL:RXH86519.1, ECO:0000313|Proteomes:UP000290289};
RN   [1] {ECO:0000313|EMBL:RXH86519.1, ECO:0000313|Proteomes:UP000290289}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC   TISSUE=Young leaf {ECO:0000313|EMBL:RXH86519.1};
RA   Hu J.;
RT   "A high-quality apple genome assembly.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=9'-cis-neoxanthin + O2 = (3S,5R,6R)-3,5-dihydroxy-6,7-
CC         didehydro-5,6-dihydro-12'-apo-beta-caroten-12'-al + 2-cis,4-trans-
CC         xanthoxin; Xref=Rhea:RHEA:19677, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:32304, ChEBI:CHEBI:34596, ChEBI:CHEBI:35306;
CC         EC=1.13.11.51; Evidence={ECO:0000256|ARBA:ARBA00036784};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=9-cis-violaxanthin + O2 = (3S,5R,6S)-5,6-epoxy-3-hydroxy-5,6-
CC         dihydro-12'-apo-beta-caroten-12'-al + 2-cis,4-trans-xanthoxin;
CC         Xref=Rhea:RHEA:16541, ChEBI:CHEBI:15379, ChEBI:CHEBI:32304,
CC         ChEBI:CHEBI:34597, ChEBI:CHEBI:35305; EC=1.13.11.51;
CC         Evidence={ECO:0000256|ARBA:ARBA00035929};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 9-cis-epoxycarotenoid + O2 = 2-cis,4-trans-xanthoxin + a
CC         12'-apo-carotenal; Xref=Rhea:RHEA:23328, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:32304, ChEBI:CHEBI:51972, ChEBI:CHEBI:51973;
CC         EC=1.13.11.51; Evidence={ECO:0000256|ARBA:ARBA00036011};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|PIRSR:PIRSR604294-1};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR604294-1};
CC   -!- SIMILARITY: Belongs to the carotenoid oxygenase family.
CC       {ECO:0000256|ARBA:ARBA00006787}.
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:RXH86519.1}.
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DR   EMBL; RDQH01000336; RXH86519.1; -; Genomic_DNA.
DR   RefSeq; XP_008382970.1; XM_008384748.2.
DR   AlphaFoldDB; A0A498ITC5; -.
DR   STRING; 3750.A0A498ITC5; -.
DR   EnsemblPlants; mRNA:MD10G0164700; CDS:MD10G0164700.1; MD10G0164700.
DR   GeneID; 103445724; -.
DR   Gramene; mRNA:MD10G0164700; CDS:MD10G0164700.1; MD10G0164700.
DR   KEGG; mdm:103445724; -.
DR   OrthoDB; 318119at2759; -.
DR   Proteomes; UP000290289; Chromosome 10.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:InterPro.
DR   InterPro; IPR004294; Carotenoid_Oase.
DR   PANTHER; PTHR10543:SF26; 9-CIS-EPOXYCAROTENOID DIOXYGENASE NCED3, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR10543; BETA-CAROTENE DIOXYGENASE; 1.
DR   Pfam; PF03055; RPE65; 1.
PE   3: Inferred from homology;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR604294-1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR604294-1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000290289}.
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          65..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         315
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         364
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         429
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         602
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ   SEQUENCE   615 AA;  68329 MW;  6700C0A2F5820F1E CRC64;
     MPSTATVAAT GTRVKPVTST TRHRRLSSLN SSNSFRNQLG FSPSSSSIFK SKTISCSLQT
     PSLVQIPKHS PTYQRPSTST STKIPRENKT QKSPTSSKPV PQQWNLLQRA ASMALDAMES
     ALLSKEKQHP LPKTSDPKVQ IAGNFAPVPE HPVEHYLPVT GKIPDSIQGV YVRNGANPLH
     EPVAGHHLFD GDGMVHALQF KDGTASYACR FTETSRISQE RDLGRPLFPK AIGELHGHSG
     IARLLLFYAR GMFGLVDPTH GIGVANAGLV YHNGHLLAMS EDDLPYHVQI TETGDLKTVG
     RYDFEGQLKS TMIAHPKVDP ATGDLFALSY DVVQRPYLKY FKFSPNGEKS PDIEINLEQP
     TMMHDFAITE RHVVIPDQQV VFKLQEMIGG GSPVIYDKNK MSRFGILDKN AKDASGIRWV
     DCPDCFCFHL WNAWEEPETD EIVVIGSCMT PPDSIFNECD ENLESVLSEI RLNLKTGKST
     RRRICSENLN LEAGMVNRNK LGRKTQSAYL ALAEPWPKVS GFAKVDLSTG EVKKHIYGDE
     KYGGEPLFLP RDPNSEDEDD GYILAFVHDE KKWKSELQIV NTMDLKVEAT IQLPSRVPYG
     FHGTFISAKD LKKQA
//
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