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Database: UniProt
Entry: N1S469_FUSC4
LinkDB: N1S469_FUSC4
Original site: N1S469_FUSC4 
ID   N1S469_FUSC4            Unreviewed;       588 AA.
AC   N1S469;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Carotenoid 9,10(9',10')-cleavage dioxygenase {ECO:0000313|EMBL:EMT69345.1};
GN   ORFNames=FOC4_g10001299 {ECO:0000313|EMBL:EMT69345.1};
OS   Fusarium oxysporum f. sp. cubense (strain race 4) (Panama disease fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=2502994 {ECO:0000313|EMBL:EMT69345.1, ECO:0000313|Proteomes:UP000016929};
RN   [1] {ECO:0000313|Proteomes:UP000016929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RA   Fang X., Huang J.;
RT   "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT   banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000016929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RX   PubMed=24743270;
RA   Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA   Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA   Fang X., Peng M., Huang J.;
RT   "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT   oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL   PLoS ONE 9:E95543-E95543(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O2 + piceatannol = 3,4-dihydroxybenzaldehyde + 3,5-
CC         dihydroxybenzaldehyde; Xref=Rhea:RHEA:73815, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:28814, ChEBI:CHEBI:50204, ChEBI:CHEBI:50205;
CC         Evidence={ECO:0000256|ARBA:ARBA00043690};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73816;
CC         Evidence={ECO:0000256|ARBA:ARBA00043690};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O2 + trans-resveratrol = 3,5-dihydroxybenzaldehyde + 4-
CC         hydroxybenzaldehyde; Xref=Rhea:RHEA:73735, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:17597, ChEBI:CHEBI:45713, ChEBI:CHEBI:50204;
CC         Evidence={ECO:0000256|ARBA:ARBA00043818};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73736;
CC         Evidence={ECO:0000256|ARBA:ARBA00043818};
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}.
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DR   EMBL; KB726397; EMT69345.1; -; Genomic_DNA.
DR   AlphaFoldDB; N1S469; -.
DR   STRING; 1229665.N1S469; -.
DR   HOGENOM; CLU_016472_6_2_1; -.
DR   Proteomes; UP000016929; Unassembled WGS sequence.
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; BETA-CAROTENE DIOXYGENASE; 1.
DR   PANTHER; PTHR10543:SF37; CAROTENOID CLEAVAGE DIOXYGENASE 7, CHLOROPLASTIC; 1.
DR   Pfam; PF03055; RPE65; 1.
PE   3: Inferred from homology;
KW   Dioxygenase {ECO:0000313|EMBL:EMT69345.1};
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:0000313|EMBL:EMT69345.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016929}.
FT   BINDING         218
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         269
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         336
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         517
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ   SEQUENCE   588 AA;  66695 MW;  E0E83E2BE0D01DED CRC64;
     MATNKEVQQS LMHELKDIGE LKLYHSEDTA TIESRKGNLG LAEKFQFEQS LPGFSTGIDI
     PGRFDAELAS CVVHGTMPSE IDGTFYRIVC DQIWARRNKV DPNNPRDIWI NGDGAVDAWR
     ISNGVVDFKQ KYVRTPRFVF ERIAREPLFG SYRNIFSGDP RVKDEVQSPG NVHVHFFREK
     LLIPKDDSPP ILMDPDTLET FGLTDFDGQL NSMSFTSHPK VDYSTGELLG FGMEASGIGS
     NDLVYYLFDK DGVKQEECWV KTPFVGWSHD FAFSDNWILF GLLPYETNVD FMRNSGEAQF
     RFNRFLPLTF GLLPRRNPKP EDIKWFYGPK NHGWVHFSNH FEENGKFYFD LFFTDGDGLS
     SFVDAHPELG PSNPNRMVGK LVRFTIDPKA ESNKLDLPQV LSHVNGEMAR IDDRYVGKPY
     RHTWGVIWGS GLWDGIVHVD THTGVSKVWQ GGDTVMVHEP CFVPRSKEAP EGDGHLVCVA
     RDKRREITYL IILDAQNITA GPVCLVEMPL RLHVAAHGNW VNAWDRSVRK PLVDYSGATP
     ELLAKFSTGA PKPYDEVWGK PVVTKYPGRW PFPVHEEAKG YPNGIDTD
//
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