ID A0A365N254_GIBIN Unreviewed; 522 AA.
AC A0A365N254;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=Lignostilbene-alpha,beta-dioxygenase isozyme I {ECO:0008006|Google:ProtNLM};
GN ORFNames=FPRO05_13103 {ECO:0000313|EMBL:RBA14887.1};
OS Gibberella intermedia (Bulb rot disease fungus) (Fusarium proliferatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=948311 {ECO:0000313|EMBL:RBA14887.1, ECO:0000313|Proteomes:UP000251714};
RN [1] {ECO:0000313|EMBL:RBA14887.1, ECO:0000313|Proteomes:UP000251714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ITEM 2341 {ECO:0000313|EMBL:RBA14887.1,
RC ECO:0000313|Proteomes:UP000251714};
RA Almiman B.F., Shittu T.A., Muthumeenakshi S., Baroncelli R.,
RA Sreenivasaprasada S.;
RT "Genome sequence of the mycotoxigenic crop pathogen Fusarium proliferatum,
RT strain ITEM 2341 from Date Palm.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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:RBA14887.1}.
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DR EMBL; PKMI01000025; RBA14887.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A365N254; -.
DR Proteomes; UP000251714; 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 Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR604294-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR604294-1}.
FT BINDING 176
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 227
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 291
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 488
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ SEQUENCE 522 AA; 59070 MW; 7DB018C63DC5AA45 CRC64;
MSAPEEHHGL KSKWPQAFDL AGSNSPCRIE GEIGDLVVLG EIPPDIDGTF YRVMCDPFVP
PHPDNVPLDG DGHVSAFRIH NGRVDMKIKY VETERYKLER KAGKALFGLY RNPFTHHPCV
RAAVDSTANT NMVYWADRLL ALKESALPYE MHPDTLETLC YDPFGGQVKA KAFTAHPKID
PFSDELVVYG YEAKGLATRD IVIYSLDKNG IKHDEQWIES PWCAPIHDCV ITPNFIVLIL
WPFEASVERM KAGKQHWAWD YSLPATFIVV PRRKTSKIPA SWKQGECRVY HWKNCMNIHA
GSAWEEDNGK LYLETSRVHD NAFPFFPPVD GRMPAPDAKA DFVRWEIDLN APSGTQMADP
EIILDVPSEF PRIDERFMTK RNEYLFLNVF IPETSQGGTN IFHGLNGLAM HNHSTGETKW
FFAGKDSLVQ EPIFIPRTPN SPEGDGWVIA MLERRVANRS ELVVLDTREF ENPVAFIQLP
MHLKAQVHGN WIDSRTRAST EAIVRQIGEV KVSGRGALEP LA
//
