ID A0A428Q0S3_9HYPO Unreviewed; 522 AA.
AC A0A428Q0S3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Lignostilbene-alpha,beta-dioxygenase isozyme I {ECO:0008006|Google:ProtNLM};
GN ORFNames=CEP53_005992 {ECO:0000313|EMBL:RSL58886.1};
OS Fusarium sp. AF-6.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=1325737 {ECO:0000313|EMBL:RSL58886.1, ECO:0000313|Proteomes:UP000287544};
RN [1] {ECO:0000313|EMBL:RSL58886.1, ECO:0000313|Proteomes:UP000287544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL62590 {ECO:0000313|EMBL:RSL58886.1,
RC ECO:0000313|Proteomes:UP000287544};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL Submitted (JUN-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:RSL58886.1}.
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DR EMBL; NKCJ01000112; RSL58886.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A428Q0S3; -.
DR STRING; 1325737.A0A428Q0S3; -.
DR Proteomes; UP000287544; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000287544}.
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 299
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; 59103 MW; C69AC92F7375D8F1 CRC64;
MTTTFEYENL KSKWPTALDL AGSNLPCRIE GEVGDLVVLG EIPSAIDGTF YRVMCDPFVP
PDPNNVPIDG DGNISAFRIR NGRVDMKIKY VETERYKLER KANKALFGLY RNPFTHHPCV
RAAVDSTANT NLVYWANHLL ALKEVALPYS IDPDTVETRG YDPFEGQVKS KTFTAHPKVD
PYTDELVVFG YEAKGLATRD VVIYALDRDG KKRDEQWIQA PWCAFIHDCA LTPNWIILVL
WPFEANMTRL KAKKQHWAWD YNLPATFIAV PRRKTTPLPT GWKEGEHRVY SWRNCMPIHT
AGAWEGQDGK LYFESSRVHD NAFPFFPPDD GRMPAKDAKA DFVRWEIDLS QPSGSVVPDP
LIVLDIPSEF PRVDERFLTH DHEFVFLNVF IPENSDGEAN IFHGLNGLAM HSHKTGQTRW
FYASDDSLVQ EPAFIPRTPD APEGDGWIVA MVERRAAGRS DLVILDTRNF EKPIAIAQLP
LHVKAQIHGN WVDAAVLPEW KSLVREAPVG EISNKGALEP LD
//