ID W7M4T7_GIBM7 Unreviewed; 546 AA.
AC W7M4T7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Lignostilbene-alpha,beta-dioxygenase isozyme I {ECO:0008006|Google:ProtNLM};
GN ORFNames=FVEG_04345 {ECO:0000313|EMBL:EWG42580.1};
OS Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS fungus) (Fusarium verticillioides).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=334819 {ECO:0000313|EMBL:EWG42580.1, ECO:0000313|Proteomes:UP000009096};
RN [1] {ECO:0000313|EMBL:EWG42580.1, ECO:0000313|Proteomes:UP000009096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3125 / FGSC 7600 {ECO:0000313|Proteomes:UP000009096};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
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; DS022246; EWG42580.1; -; Genomic_DNA.
DR RefSeq; XP_018748771.1; XM_018892139.1.
DR AlphaFoldDB; W7M4T7; -.
DR EnsemblFungi; FVEG_04345T0; FVEG_04345T0; FVEG_04345.
DR GeneID; 30062421; -.
DR KEGG; fvr:FVEG_04345; -.
DR VEuPathDB; FungiDB:FVEG_04345; -.
DR eggNOG; KOG1285; Eukaryota.
DR HOGENOM; CLU_016472_6_2_1; -.
DR OMA; KTEECWY; -.
DR OrthoDB; 318119at2759; -.
DR Proteomes; UP000009096; Chromosome 4.
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 InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR PANTHER; PTHR10543; BETA-CAROTENE DIOXYGENASE; 1.
DR PANTHER; PTHR10543:SF37; CAROTENOID CLEAVAGE DIOXYGENASE 7, CHLOROPLASTIC; 1.
DR Pfam; PF03055; RPE65; 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 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:UP000009096}.
FT REGION 519..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 190
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 244
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 309
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 505
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ SEQUENCE 546 AA; 61562 MW; 3FFC28FC43FF0DC6 CRC64;
MAHIFDVAPL IDTGYVDGKK VGNQVKYPNT GAFSGFNKPF RLEGDIFDLE VSGTIPPEIN
GTFYRVQPDH RFPPVFEDDI HFNGDGNITA IRIQNGHADY KQRYVRTDRF LAETKERRSL
FGRYRNPFTD SELVKSVIRT SANTNITFWR GMLLASKEDG PPYAMDPVTL ETIGRYDFEG
QIQSPTMTAH PKFDPETGEM ICFAYEAGGN GNDGSRQIAV WTIDADGVKT EEAWYEAPFC
GMIHDCGISK NYIVLPMTPL KCNPDRLQKG GNHWAWDPKE DQWYGIVPRR NGKPEDIIWF
RSDNAFHGHV AGCYENEDGN IVFDLTVADG NVFFFFPPED TPAGTVAKRN RLNSPTKRWI
FDPKSPSGTR VQASEEWDTS GEFSRIDDRY VTKKYNHFWQ AKIDGSREYN AAKCGSPAGG
LFNCLAHYTW DERTEDIFWA GPCATFQEPS FIPKKNGGEG EGWLVALLNH LDVLRNDVVI
FDAQNLAAGP VATIHLPMKL RLGLHGNFVD QSDIEEWQAR RQPGGDVGPV RPAEKPLPWQ
SEADNI
//
