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Database: UniProt
Entry: V5FJS7_BYSSN
LinkDB: V5FJS7_BYSSN
Original site: V5FJS7_BYSSN 
ID   V5FJS7_BYSSN            Unreviewed;       557 AA.
AC   V5FJS7;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Carotenoid cleavage dioxygenase, putative {ECO:0000313|EMBL:GAD92008.1};
GN   ORFNames=PVAR5_0594 {ECO:0000313|EMBL:GAD92008.1};
OS   Byssochlamys spectabilis (strain No. 5 / NBRC 109023) (Paecilomyces
OS   variotii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX   NCBI_TaxID=1356009 {ECO:0000313|EMBL:GAD92008.1, ECO:0000313|Proteomes:UP000018001};
RN   [1] {ECO:0000313|Proteomes:UP000018001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=No. 5 / NBRC 109023 {ECO:0000313|Proteomes:UP000018001};
RX   PubMed=24407650; DOI=10.1128/genomeA.01162-13;
RA   Oka T., Ekino K., Fukuda K., Nomura Y.;
RT   "Draft genome sequence of the formaldehyde-resistant fungus Byssochlamys
RT   spectabilis No. 5 (anamorph Paecilomyces variotii No. 5) (NBRC109023).";
RL   Genome Announc. 2:E0116213-E0116213(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}.
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:GAD92008.1}.
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DR   EMBL; BAUL01000013; GAD92008.1; -; Genomic_DNA.
DR   AlphaFoldDB; V5FJS7; -.
DR   eggNOG; KOG1285; Eukaryota.
DR   HOGENOM; CLU_016472_6_2_1; -.
DR   InParanoid; V5FJS7; -.
DR   OrthoDB; 318119at2759; -.
DR   Proteomes; UP000018001; 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   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   Dioxygenase {ECO:0000313|EMBL:GAD92008.1};
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:GAD92008.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018001}.
FT   REGION          526..557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        542..557
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         192
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         246
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         311
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         509
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ   SEQUENCE   557 AA;  63166 MW;  13464326B57585CA CRC64;
     MAHIFELAEA LSSQPAYVDG VKCDDRIKYP ATEVFQGFNR PSRIEGDVEY LEVTGVIPDD
     IDGTFFRIQP DHRFPPLYES DIHFNGDGNV TAIRVQNGVA SFKQRYVHTD RYVQESKHGK
     ALFGKYRNPY TDNEAVKGVI RTTANTNIFF WRGMLLATKE DGPPYAMDPE TLETIGRYDF
     EGQVLAPTFT AHPKFDLKTG EMVCYGYEAG GNGNDGSNDI VVYTINSEGV KTEECWYKAP
     FCGIIHDCGI TDNWVVLPMT PLKCDPDRLA KGENHWAWDP KEDQWYGIVP RRGGKPEDIK
     WFRSKNAFQG HTVSSYETED EKIVFDLTIA DGNVFFFFPP VDTPQGTVLQ RNKLQNKTTR
     WVFDPKAPSN SWVDPAEEVD TFSGEFSRVD DRFVTTKYNH YWQAVIDGLK PYDFQRCGSP
     AGGLFNTLGH FTWDRSVMET FWAGPCQTFQ EPAFIPRAGS TEEGDGYIIA LLNHLDVLRN
     DVCIFDAQKI SQGPVAVIHL PFKLRLGLHG NFVEMREIKD WKEKRERELG PVKPASAPLP
     WQQKEGASQP NGLNGHH
//
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