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Database: UniProt
Entry: A0A178EG89_9PLEO
LinkDB: A0A178EG89_9PLEO
Original site: A0A178EG89_9PLEO 
ID   A0A178EG89_9PLEO        Unreviewed;       489 AA.
AC   A0A178EG89;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Carotenoid oxygenase {ECO:0000313|EMBL:OAL54682.1};
GN   ORFNames=IQ07DRAFT_500358 {ECO:0000313|EMBL:OAL54682.1};
OS   Pyrenochaeta sp. DS3sAY3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC   Pyrenochaeta.
OX   NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL54682.1, ECO:0000313|Proteomes:UP000077535};
RN   [1] {ECO:0000313|EMBL:OAL54682.1, ECO:0000313|Proteomes:UP000077535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL54682.1,
RC   ECO:0000313|Proteomes:UP000077535};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) 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}.
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DR   EMBL; KV441638; OAL54682.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178EG89; -.
DR   STRING; 765867.A0A178EG89; -.
DR   InParanoid; A0A178EG89; -.
DR   OrthoDB; 318119at2759; -.
DR   Proteomes; UP000077535; 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:UP000077535}.
FT   BINDING         161
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         212
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         278
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         472
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ   SEQUENCE   489 AA;  55569 MW;  C6C84C3310C3DC7D CRC64;
     MSAWNYDHTR FEAEVFELEV LGQVPADLHG AFYRVQPDHA FPPMFGEDEV PLNGDGNICV
     FNFQNGHVDF KNRYVRTPKF EAERTARRAL FGRYRNKYTD DPRVRDILTR TTANTHVIYH
     ANKIMALKED APPFEIDAVT LETIGLVDYN GTFKCPTHTA HPKADSTTGE LVGFGYEAKG
     DASPDIYSFT VDKSGRITEE VCFKAPWACM IHDFWATDNF VIFPINGLKA SLEQMQKGGE
     HFFWDENLDY QLLGVVPRRG AKPEDVKWFK TPKGCYSHTI NGYEEGGKLV LDANVWTDCV
     FPFFPNSKGK KFHYDPRNVR SPVLRYCFDP NGSTKEMIYP EKVVVEGVNE FGRIDDRLLG
     KKYNRYWILT IDPSKQVYTN GTAAQAGFNT LVCYNFENGQ SQSYYHGDNV TFQEPCFVPR
     SENAAPEDGY IVILADLYSE SRSHLLLFDA QNIEKGPLAE IKLPLKLLDG LHGSWVDGKD
     VELATGSKR
//
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