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
//