ID A0A0A2K2I9_PENEN Unreviewed; 532 AA.
AC A0A0A2K2I9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Carotenoid oxygenase {ECO:0000313|EMBL:KGO61947.1};
GN ORFNames=PEX2_014430 {ECO:0000313|EMBL:KGO61947.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO61947.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO61947.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO61947.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO61947.1}.
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DR EMBL; JQFZ01000027; KGO61947.1; -; Genomic_DNA.
DR RefSeq; XP_016602613.1; XM_016738719.1.
DR AlphaFoldDB; A0A0A2K2I9; -.
DR STRING; 27334.A0A0A2K2I9; -.
DR GeneID; 27674138; -.
DR HOGENOM; CLU_016472_6_2_1; -.
DR OrthoDB; 318119at2759; -.
DR Proteomes; UP000030143; 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:UP000030143}.
FT BINDING 182
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 233
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 493
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ SEQUENCE 532 AA; 59726 MW; C1B088237BB8E43C CRC64;
MSDIAAITEK LAPQPEAAYP KTPFYEGPEA PCRFEGEVYN CIVRGTIPTE VQGTYYRCMP
DALWAPKYED DVFINGDGAI NAIRIKDGHA DFKQKYVRTS KFVIERAARQ AVFGKYRNRY
TDDPRVKHEI HSTANTHIIY FEKQLLALKE DSPPYAMDPH TLETKGPYTF NGQYTAPTFT
AHPKIDPTNG EMLTMGYEAK GDGTTDVAYY LFSKEGEKLE ECWFNAPYVG MMHDMAATDN
WVILIVPPLE TQPLDEIKKG SKHFAWAEEK PLTFGILPRR NPKPEDIRWF TYKNAFYGHT
GNAFDGEDGC VYLDAPLTNF NKFWFFPPRG QDQMEAASGK PPASGNVSQY VRWKFDPKAT
DFHVEPVVLV DADGEMPKVD DRYVGKPYNT LFYAMHDPTK GNGPVGGVYN AIAKCNVGTG
ELTFWSAGDH TAIHEVAFIP RNPESPEADG YLITLANRRD TGLSCILILD AQKITDGPVA
VIELPFRLRN GIHGSWVSAT ELDNAIDLCD MSGVTEKIRQ EFATKEVTFP VL
//
