ID A0A165DIZ8_9BASI Unreviewed; 661 AA.
AC A0A165DIZ8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Carotenoid oxygenase {ECO:0000313|EMBL:KZT52911.1};
GN ORFNames=CALCODRAFT_501753 {ECO:0000313|EMBL:KZT52911.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT52911.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT52911.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT52911.1,
RC ECO:0000313|Proteomes:UP000076842};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV424052; KZT52911.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165DIZ8; -.
DR STRING; 1353952.A0A165DIZ8; -.
DR InParanoid; A0A165DIZ8; -.
DR OrthoDB; 318119at2759; -.
DR Proteomes; UP000076842; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF89; CAROTENOID 9,10(9',10')-CLEAVAGE DIOXYGENASE 1; 1.
DR Pfam; PF03055; RPE65; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR604294-1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR604294-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000076842};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 625..647
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 576..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 207
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 256
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 319
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 562
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ SEQUENCE 661 AA; 71943 MW; 3E7359A69EB14570 CRC64;
MPAHPYLSGN FAPTAHEHPL TACSITGTLP PSLSGGQYIR NGSNPLHTPK GGEERPYHWF
DGDGMLCGVL FGQGEAWFVN RLLVTDVLLA SEGLAAPLLP SITTLVSPTT SLPLLTYHIL
RSLLLALSTH LTPSPLRSLS VANTSILFHA RRALALCESG PPLEVRLPGL ETVGWQTFST
HRAGKSLGGL SAAGGLLGFF RSWTGAHPHT DPVTGELLLL HSSFLPPYLR YTVLSPHGTP
VILSAPIPLR QPKMMHDFAA SASHTVILDL PLVFGPMNLL RGRPVLYYDR TLRSRFGLVP
RYMQAETRWF EDDPCVVFHC VNAWDTVDQA GEVDAVNLLC CRFQSDALVF AAGNLPLSST
VEDPPQLHYY RFPLSSPALS PQAHNPSHSF PLLSIPFEFP CLPPPLSTRD SRFVFGCSMQ
HGSFTPALQG AKIDCLVRVD VRALIARGLA RKHGAYTPVD ARSMREFIAS TDRDDPVRVF
CLPPAHYASE PSFVPLPSFT PSSPSTHADG HLVFYVFDER QLLPDGSVRE GARSELWVLD
ARDMATVVAR VGLPGRVPYG LHGTFVTGKE ITSQRLDRPI RHRPQSRSPQ QRHAKPSGCP
RGWSAHWLVT AVVKDGLAKG DPVELLLAVL GLLQILLGLG LVVGSYLNEG AEGGGRFGME
L
//
