ID A0A1F8A5T5_9EURO Unreviewed; 554 AA.
AC A0A1F8A5T5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 08-NOV-2023, entry version 14.
DE SubName: Full=Dioxygenase {ECO:0000313|EMBL:OGM47057.1};
GN ORFNames=ABOM_003651 {ECO:0000313|EMBL:OGM47057.1};
OS Aspergillus bombycis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM47057.1, ECO:0000313|Proteomes:UP000179179};
RN [1] {ECO:0000313|EMBL:OGM47057.1, ECO:0000313|Proteomes:UP000179179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX PubMed=27664179;
RA Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT bombycis.";
RL Genome Biol. Evol. 0:0-0(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}.
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:OGM47057.1}.
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DR EMBL; LYCR01000026; OGM47057.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8A5T5; -.
DR STRING; 109264.A0A1F8A5T5; -.
DR OrthoDB; 294919at2759; -.
DR Proteomes; UP000179179; 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:SF24; CAROTENOID ISOMEROOXYGENASE; 1.
DR Pfam; PF03055; RPE65; 1.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000313|EMBL:OGM47057.1};
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:OGM47057.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000179179}.
FT BINDING 223
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 272
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 339
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 540
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ SEQUENCE 554 AA; 61431 MW; DE3DBEDAE358E410 CRC64;
MAITTSITES QVHFNNWPND RGFDANYEER SPIELSVTGR IPSYAAGVLY RTGPGKYKVD
RENGETFQVS HWFDGFSETH RFQLLAPDTA HSSLRVFYNS RFSTDFLIEE ARKTGCLGKI
SFGQKRDPCK TVYQKAQSEF NPDPSSANVG VTLSVNMPGL DKSMNENQQS SGRWTGYSGI
KTLYAKTDSA SYKRLNPETL EPVGLASQKD LHPDLDGLLS ASHARSDPIT GDVYNFNLAF
GKSSTYQVFH VSASTGKTTI LATFEGTPAY LHSLFLSKDY VILCVWNSHV NPTMLEKGSF
MEAIQPFDAS QPTKWYVVDR TQGQGLVATY ESPPFFCFHT VNAWQEPSVG GNGVDIVAEL
VRFDNTDVLH ALYYEKLVSS SVEAKAHVQL KQDTSRSDFA RFRLSNIPAS PITEVKTAAA
EWMSCKAFSP ELPTMNPKLV TQKHRYTYAI TDCGESTFFD GIIKFDSETM ETLLWNDHAQ
SPGEPIFIPR PDGLEEDDGV LLSVVLDGYS GKSYLLCLDA HTLKELGRAH VNGPVGFGFH
GQHIPLKGAP TGDY
//
