ID A0A0M9ESV7_FUSLA Unreviewed; 458 AA.
AC A0A0M9ESV7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Carotenoid oxygenase {ECO:0000313|EMBL:KPA39209.1};
GN ORFNames=FLAG1_07928 {ECO:0000313|EMBL:KPA39209.1};
OS Fusarium langsethiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=179993 {ECO:0000313|EMBL:KPA39209.1, ECO:0000313|Proteomes:UP000037904};
RN [1] {ECO:0000313|EMBL:KPA39209.1, ECO:0000313|Proteomes:UP000037904}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fl201059 {ECO:0000313|EMBL:KPA39209.1,
RC ECO:0000313|Proteomes:UP000037904};
RA Lysoe E., Divon H.H., Terzi V., Orru L., Lamontanara A., Kolseth A.-K.,
RA Frandsen R.J., Nielsen K., Thrane U.;
RT "The draft genome sequence of Fusarium langsethiae, a T-2/HT-2 mycotoxin
RT producer.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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:KPA39209.1}.
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DR EMBL; JXCE01000211; KPA39209.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M9ESV7; -.
DR OrthoDB; 318119at2759; -.
DR Proteomes; UP000037904; 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: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 Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR604294-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000037904}.
FT REGION 398..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 245
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 300
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 363
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ SEQUENCE 458 AA; 50760 MW; A590B6C23469F90A CRC64;
MDSLQHIVPA AVSMSHPKEQ SPPQTLRHPY LIGNFAPIHK TLNLTPCTHS GCIPPELTDG
QYVRNGGNLV SHEDLGRDAH WFDGDGMLSG VLFRKGHSDG QIVPEFVNQY ILTDLYLSRK
TTSVSSPIMP SITTLVNPLS SLLKIMLATF RTMFLVFLSN LPGSQQALKR TSVANTAILY
HDGRALATCE SGPPMRIQLP SLDTVGWYNG AHAEGEPEQA LSENKIEPFG GDSLFKSMRE
WTTGHPKVDP VSGEMILYHN TFIQPYVHYS VLPKTDVQAP TTGRLVNQAV PGVSGARMMH
DFGASRTHTI IMDLPLTLDP MNLTKNKEVV SYDPSKPSRF GVFPRHEPSN VRWFQTAPSC
IFHTANSWDT KSVNGTSSVN LLACRMTSST VVYTAGNIKP PVKPKRHNNR LPHVKENVSQ
WDEKDIQRFE AAPMLESPTE KLHGDNYFSS SDEADDYS
//
