ID A0A135V397_9PEZI Unreviewed; 607 AA.
AC A0A135V397;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 08-NOV-2023, entry version 16.
DE SubName: Full=Carotenoid cleavage dioxygenase 1 {ECO:0000313|EMBL:KXH67071.1};
GN ORFNames=CSAL01_10915 {ECO:0000313|EMBL:KXH67071.1};
OS Colletotrichum salicis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH67071.1, ECO:0000313|Proteomes:UP000070121};
RN [1] {ECO:0000313|EMBL:KXH67071.1, ECO:0000313|Proteomes:UP000070121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH67071.1,
RC ECO:0000313|Proteomes:UP000070121};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum salicis CBS 607.94.";
RL Submitted (FEB-2014) 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:KXH67071.1}.
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DR EMBL; JFFI01000546; KXH67071.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135V397; -.
DR STRING; 1209931.A0A135V397; -.
DR OrthoDB; 294919at2759; -.
DR Proteomes; UP000070121; 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:KXH67071.1};
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:KXH67071.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000070121}.
FT REGION 534..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 254
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 306
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 376
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 601
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ SEQUENCE 607 AA; 66382 MW; 16ABEFDBD0C6B921 CRC64;
MATTTTTKTS TTSITMSANT KIPARTVRRT AKDEAADLQM FEENRLRAPY DEWPNEAGFD
GLTEERGPIE LHVQGQIPAW AAGALYRTGP GSCKIEDTPK GTYYVSHWFD GFAQTHKFDI
IPPESPGGRT RVLYSSRRQS DDLVASIKAA GHQNRYTFGQ KADPCVGMLS KFMGVFARGT
APNICVAVNA NVPGFDTKDQ GPAGPGHRNA VRSLWLSTDS SPLMEIDPAT LEPIGLAKQE
KLHPSLSGPM SCAHAQRDPV TGDMYNFNLA FAMKSTYRIF RTSFATGETE ILATITGPDA
KPAYIHSFFL TESFVVLCIP SSHLGYKGLS VPWERNILDA IVPFDKNNTC KWYFIDRHHG
NGVVASFNTP AGFFFHATNA FEEPAADGSD GILDVYCEIS GYQNLNILYN LYYDVIMNRN
SAGEKFWTDE NNRYKNGYAS LQRFKFRIPK PDGSQTAKTT TITTATPPEL VASIPAPHAG
ELPTINPAHL TKRHRYVYSL SDRGLSTLLD TIVKTDADTA EALMWECPTA HTPGEPIFVP
RPSSAGGADG TDEQMAEDDG VILSVVLDGT AQTSYLLCLD ARTMTELGRA ECEFAVGIGF
HGIHAPS
//