ID A0A1Y2VNU0_9PEZI Unreviewed; 599 AA.
AC A0A1Y2VNU0;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 08-NOV-2023, entry version 18.
DE RecName: Full=Carotenoid oxygenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=M426DRAFT_70005 {ECO:0000313|EMBL:OTA98346.1};
OS Hypoxylon sp. CI-4A.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX NCBI_TaxID=1001833 {ECO:0000313|EMBL:OTA98346.1, ECO:0000313|Proteomes:UP000242955};
RN [1] {ECO:0000313|EMBL:OTA98346.1, ECO:0000313|Proteomes:UP000242955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CI-4A {ECO:0000313|EMBL:OTA98346.1,
RC ECO:0000313|Proteomes:UP000242955};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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; KZ111668; OTA98346.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2VNU0; -.
DR STRING; 1001833.A0A1Y2VNU0; -.
DR InParanoid; A0A1Y2VNU0; -.
DR OrthoDB; 294919at2759; -.
DR Proteomes; UP000242955; 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 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:UP000242955}.
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 249
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 301
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 371
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 584
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ SEQUENCE 599 AA; 66161 MW; E833327D4AC013AF CRC64;
MASGAEVLGT RERQILGGPE NEDVDFENTV QGMLDADSQD WPNEAGFEGL DEIRGPVELE
VKGSIPNWAA GTLYRTGPGQ YTIDDTPRGQ FRTIHWFDGL SHSHRFSIIA DPNNTDVPVR
VEYWSRRQSQ ALYDAIKKHG RRLEPSFGQR MDPCVGIFGK IMSVWRGIPT DKPINYDNVG
VAVHANIPGL PSAADKPAQG GHRGGIDNLW ITTDTGTMKE VDQHTLEPVG KARQEKLHPL
LKGPLSCAHA QRDPVTGDFF NYNLDLGYPS TYRIFRTSAS TGKTDILATL AGADVKPAYI
HSFFLAPSYV VFCIPSSHLG LMGIKVPWNG SIADGIDPFD ESKLCRWFVI DRIGDRGVVA
TFDSPAGFYF HSINSFEEHD EATGGDNVYC DVVQYPTIDI IRALQVDVII KHNGAAQNFW
GDEERNRNSQ ARLARWKFTI PKLGTAEKDA SMVRRKAEKV FEIKAPHVGE LPTINAAYAT
RKYQYVYSLA SRGYSTLLDT IVKTNVVTRE TLFWNNPKGH TPGEAIFVSR PKSHGEDLDE
DDGVLLSVVL DGAGKTSYLV CLDARTMKEL GRAECDFAIA LGFHGLHWPT APSSSSTSS
//
