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Database: UniProt
Entry: A0A2T6ZSE2_TUBBO
LinkDB: A0A2T6ZSE2_TUBBO
Original site: A0A2T6ZSE2_TUBBO 
ID   A0A2T6ZSE2_TUBBO        Unreviewed;       525 AA.
AC   A0A2T6ZSE2;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Acyl-CoA dehydrogenase/oxidase {ECO:0000313|EMBL:PUU78398.1};
GN   ORFNames=B9Z19DRAFT_983297 {ECO:0000313|EMBL:PUU78398.1};
OS   Tuber borchii (White truffle).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Tuberaceae; Tuber.
OX   NCBI_TaxID=42251 {ECO:0000313|EMBL:PUU78398.1, ECO:0000313|Proteomes:UP000244722};
RN   [1] {ECO:0000313|EMBL:PUU78398.1, ECO:0000313|Proteomes:UP000244722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tbo3840 {ECO:0000313|EMBL:PUU78398.1,
RC   ECO:0000313|Proteomes:UP000244722};
RG   DOE Joint Genome Institute;
RA   Murat C., Kuo A., Barry K.W., Clum A., Dockter R.B., Fauchery L., Iotti M.,
RA   Kohler A., Labutti K., Lindquist E.A., Lipzen A., Ohm R.A., Wang M.,
RA   Grigoriev I.V., Zambonelli A., Martin F.M.;
RT   "Draft genome sequence of Tuber borchii Vittad., a whitish edible
RT   truffle.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347}.
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:PUU78398.1}.
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DR   EMBL; NESQ01000120; PUU78398.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T6ZSE2; -.
DR   STRING; 42251.A0A2T6ZSE2; -.
DR   Proteomes; UP000244722; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR   Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR   Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR   Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR   InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR   InterPro; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR013786; AcylCoA_DH/ox_N.
DR   InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR   InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR   InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR   PANTHER; PTHR48083:SF20; LONG-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   PRINTS; PR00363; CYTOCHROMEB5.
DR   SMART; SM01117; Cyt-b5; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR   SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244722}.
FT   DOMAIN          2..78
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   REGION          75..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   525 AA;  58918 MW;  D781C33C1163CC97 CRC64;
     MSKIFKATEV AEHKKPDSLW IIVEGDVYDV TKFQNDHPGG KKILQRVGGK DATAQFWKYH
     NEGILKKYKT QLQIGSLEGK APPPEPKKEE PKKEEQALET FGDLIPFGDP AWYQGYHSPY
     YNASHAALRD EVRAWVEEKI EPHLNDWEKQ KFVPVEIYKE MGTRGYLPGL LGVKYPKEYT
     PYSVASVPPE KWDHFHEFLL TDELSRTGSG GFVWNMIGGY SIGLPPVMKF GRKELKDRIV
     PGILTGEKRI CLCITEPDAG SDVANLTCEA KKTPDGKHYI VNGEKKWITN GIWSEYFTVA
     VRTGGPGMGG VSVLLIERGP GVSTREMDCQ GVHGSGTTYI TFEDVKVPVE NLIGKENAGF
     KVIMTNFNHE RLGIVIQCTR FSRVLYEESM KYANRRRTFG KKLIEHPVIR LKLAHMARQI
     EATHNWLENI VYQSSCMSDT EAMLKLGGAI AGLKAQSTTT FEFCAREATQ IFGGIGYTKG
     GVGAKVERLY RDVRGYSIPG GSEEIMLDLS IRQSLKVHQA LGMKL
//
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