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Database: UniProt
Entry: A0A165KPJ2_EXIGL
LinkDB: A0A165KPJ2_EXIGL
Original site: A0A165KPJ2_EXIGL 
ID   A0A165KPJ2_EXIGL        Unreviewed;       521 AA.
AC   A0A165KPJ2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Acyl-CoA dehydrogenase NM domain-like protein {ECO:0000313|EMBL:KZV96657.1};
GN   ORFNames=EXIGLDRAFT_670919 {ECO:0000313|EMBL:KZV96657.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV96657.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZV96657.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZV96657.1,
RC   ECO:0000313|Proteomes:UP000077266};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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}.
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DR   EMBL; KV425940; KZV96657.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165KPJ2; -.
DR   STRING; 1314781.A0A165KPJ2; -.
DR   InParanoid; A0A165KPJ2; -.
DR   OrthoDB; 294001at2759; -.
DR   Proteomes; UP000077266; 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:SF28; ACYL-COA DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10880); 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   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:UP000077266}.
FT   DOMAIN          8..87
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
SQ   SEQUENCE   521 AA;  58148 MW;  B3ECB12B78CD184C CRC64;
     MSAPKKELKE FTPEEIAKHN KSGDLWTIID GKVYDLSRFQ NLHPGGLAAL LDPDVAGQDA
     TEIFYGLHRH EVLQKPQYAR LQIGTVKGEL SLIESREPGQ ISGVPYAEPT WLQKGYYSPY
     YTDKHREFQL VVRKFIDEVV YEDAQAREED GKRVSQEVLD KMADVEMHAM RLGPGKHLKG
     RTLMGGLVKP EEFDYFHELI ITQELTRVGA RGYGDGLLGG MVIGLPPVLN FGSKELQERI
     VPDILKGKKF ISLAISEAYA GSDVSNLKTT AVKSEDGKFW IVNGSKKWIT NGTFSDYFTT
     GVRTDGGLTV LLIERGEGVE TKQIKTSYST TAGTAYITFD NVKVPVENTL GPENDGLRVI
     LSNFNHERWV MCCASARSQR LVIEECLTWA NQRQVFGKPL IAQAVIRNKL AQMIARTEAG
     HNWLENVTHQ MNNMSYKEMS AKLAGQIAFL KMYLTQNAQD TARDAVQIFG GRGTTRTGMG
     RFIEHYHRTI TFDSLLGGAE DVLGDLGVRQ AIRKIPAGAR L
//
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