ID A0A165ZZY0_9AGAM Unreviewed; 519 AA.
AC A0A165ZZY0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KZV63228.1};
GN ORFNames=PENSPDRAFT_590220 {ECO:0000313|EMBL:KZV63228.1};
OS Peniophora sp. CONT.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Peniophoraceae; Peniophora.
OX NCBI_TaxID=1314672 {ECO:0000313|EMBL:KZV63228.1, ECO:0000313|Proteomes:UP000077086};
RN [1] {ECO:0000313|EMBL:KZV63228.1, ECO:0000313|Proteomes:UP000077086}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CONT {ECO:0000313|EMBL:KZV63228.1,
RC ECO:0000313|Proteomes:UP000077086};
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; KV424690; KZV63228.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165ZZY0; -.
DR STRING; 1314672.A0A165ZZY0; -.
DR InParanoid; A0A165ZZY0; -.
DR OrthoDB; 294001at2759; -.
DR Proteomes; UP000077086; Unassembled WGS sequence.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; 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; IPR006089; Acyl-CoA_DH_CS.
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; PS00072; ACYL_COA_DH_1; 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:UP000077086}.
FT DOMAIN 8..87
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
SQ SEQUENCE 519 AA; 56639 MW; A3746C8D7EE6B170 CRC64;
MATPQKELKT FTVEEVAKHN KEGDLWIIID AQVYDISKFA AMHPGGQAVL QVSSIAGKDA
TEAFFGLHRH EVLLRPQYAR LIIGTVRDDK PTIQARTAGS VSGVPYAEPT WLAAGFKSPY
FTESHRRFHK ALRTFIDDVV APDAVKCEEN GKRISQDVVE KLCGNGILAM RIGPGAHLKG
LKLMGGVITP EEFDCFHELI INQELARTST RGYVDGILAG GVIGLPPVLN YGSKEIQAKV
VPDVLAGRKF IALAISEAFA GSDVAGLQTT ATREGDEWVI EGTKKWITNG TFADYFTVGC
RTPEGYIAVL VPRSEGLETK AIKTSYSSTA GTAYVTFDKV RVPVANTLGK VGQGLQIILS
NFNHERWMIM SMSLSTQRRI VEECLLWANQ RKVFGKPLSS QAVVRARIAQ MVARVEGAQA
WLESLTYQMN NMTYAQMSEN LAGPIALLKQ YITSTGRATA QDAVQVFGGR GITQSGMGKL
VENYHRTSPF DAILGGAEDV MGDLGVRQAL KKMPKNARL
//