ID A0A238FBS6_9BASI Unreviewed; 448 AA.
AC A0A238FBS6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=BQ2448_1633 protein {ECO:0000313|EMBL:SCV70239.1};
GN ORFNames=BQ2448_1633 {ECO:0000313|EMBL:SCV70239.1};
OS Microbotryum intermedium.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX NCBI_TaxID=269621 {ECO:0000313|EMBL:SCV70239.1, ECO:0000313|Proteomes:UP000198372};
RN [1] {ECO:0000313|Proteomes:UP000198372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jeantristanb JTB J.-T., Ricardo R.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU362125};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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DR EMBL; FMSP01000005; SCV70239.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238FBS6; -.
DR STRING; 269621.A0A238FBS6; -.
DR OrthoDB; 1474114at2759; -.
DR Proteomes; UP000198372; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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 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 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 SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362125};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU362125};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000198372}.
FT DOMAIN 33..161
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 165..261
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 273..428
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 448 AA; 49682 MW; 6EA8C7626774B7B7 CRC64;
MTSSSTLQQP RGSLTPYAEN QWVRGIPSPY YNDSHERLRI AARAWTEEYL MDAPYEWEEN
REIDHRIYQQ LAKDGLLVCL AFGAKIPKKW ANEKGEVFGG IKVGQWDGFH DAILIDELTR
CGSLGAVQGL MGGLQIGLPP VFHYGSQELQ DRVLPEVFSG KKRICLAITE PEAGSDVKNL
SCQAKLSSDG QHFIVNGVKK WITNGVYSDY FTALVRTSGK AGQQAGISFL LIPNGPGVTR
RKMLMSGQWC AGTTYLTFED VKVPVENLIG TKDQGFKLAM QNFNHERLMI VYNSHRLSRI
CLEDSINYAT KRKVFGKPLS ESEVVRMKIA HMAREVDSMQ TWIESIVYAV ENLSHEEANA
QLGGTTAMLK AHASLVLEIV AREAVQILGG IGHTRGGVGE RIERIRRDVK GVAIPGGSEE
VMLMQSSKVA INRFQAALKA AEQNQAKL
//
