ID A0A1M2V240_TRAPU Unreviewed; 287 AA.
AC A0A1M2V240;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 08-NOV-2023, entry version 19.
DE SubName: Full=Glutaryl-CoA dehydrogenase, mitochondrial {ECO:0000313|EMBL:OJT01650.1};
GN ORFNames=TRAPUB_7908 {ECO:0000313|EMBL:OJT01650.1};
OS Trametes pubescens (White-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=154538 {ECO:0000313|EMBL:OJT01650.1, ECO:0000313|Proteomes:UP000184267};
RN [1] {ECO:0000313|EMBL:OJT01650.1, ECO:0000313|Proteomes:UP000184267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FBCC735 {ECO:0000313|EMBL:OJT01650.1,
RC ECO:0000313|Proteomes:UP000184267};
RA Makela M.R., Granchi Z., Peng M., De Vries R.P., Grigoriev I., Riley R.,
RA Hilden K.;
RT "Genome sequence of the basidiomycete white-rot fungus Trametes
RT pubescens.";
RL Submitted (OCT-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|RuleBase:RU362125}.
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:OJT01650.1}.
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DR EMBL; MNAD01001728; OJT01650.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M2V240; -.
DR STRING; 154538.A0A1M2V240; -.
DR OMA; TVWAQTD; -.
DR OrthoDB; 275353at2759; -.
DR Proteomes; UP000184267; 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; 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; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR PANTHER; PTHR42807; GLUTARYL-COA DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR42807:SF1; GLUTARYL-COA DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 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:UP000184267}.
FT DOMAIN 28..120
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 131..279
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 287 AA; 31238 MW; 0B217C887CA3CE05 CRC64;
MHPIYAYGTQ AQKDKYLPLL AKGKLIGCFG LTEPNHGSDP AGMETTATEV DGGFVINGSK
TWISNAPVAD VFIIWARCKW DNKVRGFILE KGAKGLSAPA IKHKLALRCS LTGSIFMDNV
QVSHDALLPH GQGLGAPFGC LNNARFGIAW GTMGALEDCV HRTREYALER QQFKRPLASF
QLVQKKLVDA QTEVTLGLLA CLQVGRLKDE GKVAPEMISL IKRNNCGKAL EHARRVLDIL
GGNACSDEYH VGRHVANLQV VNTYEGTYDI HTLILGKAIT GIQAFAN
//
