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Database: UniProt
Entry: A0A286ULU9_9AGAM
LinkDB: A0A286ULU9_9AGAM
Original site: A0A286ULU9_9AGAM 
ID   A0A286ULU9_9AGAM        Unreviewed;       433 AA.
AC   A0A286ULU9;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=short-chain 2-methylacyl-CoA dehydrogenase {ECO:0000256|ARBA:ARBA00039036};
DE            EC=1.3.8.5 {ECO:0000256|ARBA:ARBA00039036};
GN   ORFNames=PNOK_0320000 {ECO:0000313|EMBL:PAV20573.1};
OS   Pyrrhoderma noxium.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Hymenochaetales; Hymenochaetaceae; Pyrrhoderma.
OX   NCBI_TaxID=2282107 {ECO:0000313|EMBL:PAV20573.1, ECO:0000313|Proteomes:UP000217199};
RN   [1] {ECO:0000313|Proteomes:UP000217199}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FFPRI411160 {ECO:0000313|Proteomes:UP000217199};
RA   Chung C.-L., Lee J.T., Akiba M., Lee H.-H., Kuo T.-H., Liu D., Ke H.-M.,
RA   Yokoi T., Roa M.B., Lu M.J., Chang Y.-Y., Ann P.-J., Tsai J.-N.,
RA   Chen C.-Y., Tzean S.-S., Ota Y., Hattori T., Sahashi N., Liou R.-F.,
RA   Kikuchi T., Tsai I.J.;
RT   "The Genomic Landscape Of Tree Rot In Phellinus noxius And Its
RT   Hymenochaetales Members.";
RL   bioRxiv 0:0-0(2017).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-methylbutanoyl-CoA + H(+) + oxidized [electron-transfer
CC         flavoprotein] = (2E)-2-methylbut-2-enoyl-CoA + reduced [electron-
CC         transfer flavoprotein]; Xref=Rhea:RHEA:43780, Rhea:RHEA-COMP:10685,
CC         Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57336,
CC         ChEBI:CHEBI:57337, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307; EC=1.3.8.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00036426};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43781;
CC         Evidence={ECO:0000256|ARBA:ARBA00036426};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU362125};
CC   -!- PATHWAY: Amino-acid degradation; L-isoleucine degradation.
CC       {ECO:0000256|ARBA:ARBA00037895}.
CC   -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation.
CC       {ECO:0000256|ARBA:ARBA00005198}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347, 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:PAV20573.1}.
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DR   EMBL; NBII01000003; PAV20573.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A286ULU9; -.
DR   STRING; 2282107.A0A286ULU9; -.
DR   InParanoid; A0A286ULU9; -.
DR   OrthoDB; 275353at2759; -.
DR   Proteomes; UP000217199; Chromosome 3.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   CDD; cd01158; SCAD_SBCAD; 1.
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; 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   PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43884:SF1; SHORT/BRANCHED CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL; 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.
DR   PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 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:UP000217199}.
FT   DOMAIN          59..167
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          174..267
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          280..426
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   433 AA;  47277 MW;  41075B6DE10B1900 CRC64;
     MYNRTLASSF SRATASARSL RAHGRIQAQA PTFKHPARSF SVTRSRRSES VLNSLDTLTE
     EELMLQESVR RFSAEVVGPK VREMDEKEMM DPEIIAGLYE QGLMGIETPT EYGGAGCSFT
     SAIIAIEELA KVDPSVSVLC DVHNTLVNTI FRVHGTKEQK EKFLPLLSEK GVGSFCLSEP
     ASGSDAFALQ TKAQKEGNDW IINGSKMWIT NSYEAEVFLI FANVDPTKGY KGITCFAATK
     DMGIQIAKKE QKLGIRASST CTLNFDDLRV PSENIIGGIG QGYKIAIECL NEGRIGIAAQ
     MIGLAQGAFD KAVPYTYQRV QFGQPVGTFQ GMAFQIAQAA TDIAGARLLT YNAARRKEEG
     KSFTKEAAMA KLAASQVAQR VSGMAIEWAG GVGFTRETGI EKYWRDSKIG AIYEGTSNIQ
     LQTIAKLIQK EYS
//
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