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
//