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Database: UniProt
Entry: A0A1S9DW60_ASPOZ
LinkDB: A0A1S9DW60_ASPOZ
Original site: A0A1S9DW60_ASPOZ 
ID   A0A1S9DW60_ASPOZ        Unreviewed;       637 AA.
AC   A0A1S9DW60;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Acyl-CoA dehydrogenase domain-containing protein {ECO:0000313|EMBL:OOO13230.1};
GN   ORFNames=OAory_01009790 {ECO:0000313|EMBL:OOO13230.1};
OS   Aspergillus oryzae (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5062 {ECO:0000313|EMBL:OOO13230.1, ECO:0000313|Proteomes:UP000190312};
RN   [1] {ECO:0000313|EMBL:OOO13230.1, ECO:0000313|Proteomes:UP000190312}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCC7051 {ECO:0000313|EMBL:OOO13230.1,
RC   ECO:0000313|Proteomes:UP000190312};
RA   Thammarongtham C., Vorapreeda T., Nookaew I., Srisuk T., Land M.,
RA   Jeennor S., Laoteng K.;
RT   "Genome sequencing of Aspergillus oryzae BCC7051.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={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:OOO13230.1}.
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DR   EMBL; MKZY01000002; OOO13230.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S9DW60; -.
DR   VEuPathDB; FungiDB:AO090005000482; -.
DR   eggNOG; KOG0137; Eukaryota.
DR   OMA; IEMVAMT; -.
DR   Proteomes; UP000190312; 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; 2.40.110.20; -; 1.
DR   Gene3D; 6.10.250.600; -; 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; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR   InterPro; IPR041504; AidB_N.
DR   PANTHER; PTHR42707; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR42707:SF2; ACYL-COA DEHYDROGENASE FAMILY MEMBER 11; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF18158; AidB_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:UP000190312}.
FT   DOMAIN          22..164
FT                   /note="Adaptive response protein AidB N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18158"
FT   DOMAIN          187..302
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          312..482
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   637 AA;  70538 MW;  3A26E7B9DE94F866 CRC64;
     MESGPRHATV DRGHITKPER LENTYTSDTS LQRALSWYLP AQKLEQAQPQ LVELGEEAIS
     DQIREWSADA ERHQPYVKGF NVWGQRYDYD RLITSEGWKQ LGKWGARHGV VSLGYEPTYG
     AERRLVQYTV NYLYSPSSGL YSCPVSMSDG AALVLNQERK NVAADHPFQT AYQKLISKKE
     DYWTSGQWMT ERAGGSDVQN TETWATYSPL SHKSKASNGL DEGDYLINGF KFFSSATDAN
     IALMLAKTPS GKLSTFLAPL RKTIVGEDGK PRVVTNGVRI HRLKNKLGTK ELPTAELELK
     DMRAHLVGTV DHGVMAIAPL LNITRTHTFI GSLAAWRRAI SITKSFAKAR TTVGEPLWLI
     PMHLSLLADL EVKHRGAMNL AFFTVAVMGV VENNGVSTPA AHLPTKGKEA QVVFRALTAI
     AKAVISKNAI AGIQECQEGM GGVGYMDEPD EPEFNIARLL RNTAVNSIWE GTTNVLASEL
     VRFLVKRDNL TIFSAWFERT LALITTPEFA SALKQIWSDF LSRTKATSEP RFILADARRV
     MFTLAWILCG ALLALDAERD GDGVTTEIAR RWILSGEGGV GDMVWRDIIS VQRTASAGPS
     SITNEHLRWD CRIAWGVELP AKQVSGHRSF QGTGSKL
//
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