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Database: UniProt
Entry: A0A1G4ASP9_9PEZI
LinkDB: A0A1G4ASP9_9PEZI
Original site: A0A1G4ASP9_9PEZI 
ID   A0A1G4ASP9_9PEZI        Unreviewed;       427 AA.
AC   A0A1G4ASP9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   08-NOV-2023, entry version 17.
DE   SubName: Full=Acyl-CoA dehydrogenase domain-containing protein {ECO:0000313|EMBL:OHE92197.1};
GN   ORFNames=CORC01_12491 {ECO:0000313|EMBL:OHE92197.1};
OS   Colletotrichum orchidophilum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum.
OX   NCBI_TaxID=1209926 {ECO:0000313|EMBL:OHE92197.1, ECO:0000313|Proteomes:UP000176998};
RN   [1] {ECO:0000313|EMBL:OHE92197.1, ECO:0000313|Proteomes:UP000176998}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 309357 {ECO:0000313|EMBL:OHE92197.1,
RC   ECO:0000313|Proteomes:UP000176998};
RA   Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
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}.
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:OHE92197.1}.
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DR   EMBL; MJBS01000155; OHE92197.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G4ASP9; -.
DR   STRING; 1209926.A0A1G4ASP9; -.
DR   OrthoDB; 275353at2759; -.
DR   Proteomes; UP000176998; 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   CDD; cd01151; GCD; 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; 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; 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   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:UP000176998}.
FT   DOMAIN          47..158
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          162..260
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          273..420
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   427 AA;  46454 MW;  97E7763030AE4885 CRC64;
     MYRNALRTCA TRRAATRTLP AARTFASASE GPAFNWEDPL NTKNLLTEEE LAISETAERY
     CQERMLPRVL QAYRDEQYDQ KILEEMGDLG LLGATIEGYG CAGVSTVAGG LITKAVERVD
     SGYRSGMSVQ SSLVMGGIAE FGTEEQKERF LPKMATGKLL GAFGLTEPNH GSDPGSMETT
     AKPHPTKEGY YSLSGAKTWI TNSPIADVLM VWAKLQETGK IRGFLVERSQ CPPGTLETPP
     IKNKNGLRAS ITGMIQLDDV PVPKENMFPL VEGLRGPFSC LNSARYGISL GVIGALEDCI
     ARARTYALER KQFKGNPIAK YQLVQKKLAD AATDAAYGTV AAIQVGRLKD EGKVTPEMIS
     MVKRQNCDRA LQNARVLQEI FGGNAVSDEY GIGRHVANLF VTQTYEGQSD IHSLILGRAI
     TGIQAFV
//
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