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Database: UniProt
Entry: A0A2P8A4A8_9PEZI
LinkDB: A0A2P8A4A8_9PEZI
Original site: A0A2P8A4A8_9PEZI 
ID   A0A2P8A4A8_9PEZI        Unreviewed;       441 AA.
AC   A0A2P8A4A8;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   08-NOV-2023, entry version 13.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:PSK55302.1};
GN   ORFNames=B9Z65_2691 {ECO:0000313|EMBL:PSK55302.1};
OS   Elsinoe australis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Myriangiales; Elsinoaceae; Elsinoe.
OX   NCBI_TaxID=40998 {ECO:0000313|EMBL:PSK55302.1, ECO:0000313|Proteomes:UP000243723};
RN   [1] {ECO:0000313|EMBL:PSK55302.1, ECO:0000313|Proteomes:UP000243723}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NL1 {ECO:0000313|EMBL:PSK55302.1,
RC   ECO:0000313|Proteomes:UP000243723};
RA   Cheng Q.;
RT   "Draft genome sequence of Elsinoe australis.";
RL   Submitted (MAY-2017) 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:PSK55302.1}.
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DR   EMBL; NHZQ01000067; PSK55302.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P8A4A8; -.
DR   STRING; 40998.A0A2P8A4A8; -.
DR   Proteomes; UP000243723; 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; 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; PTHR48083:SF15; ACYL-COA DEHYDROGENASE APDG; 1.
DR   PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 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:UP000243723}.
FT   DOMAIN          23..152
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          156..252
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          264..421
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   441 AA;  48452 MW;  41C52862FB396734 CRC64;
     MGPRLVPFSE PPYLAGIPSP YYSESHLKWQ KNCRKFVEEN LLKHAMDWER EETVPEHVFE
     TFAKANMLLP ALPAPLPVER LRSLGINDIL GTTIEEWDYF HTLIYNDEML RSGLAGPPGS
     LTTGIAFGVP PIIKFGSKQL QDRFLPELLT GKKRSCIAIT EPDAGSDVAN IQTTAKQSAD
     GKKYIVNGAK KWITNGVWSH SATMAVRTGG PGPGGLSMLV VPLLGYPGVS MRRLKVAGQI
     SAGTTYIELD DVEVPIENLI GQEGMGMKYI MTNFNHERLA IAVGATRQAR VALSSAFEYC
     LQREAFGKTL MEQPVVRHRL AKCGAQLEAQ WAWVEHFVYA MTKMPKEEAD VELGGLTAAA
     KAQAGMVLNE CAQCAVLLFG GNGFTRSGKG EIAERLYREV PGNRLPGGSE DVMLDLMVRQ
     LVKIYQSGKK IQERPEGSSK L
//
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