ID   A0A0G2H6K2_9PEZI        Unreviewed;       471 AA.
AC   A0A0G2H6K2;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Putative acyl-dehydrogenase family member 11 {ECO:0000313|EMBL:KKY24320.1};
GN   ORFNames=UCDDS831_g02497 {ECO:0000313|EMBL:KKY24320.1};
OS   Diplodia seriata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Diplodia.
OX   NCBI_TaxID=420778 {ECO:0000313|EMBL:KKY24320.1, ECO:0000313|Proteomes:UP000034182};
RN   [1] {ECO:0000313|EMBL:KKY24320.1, ECO:0000313|Proteomes:UP000034182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS831 {ECO:0000313|EMBL:KKY24320.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY24320.1, ECO:0000313|Proteomes:UP000034182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS831 {ECO:0000313|EMBL:KKY24320.1};
RA   Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT   "Distinctive expansion of gene families associated with plant cell wall
RT   degradation and secondary metabolism in the genomes of grapevine trunk
RT   pathogens.";
RL   Submitted (MAY-2015) 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:KKY24320.1}.
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DR   EMBL; LAQI01000060; KKY24320.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2H6K2; -.
DR   Proteomes; UP000034182; 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:SF32; -; 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}.
FT   DOMAIN          34..157
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          161..263
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          275..426
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   471 AA;  51336 MW;  5502EED1FBBE84D7 CRC64;
     MSDSKLLINS EKGHVSASQR IPPIALPYVS DRAKKTLDIV EKFVEEECIP ADSVYLQQIG
     NTPQERFSAH PPIIEDLKKK AQALGLWNMF LPKGHFKEGA GFSNLEYGLM AELLGKSRTA
     SEATNCAAPD TGNMEVLAKY GNEAQKRRWL DPLLAGKIRS AFLMTEPQVA SSDATNIELN
     MRLEGDTWVL NGQKWWSSGA GDPRCAIYVV MGKSDPANPD PYKQQSVILV PADTPGVTVH
     RMLSVMGFDD APHGHGHISF DNVRVPASAM VLGPGRGFEI IQGRLGPGRI HHAMRSIGAA
     ERALEWLLAR LNDPRKRPFG ALLSSHGVML DRVARSRIDI DAARLMVLNA AIKMDLVGPK
     NALKEIAEVK VLVPTTALAV IDRAIQAYGG AGVCQDTPLA GMYANGRTMR IVDGPDEVHV
     LQLGRNENKR GKPLGERIEA QKAKADELFR QAGLTRTDPL SLERSTGKAK L
//