ID M7UVT6_BOTF1 Unreviewed; 427 AA.
AC M7UVT6;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Putative thermophilic desulfurizing enzyme family protein {ECO:0000313|EMBL:EMR91168.1};
GN ORFNames=BcDW1_271 {ECO:0000313|EMBL:EMR91168.1};
OS Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR91168.1, ECO:0000313|Proteomes:UP000012045};
RN [1] {ECO:0000313|Proteomes:UP000012045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT grape berries.";
RL Genome Announc. 1:E0025213-E0025213(2013).
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DR EMBL; KB707678; EMR91168.1; -; Genomic_DNA.
DR AlphaFoldDB; M7UVT6; -.
DR STRING; 1290391.M7UVT6; -.
DR HOGENOM; CLU_018204_10_1_1; -.
DR Proteomes; UP000012045; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
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; IPR013107; Acyl-CoA_DH_C.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_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:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF08028; Acyl-CoA_dh_2; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR PIRSF; PIRSF016578; HsaA; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE 4: Predicted;
FT DOMAIN 46..132
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 261..401
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 427 AA; 46979 MW; 633FF29FCD97C5B2 CRC64;
MAAQSTSISE NNPYSEYHQK FQSAVPQSEE EWLSRASEIS QIFSKDAAKR DIDNKTPHDE
VSLLKSSGLL KILGPKKYGG GGQSWDIGYK VIREVAKGDG SLGMLLGYHL LWSTTANVVG
TDEQIDRLQK EIIENNYFMG GAVNPRDSDL SIKSDGDNIV FNGQKHFNTG GVVSDMTILE
GVLEGTGKHI FAAVPTRQPG IQFAHNWNNI GLRLTESGSV KIENVRVSWE DALGWNAQTK
EPLPQILTVP FATLLLPTIQ LVFANFYIGI SLGAIESAAK YTTTYTRAWP FGGDNKDSAT
EEWYILERYG TFHAHLSAVV ALADSTGKKL TDIYAKHQGG RSVSARERGE LAEAVAAVKV
VATDVGLNVT SGVFEMTGAR ATSKNVGLDR FWRDIRTHSL HDPVAYKKRE LGRWALLGEI
PEPTWYT
//
