ID A0A2N6NP18_BEABA Unreviewed; 433 AA.
AC A0A2N6NP18;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Dibenzothiophene desulfurization enzyme C {ECO:0000313|EMBL:PMB69023.1};
GN Name=soxC {ECO:0000313|EMBL:PMB69023.1};
GN ORFNames=BM221_005609 {ECO:0000313|EMBL:PMB69023.1};
OS Beauveria bassiana (White muscardine disease fungus) (Tritirachium
OS shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=176275 {ECO:0000313|EMBL:PMB69023.1, ECO:0000313|Proteomes:UP000235728};
RN [1] {ECO:0000313|EMBL:PMB69023.1, ECO:0000313|Proteomes:UP000235728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEF-007 {ECO:0000313|EMBL:PMB69023.1,
RC ECO:0000313|Proteomes:UP000235728};
RX PubMed=27470140; DOI=10.1007/s00253-016-7734-y;
RA Kim S., Lee S.J., Nai Y.S., Yu J.S., Lee M.R., Yang Y.T., Kim J.S.;
RT "Characterization of T-DNA insertion mutants with decreased virulence in
RT the entomopathogenic fungus Beauveria bassiana JEF-007.";
RL Appl. Microbiol. Biotechnol. 100:8889-8900(2016).
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:PMB69023.1}.
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DR EMBL; MRVG01000005; PMB69023.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N6NP18; -.
DR OMA; HNWDNVG; -.
DR Proteomes; UP000235728; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000235728}.
FT DOMAIN 49..129
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 263..407
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
SQ SEQUENCE 433 AA; 47594 MW; 0571ECA92D4CF0DF CRC64;
MSSNARDAPA TDPKVYDEYI DKWQQQQPTD VAGWLQRAKD VAKVLDTDAG IRERENKSPR
AEIALLKHSG LLKVLGQPKY GGGGQPWSVG YKVIQEVAKG DGSIGMLLGY HLLWSTTARV
VGSDEQVERT EELIIKNNYF VGGAVNPRDS DLKITNDGDN IVFNGFKFFN TGGVISDLTV
LEGVYEDTSD HIFAIVKTDQ SGIQFGHDWN NIGLRLTESG SVKIENVKAP WADALGWDAA
AKKPDPAVLG IAFGSLLLPT IQLVFSNFYL GIAWGALNTA TAYTNSSTRA WPFGGDNKEK
PQDEFYILST YGNFLAHLRA ATALAEKAGQ EVDAVYEGTQ KSVQNRAKVT AQARGEVAEW
IASVKVVSTD VGLRVTSGVF ELTGSKATAT KVGLDRFWRD IRTHTLHDPV AYKNRELGRY
QLLQEFPEPT WYT
//
