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Database: UniProt
Entry: A0A1S8BF20_9PEZI
LinkDB: A0A1S8BF20_9PEZI
Original site: A0A1S8BF20_9PEZI 
ID   A0A1S8BF20_9PEZI        Unreviewed;       461 AA.
AC   A0A1S8BF20;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Dibenzothiophene desulfurization enzyme C {ECO:0000313|EMBL:OMP86090.1};
GN   ORFNames=BK809_0002302 {ECO:0000313|EMBL:OMP86090.1};
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:OMP86090.1, ECO:0000313|Proteomes:UP000190776};
RN   [1] {ECO:0000313|EMBL:OMP86090.1, ECO:0000313|Proteomes:UP000190776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F98.1 {ECO:0000313|EMBL:OMP86090.1,
RC   ECO:0000313|Proteomes:UP000190776};
RA   Robert-Siegwald G., Vallet J., Abou-Mansour E., Xu J., Rey P., Bertsch C.,
RA   Rego C., Larignon P., Fontaine F., Lebrun M.-H.;
RT   "Draft genome sequence of Diplodia seriata F98.1, a fungal species involved
RT   in grapevine trunk diseases.";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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:OMP86090.1}.
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DR   EMBL; MSZU01000081; OMP86090.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S8BF20; -.
DR   STRING; 420778.A0A1S8BF20; -.
DR   OrthoDB; 2264654at2759; -.
DR   Proteomes; UP000190776; 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   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:UP000190776}.
FT   DOMAIN          53..141
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          276..435
FT                   /note="Acyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08028"
SQ   SEQUENCE   461 AA;  50024 MW;  B2C7B1CBA66E0574 CRC64;
     MAATTNGSAV LAAIAHGTIP PPATDPIIYE EYRFRWASLP STAEEWVARA AEVKEVLARD
     AVKRDRENKT PRAEIALLKH SGLLKVLGPL QYGGGGQPWS VGYRVIREVA KGDGSIGMLL
     GYHLLWSTTA NVVGTAEQAE ALQEYIVGNN LFLGGAVNPR DNDLKVTSEG DSIVFSGFKN
     FNTGGVVSDL TVLEGVLDGT DDHIFTVVRT QQPGIQFAHN WDNIGLRLTE SGSVRIDNVV
     VPWSDALGWD GLTRRPDPSV LGIPYASLLL PTIQLVFSNF YLGIAQGALD FAAAYTRKST
     RAWPHITHAA GDPPKASPLD EFYVLERYGN FHAHLAAADA LADRAGAAAA ALYAAYNHRH
     IADASLPLLH RDNRGELSAR QRGEFAELVA SVKVVTTDVG LSVTNGVFEV TGSRATAAGV
     GLDRFWRDVR THTLHDPVAY KKRELGRWVL LDEVPEVTWY T
//
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