ID Q0BUG0_GRABC Unreviewed; 435 AA.
AC Q0BUG0;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Dibenzothiophene monooxygenase dszC {ECO:0000313|EMBL:ABI61542.1};
DE EC=1.14.14.- {ECO:0000313|EMBL:ABI61542.1};
GN OrderedLocusNames=GbCGDNIH1_0644 {ECO:0000313|EMBL:ABI61542.1};
OS Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Granulibacter.
OX NCBI_TaxID=391165 {ECO:0000313|EMBL:ABI61542.1, ECO:0000313|Proteomes:UP000001963};
RN [1] {ECO:0000313|EMBL:ABI61542.1, ECO:0000313|Proteomes:UP000001963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1260 / CGDNIH1 {ECO:0000313|Proteomes:UP000001963};
RX PubMed=17827295; DOI=10.1128/JB.00793-07;
RA Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA Kupko J.J.III., Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT "Genome sequence analysis of the emerging human pathogenic acetic acid
RT bacterium Granulibacter bethesdensis.";
RL J. Bacteriol. 189:8727-8736(2007).
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DR EMBL; CP000394; ABI61542.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0BUG0; -.
DR STRING; 391165.GbCGDNIH1_0644; -.
DR KEGG; gbe:GbCGDNIH1_0644; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_10_0_5; -.
DR OrthoDB; 6184213at2; -.
DR Proteomes; UP000001963; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR CDD; cd01163; DszC; 1.
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 InterPro; IPR023922; S04_starv_induced_SfnB.
DR NCBIfam; TIGR04022; sulfur_SfnB; 1.
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 Monooxygenase {ECO:0000313|EMBL:ABI61542.1};
KW Oxidoreductase {ECO:0000313|EMBL:ABI61542.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001963}.
FT DOMAIN 54..155
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 278..410
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 435 AA; 47098 MW; D1B221EE75C7D188 CRC64;
MSVTELDPAS LRTASTPDTS STPHRVGSGE RGVPGVSRPA QPAHVITSDE EAVEVAHRLA
ARFAEGASER DRHSAIPRDE LDAYSQSGLW AINVPRAFGG ADVSYATVAE VIRIISAADP
SIGQITQNHL GIVFSIRANG TPEQQSILFG EILRGTRLGN AFSERGTKNV AEFITRFTDQ
GDHVIVTGQK YYSSGALLAH LVPIVALDEQ NRAWYAIADR NAPGLTVIND WSAFGQRGTA
SGTVLIDHVR VPKTHLIAGF KAYDPATVQA ESAIFQIIQA AVDAGIAEAA IKDTIRFVRE
KARPWIDAGQ DNAWEDPYTI QTIASLQIRL NAALAILEKA GHAIDEAVAN PTTDTVARAQ
IITAESKVLT TEIAIEATNK LFELGGTSST DGKYNFDRHW RNARTHTLHD PVRWKYAAIG
NYYLNGINPP LHAWS
//
