ID   A0A241WCX4_9GAMM        Unreviewed;       410 AA.
AC   A0A241WCX4;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=SfnB family sulfur acquisition oxidoreductase {ECO:0000313|EMBL:OTG91821.1};
GN   ORFNames=B9T34_00255 {ECO:0000313|EMBL:OTG91821.1};
OS   Acinetobacter sp. ANC 3813.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1977873 {ECO:0000313|EMBL:OTG91821.1, ECO:0000313|Proteomes:UP000194864};
RN   [1] {ECO:0000313|EMBL:OTG91821.1, ECO:0000313|Proteomes:UP000194864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANC 3813 {ECO:0000313|EMBL:OTG91821.1,
RC   ECO:0000313|Proteomes:UP000194864};
RA   Nemec A., Radolfova-Krizova L.;
RT   "High diversity of culturable Acinetobacter species in natural soil and
RT   water ecosystems.";
RL   Submitted (APR-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:OTG91821.1}.
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DR   EMBL; NEGK01000001; OTG91821.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A241WCX4; -.
DR   OrthoDB; 6502068at2; -.
DR   Proteomes; UP000194864; 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   InterPro; IPR023922; S04_starv_induced_SfnB.
DR   NCBIfam; TIGR04022; sulfur_SfnB; 1.
DR   PANTHER; PTHR48083:SF13; ACYL-COA DEHYDROGENASE FAMILY MEMBER 11; 1.
DR   PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, 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          34..133
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          253..386
FT                   /note="Acyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08028"
SQ   SEQUENCE   410 AA;  44744 MW;  BAC75F78A6A66DC2 CRC64;
     MTSFQNIVPF QSSSTAGSAQ AHIIQSDAEA LEIAQHLAEQ FKQTAVTRDA QRILPFEEIE
     AYSQSGLWAI TLPKAYGGAE VSSYTVAQVI ALISGADGSI GQIPQNHFYA LEVLRNTATE
     QQKQKLYAEV LQGARFGNAL AEFKTKSASQ KQTSITKTAD GFVVNGEKFY CTGSLFAHRI
     PTLVKDAEGR EFLAFISRDS QGLELIDDWS GFGQRTTGSG TVKFNHVAVA AEDVIPFDTA
     FSEPTLVGPF AQIMHAAIET GIARAAFEET LVRVRQARPW IDSGVDHATD DPLTKFELGR
     IIADVRASEV LLKQAGLSID DARPNPTAEN IAKASLDVAK VRAHSTETAL KASSKLIELA
     GSRGSQRADG LDRYWRNARV HTLHDASRWK YYFIANYLLN GVLPPRRGTL
//