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Database: UniProt
Entry: A0A0M2T1M3_9BACI
LinkDB: A0A0M2T1M3_9BACI
Original site: A0A0M2T1M3_9BACI 
ID   A0A0M2T1M3_9BACI        Unreviewed;       398 AA.
AC   A0A0M2T1M3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KKK39137.1};
GN   ORFNames=WQ57_05015 {ECO:0000313|EMBL:KKK39137.1};
OS   Mesobacillus campisalis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX   NCBI_TaxID=1408103 {ECO:0000313|EMBL:KKK39137.1, ECO:0000313|Proteomes:UP000034166};
RN   [1] {ECO:0000313|EMBL:KKK39137.1, ECO:0000313|Proteomes:UP000034166}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA2-6 {ECO:0000313|EMBL:KKK39137.1,
RC   ECO:0000313|Proteomes:UP000034166};
RA   Mathan Kumar R., Kaur G., Kumar A., Singh N.K., Kaur N., Kumar N.,
RA   Mayilraj S.;
RT   "Taxonomic description and genome sequence of Bacillus campisalis sp. nov.,
RT   a novel member of the genus Bacillus isolated from solar saltern.";
RL   Submitted (APR-2015) 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:KKK39137.1}.
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DR   EMBL; LAYY01000004; KKK39137.1; -; Genomic_DNA.
DR   RefSeq; WP_046522628.1; NZ_LAYY01000004.1.
DR   AlphaFoldDB; A0A0M2T1M3; -.
DR   PATRIC; fig|1408103.3.peg.1126; -.
DR   OrthoDB; 1170793at2; -.
DR   Proteomes; UP000034166; 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:UP000034166}.
FT   DOMAIN          9..88
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          244..376
FT                   /note="Acyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08028"
SQ   SEQUENCE   398 AA;  43776 MW;  306C1FBDA32A72E7 CRC64;
     MTSIAVETAT DLVEKARSFA PRLRERAKET DELRRIPEAT IKELKETGLF HILRPKRFGG
     YEADMKTYTK CVAEVSRGCG STGWVYGLCC IRELMISESF SEKTHLEIYG SGEDVLFAGV
     FEPRKIKVQK VEGGYIIEEG FWPFCSGSLH ATWGYFGMPI VDEKGNHVDQ GLITVPMSQV
     EIADDWNVVG LKGTGSNSVY MNGVFVPDHR VVSFTDAIHG KFQSSHFRDI PLYNTALFPA
     LAMSLAVPAL GMAQAALEFF MKVLPNRKAA NLGVEQLSEA ASTHNQVAEV SLKIEAAELL
     FHKVADNLDT WAGSGEYMPK PERVKSLATL GYAVQICKEA IDLILLASGS AIVAQGHPLQ
     RISADFSALY THRTISPITS KENYGRVLCA LDSNTKNI
//
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