ID A0A1T5IBF0_9CLOT Unreviewed; 379 AA.
AC A0A1T5IBF0;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Butyryl-CoA dehydrogenase {ECO:0000313|EMBL:SKC36302.1};
GN ORFNames=SAMN02194393_00142 {ECO:0000313|EMBL:SKC36302.1};
OS Maledivibacter halophilus.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Maledivibacter.
OX NCBI_TaxID=36842 {ECO:0000313|EMBL:SKC36302.1, ECO:0000313|Proteomes:UP000190285};
RN [1] {ECO:0000313|EMBL:SKC36302.1, ECO:0000313|Proteomes:UP000190285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1 {ECO:0000313|EMBL:SKC36302.1,
RC ECO:0000313|Proteomes:UP000190285};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU362125};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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DR EMBL; FUZT01000001; SKC36302.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5IBF0; -.
DR STRING; 36842.SAMN02194393_00142; -.
DR OrthoDB; 9802447at2; -.
DR Proteomes; UP000190285; Unassembled WGS sequence.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR CDD; cd01158; SCAD_SBCAD; 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; IPR006089; Acyl-CoA_DH_CS.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_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; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR PIRSF; PIRSF016578; HsaA; 2.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362125};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU362125};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000190285}.
FT DOMAIN 7..118
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 122..217
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 229..376
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 379 AA; 42105 MW; 059CED2579B3F257 CRC64;
MDFNLPKEHL LAKKMFKEFA ENEVKPLAAE IDEEERFPEE TVEKLVKYGF MGIPMPKEYG
GQGADTLAYV MSVEEIAKVC LTTTTIYTAH TSLCSYPISK YGTNEQKEKY LKPLCRGERL
GAFGLTEPGA GSDAAMQTTT AVLKDDHYVL NGSKIFITNS GYADTYIIIA MTDKSKGTRG
CSAFIVESNF PGFSVGKKEK KMGIRGSTAC ELIFDNCIVP KENLLGKEGQ GFKIAMKALD
VGRIGIAAQA LGLAEGAFEE TCNYVKERKQ FGRSISKFQN TKFELADMRM KLEAAQLMVY
KVARLKDEGK PFTVNAAMAK LYCSQLSSEI TTRCLQLFGG YGYTREYPIE RMMRDARITE
IYEGTSEVQK MVIAGSLKL
//
