ID   ACDA_BACSU              Reviewed;         379 AA.
AC   P45867;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Acyl-CoA dehydrogenase;
DE            EC=1.3.99.-;
GN   Name=acdA; Synonyms=acd; OrderedLocusNames=BSU37170;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9353933; DOI=10.1099/00221287-143-10-3313;
RA   Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V.,
RA   Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G.,
RA   Kunst F., Danchin A., Glaser P.;
RT   "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334
RT   degrees).";
RL   Microbiology 143:3313-3328(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   GENE NAME, AND INDUCTION.
RC   STRAIN=168;
RX   PubMed=17189250; DOI=10.1074/jbc.m606831200;
RA   Matsuoka H., Hirooka K., Fujita Y.;
RT   "Organization and function of the YsiA regulon of Bacillus subtilis
RT   involved in fatty acid degradation.";
RL   J. Biol. Chem. 282:5180-5194(2007).
CC   -!- FUNCTION: Involved in the degradation of long-chain fatty acids.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + a 2,3-saturated acyl-CoA = a 2,3-dehydroacyl-CoA + AH2;
CC         Xref=Rhea:RHEA:48608, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:60015, ChEBI:CHEBI:65111;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC   -!- INDUCTION: Repressed by FadR in the absence of LCFAs (fatty acids of
CC       14-20 carbon atoms). When LCFAs are present in the medium, they are
CC       converted to long-chain acyl-CoAs, which antagonize FadR as to its
CC       binding to fadR boxes on target DNA and thus derepress transcription.
CC       {ECO:0000269|PubMed:17189250}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; Z49782; CAA89868.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15745.1; -; Genomic_DNA.
DR   PIR; S55421; S55421.
DR   RefSeq; NP_391598.1; NC_000964.3.
DR   RefSeq; WP_003242719.1; NZ_JNCM01000034.1.
DR   AlphaFoldDB; P45867; -.
DR   SMR; P45867; -.
DR   STRING; 224308.BSU37170; -.
DR   PaxDb; P45867; -.
DR   PRIDE; P45867; -.
DR   EnsemblBacteria; CAB15745; CAB15745; BSU_37170.
DR   GeneID; 938457; -.
DR   KEGG; bsu:BSU37170; -.
DR   PATRIC; fig|224308.179.peg.4027; -.
DR   eggNOG; COG1960; Bacteria.
DR   InParanoid; P45867; -.
DR   OMA; RDVKLNQ; -.
DR   PhylomeDB; P45867; -.
DR   BioCyc; BSUB:BSU37170-MON; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.540.10; -; 1.
DR   Gene3D; 2.40.110.10; -; 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.
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   SUPFAM; SSF47203; SSF47203; 1.
DR   SUPFAM; SSF56645; SSF56645; 1.
DR   PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE   2: Evidence at transcript level;
KW   FAD; Fatty acid metabolism; Flavoprotein; Lipid degradation;
KW   Lipid metabolism; Oxidoreductase; Reference proteome.
FT   CHAIN           1..379
FT                   /note="Acyl-CoA dehydrogenase"
FT                   /id="PRO_0000201182"
SQ   SEQUENCE   379 AA;  41446 MW;  4D09861D59718EF9 CRC64;
     MNFSLSEEHE MIRKLVRDFA KHEVAPTAAE RDEQERFDRE LFREMANLGL TGIPWPEDYG
     GIGSDYLAYV IAVEELSKVC ASTGVTLSAH ISLCSWPLFA FGTEEQKTEY LTQLALGEKI
     GAFALTEAGS GSDAGSMKTT AERIGDDYVL NGSKVFITNG GVADIYIVFA VTDPEKKKKG
     VTAFIVEKDF EGFFTGKKEK KLGIRSSPTT EIMFEDCVVP ASKRLGEEGE GFKIAMKTLD
     GGRNGIAAQA VGIAQGALDA ALQYAKERKQ FGKSIAEQQG IAFKLADMAT MIEASRLLTY
     QAAWLESSGL PYGKASAMSK LMAGDTAMKV TTEAVQIFGG YGYTKDYPVE RYMRDAKITQ
     IYEGTQEIQR LVISRMLAD