ID   FADE_BACSU              Reviewed;         594 AA.
AC   O32176;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Probable acyl-CoA dehydrogenase;
DE            EC=1.3.99.-;
GN   Name=fadE; Synonyms=yusJ; OrderedLocusNames=BSU32820;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
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   [2]
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; AL009126; CAB15271.1; -; Genomic_DNA.
DR   PIR; C70021; C70021.
DR   RefSeq; NP_391161.1; NC_000964.3.
DR   RefSeq; WP_003244094.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; O32176; -.
DR   SMR; O32176; -.
DR   STRING; 224308.BSU32820; -.
DR   jPOST; O32176; -.
DR   PaxDb; O32176; -.
DR   PRIDE; O32176; -.
DR   EnsemblBacteria; CAB15271; CAB15271; BSU_32820.
DR   GeneID; 936717; -.
DR   KEGG; bsu:BSU32820; -.
DR   PATRIC; fig|224308.179.peg.3556; -.
DR   eggNOG; COG1960; Bacteria.
DR   InParanoid; O32176; -.
DR   OMA; TRQVFFN; -.
DR   PhylomeDB; O32176; -.
DR   BioCyc; BSUB:BSU32820-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..594
FT                   /note="Probable acyl-CoA dehydrogenase"
FT                   /id="PRO_0000360672"
FT   ACT_SITE        405
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   594 AA;  65336 MW;  F59BED1AA0D903CE CRC64;
     MAKKAADVQK GGGFLIEDVT YDQMYTPEDF TDEHKMIAKT TEDYIEQDVL PHIDDIENHQ
     FEHSVRLLKK AGELGLLGAD VPEEYGGLGL DKISSALITE KFSRAGSFSL SYGAHVGIGS
     LPIVFFGSEE QKKKYLPGLA SGEKIAAYAL TEPGSGSDAL GAKTTAVLNE AGTHYVLTGE
     KQWITNSAFA DVFVVYAKVD GDKFSAFIVE KEFPGVSTGP EEKKMGIKGS STRTLILDQA
     EVPKENLLGE IGKGHVIAFN ILNIGRYKLA VGTIGASKRV IELSAAYANQ RRQFKTPIAG
     FSLTQEKIGT MASRLYAMES SVYRTVGLFE DNMSQFTAED LKDGRQIAKS IAEYAIECSL
     NKVFGSETLD YIVDEGVQIH GGYGFMQEYE VERAYRDSRI NRIFEGTNEI NRLIVPSTFL
     KKALKGELPL FEKAQSLQEE LMMLMPEEPG SGVLEQEKYI VKQAKKIALF AAGLAAQKYG
     KAIDREQEIL VNVADIVSNV YAMESAVLRT EKAIAAQGAE KAAQKVLYTE IFVQEAFNEI
     EAHAKESLIA MEEGDSLRMM LSALRKLTRV TPKNVIQKKR EAAAGIFEAE KYTV