ID   ACDB_BACSU     STANDARD;      PRT;   378 AA.
AC   P45857;
DT   01-NOV-1995 (Rel. 32, Created)
DT   10-OCT-2003 (Rel. 42, Last sequence update)
DT   01-FEB-2005 (Rel. 46, Last annotation update)
DE   Acyl-CoA dehydrogenase (EC 1.3.99.-).
GN   Name=mmgC; OrderedLocusNames=BSU24150;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=168 / MB24;
RX   MEDLINE=96326319; PubMed=8759838;
RA   Bryan E.M., Beall B.W., Moran C.P. Jr.;
RT   "A sigma E dependent operon subject to catabolite repression during
RT   sporulation in Bacillus subtilis.";
RL   J. Bacteriol. 178:4778-4786(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=168 / JH642;
RX   MEDLINE=97124195; PubMed=8969508;
RA   Mizuno M., Masuda S., Takemaru K.-I., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of
RT   the Bacillus subtilis genome containing the skin element and many
RT   sporulation genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.K., Codani J.J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Dusterhoft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   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.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   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).
CC   -!- CATALYTIC ACTIVITY: Acyl-CoA + ETF = 2,3-dehydroacyl-CoA + reduced
CC       ETF.
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
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CC   --------------------------------------------------------------------------
DR   EMBL; U29084; AAB09615.1; -.
DR   EMBL; D84432; BAA12589.1; -.
DR   EMBL; Z99116; CAB14346.1; -.
DR   PIR; D69658; D69658.
DR   HSSP; Q06319; 1BUC.
DR   SubtiList; BG11321; mmgC.
DR   InterPro; IPR006089; Acyl-CoA_dh.
DR   InterPro; IPR006090; Acyl-CoA_dh_C.
DR   InterPro; IPR006091; Acyl-CoA_dh_M.
DR   InterPro; IPR006092; Acyl-CoA_dh_N.
DR   InterPro; IPR009100; AcylCoA_dehyd_NM.
DR   InterPro; IPR009075; AcylCoADH_C_like.
DR   Pfam; PF00441; Acyl-CoA_dh; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR   PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 1.
KW   Complete proteome; FAD; Flavoprotein; Oxidoreductase.
FT   CONFLICT     97     97       L -> M (in Ref. 1).
FT   CONFLICT    171    171       A -> D (in Ref. 1).
FT   CONFLICT    328    328       A -> AA (in Ref. 1).
SQ   SEQUENCE   378 AA;  40870 MW;  BDCCB0CA2301EDB5 CRC64;
     MHVTQEQVMM RKMVRDFARK EIAPAAEIME KTDEFPFQLI KKMGKHGLMG IPVPEQYGGA
     GADVVSYILA IHEISRISAA VGVILSVHTS VGTNPILYFG NEEQKMKYIP NLASGDHLGA
     FALTEPHSGS DAGSLRTTAI KKNGKYLLNG SKIFITNGGA ADIYITFALT APDQGRHGIS
     AFIVEKNTPG FTVGKKERKL GLYGSNTTEL IFDNAEVPEA NLLGKEGDGF HIAMANLNVG
     RIGIAAQALG IAEAALEHAV DYAKQRVQFG RPIAANQGIS FKLADMATRA EAARHLVYHA
     ADLHNRGLNC GKEASMAKQF ASDAAVKALD AVQIYGGYGY MKDYPVERLL RDAKVTQIYE
     GTNEIQRLII SKYLLGGT
//