ID   ACDP_MYCLE     STANDARD;      PRT;   389 AA.
AC   P46703;
DT   01-NOV-1995 (Rel. 32, Created)
DT   01-NOV-1995 (Rel. 32, Last sequence update)
DT   25-OCT-2004 (Rel. 45, Last annotation update)
DE   Probable acyl-CoA dehydrogenase fadE25 (EC 1.3.99.-).
GN   Name=fadE25; Synonyms=acd; OrderedLocusNames=ML0737;
GN   ORFNames=B1308_F1_34;
OS   Mycobacterium leprae.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX   NCBI_TaxID=1769;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=96084954; PubMed=7489918; DOI=10.1016/0378-1119(95)00427-8;
RA   Doukhan L., Predich M., Nair G., Dussurget O., Mandic-Mulec I.,
RA   Cole S.T., Smith D.R., Smith I.;
RT   "Genomic organization of the mycobacterial sigma gene cluster.";
RL   Gene 165:67-70(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   MEDLINE=21128732; PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; U00012; AAA85936.1; -.
DR   EMBL; AL583919; CAC30246.1; -.
DR   PIR; B87001; B87001.
DR   HSSP; P15651; 1JQI.
DR   Leproma; ML0737; -.
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; Hypothetical protein;
KW   Oxidoreductase.
SQ   SEQUENCE   389 AA;  41719 MW;  EFC80CDB3ED884B1 CRC64;
     MVGWSGNPLF DLFKLPEEHN ELRATIRALA EKEIAPHAAD VDQRARFPEE ALAALNASGF
     NAIHVPEEYG GQGADSVAAC IVIEEVARVD ASASLIPAVN KLGTMGLILR GSEELKKQVL
     PSLAAEGAMA SYALSEREAG SDAASMRTRA KADGDDWILN GFKCWITNGG KSTWYTVMAV
     TDPDKGANGI SAFIVHKDDE GFSIGPKEKK LGIKGSPTTE LYFDKCRIPG DRIIGEPGTG
     FKTALATLDH TRPTIGAQAV GIAQGALDAA IVYTKDRKQF GESISTFQSI QFMLADMAMK
     VEAARLIVYA AAARAERGEP DLGFISAASK CFASDIAMEV TTDAVQLFGG AGYTSDFPVE
     RFMRDAKITQ IYEGTNQIQR VVMSRALLR
//