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ACDP_MYCTO
ID   ACDP_MYCTO              Reviewed;         389 AA.
AC   P9WQG0; L0TCB5; P63427; P96879;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=Probable acyl-CoA dehydrogenase fadE25;
DE            EC=1.3.99.-;
GN   Name=fadE25; Synonyms=acd; OrderedLocusNames=MT3374;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK47715.1; -; Genomic_DNA.
DR   PIR; C70979; C70979.
DR   RefSeq; WP_003417122.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WQG0; -.
DR   SMR; P9WQG0; -.
DR   PRIDE; P9WQG0; -.
DR   EnsemblBacteria; AAK47715; AAK47715; MT3374.
DR   KEGG; mtc:MT3374; -.
DR   PATRIC; fig|83331.31.peg.3631; -.
DR   HOGENOM; CLU_018204_0_2_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
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   3: Inferred from homology;
KW   FAD; Flavoprotein; Oxidoreductase.
FT   CHAIN           1..389
FT                   /note="Probable acyl-CoA dehydrogenase fadE25"
FT                   /id="PRO_0000426782"
SQ   SEQUENCE   389 AA;  41723 MW;  2E77D0F28A9C8E08 CRC64;
     MVGWAGNPSF DLFKLPEEHD EMRSAIRALA EKEIAPHAAE VDEKARFPEE ALVALNSSGF
     NAVHIPEEYG GQGADSVATC IVIEEVARVD ASASLIPAVN KLGTMGLILR GSEELKKQVL
     PALAAEGAMA SYALSEREAG SDAASMRTRA KADGDHWILN GAKCWITNGG KSTWYTVMAV
     TDPDRGANGI SAFMVHKDDE GFTVGPKERK LGIKGSPTTE LYFENCRIPG DRIIGEPGTG
     FKTALATLDH TRPTIGAQAV GIAQGALDAA IAYTKDRKQF GESISTFQAV QFMLADMAMK
     VEAARLMVYS AAARAERGEP DLGFISAASK CFASDVAMEV TTDAVQLFGG AGYTTDFPVE
     RFMRDAKITQ IYEGTNQIQR VVMSRALLR
 
 
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