ID   ACDC_MYCTO              Reviewed;         388 AA.
AC   P9WQG2; L0T5G1; P71539;
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=Acyl-CoA dehydrogenase fadE12;
DE            EC=1.3.99.-;
GN   Name=fadE12; OrderedLocusNames=MT1000;
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; AAK45249.1; -; Genomic_DNA.
DR   PIR; B70719; B70719.
DR   RefSeq; WP_003898667.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WQG2; -.
DR   SMR; P9WQG2; -.
DR   EnsemblBacteria; AAK45249; AAK45249; MT1000.
DR   KEGG; mtc:MT1000; -.
DR   PATRIC; fig|83331.31.peg.1072; -.
DR   HOGENOM; CLU_018204_0_2_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   Gene3D; 1.10.540.10; -; 1.
DR   Gene3D; 2.40.110.10; -; 1.
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.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Oxidoreductase.
FT   CHAIN           1..388
FT                   /note="Acyl-CoA dehydrogenase fadE12"
FT                   /id="PRO_0000426781"
SQ   SEQUENCE   388 AA;  41515 MW;  7F9DAF7778B75B15 CRC64;
     MTDTSFIESE ERQALRKAVA SWVANYGHEY YLDKARKHEH TSELWAEAGK LGFLGVNLPE
     EYGGGGAGMY ELSLVMEEMA AAGSALLLMV VSPAINGTII AKFGTDDQKK RWLPGIADGS
     LTMAFAITEP DAGSNSHKIT TTARRDGSDW IIKGQKVFIS GIDQAQAVLV VGRSEEAKTG
     KLRPALFVVP TDAPGFSYTP IEMELVSPER QFQVFLDDVR LPADALVGAE DAAIAQLFAG
     LNPERIMGAA SAVGMGRFAL GRAVDYVKTR KVWSTPIGAH QGLAHPLAQC HIEVELAKLM
     TQKAATLYDH GDDFGAAEAA NMAKYAAAEA SSRAVDQAVQ SMGGNGLTKE YGVAAMMTSA
     RLARIAPISR EMVLNFVAQT SLGLPRSY