ID   Y873_MYCTO              Reviewed;         650 AA.
AC   P9WQF6; L0T558; O53885; P63429; Q10535;
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 FadE10;
DE            EC=1.3.-.-;
GN   Name=fadE10; OrderedLocusNames=MT0896;
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; AAK45138.1; -; Genomic_DNA.
DR   PIR; A70817; A70817.
DR   RefSeq; WP_003898626.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WQF6; -.
DR   SMR; P9WQF6; -.
DR   EnsemblBacteria; AAK45138; AAK45138; MT0896.
DR   KEGG; mtc:MT0896; -.
DR   PATRIC; fig|83331.31.peg.962; -.
DR   HOGENOM; CLU_018204_11_1_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..650
FT                   /note="Probable acyl-CoA dehydrogenase FadE10"
FT                   /id="PRO_0000426784"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        422
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   650 AA;  70745 MW;  FECF934A3F01C0D1 CRC64;
     MAQQTQVTEE QARALAEESR ESGWDKPSFA KELFLGRFPL GLIHPFPKPS DAEEARTEAF
     LVKLREFLDT VDGSVIERAA QIPDEYVKGL AELGCFGLKI PSEYGGLNMS QVAYNRVLMM
     VTTVHSSLGA LLSAHQSIGV PEPLKLAGTA EQKRRFLPRC AAGAISAFLL TEPDVGSDPA
     RMASTATPID DGQAYELEGV KLWTTNGVVA DLLVVMARVP RSEGHRGGIS AFVVEADSPG
     ITVERRNKFM GLRGIENGVT RLHRVRVPKD NLIGREGDGL KIALTTLNAG RLSLPAIATG
     VAKQALKIAR EWSVERVQWG KPVGQHEAVA SKISFIAATN YALDAVVELS SQMADEGRND
     IRIEAALAKL WSSEMACLVG DELLQIRGGR GYETAESLAA RGERAVPVEQ MVRDLRINRI
     FEGSSEIMRL LIAREAVDAH LTAAGDLANP KADLRQKAAA AAGASGFYAK WLPKLVFGEG
     QLPTTYREFG ALATHLRFVE RSSRKLARNT FYGMARWQAS LEKKQGFLGR IVDIGAELFA
     ISAACVRAEA QRTADPVEGE QAYELAEAFC QQATLRVEAL FDALWSNTDS IDVRLANDVL
     EGRYTWLEQG ILDQSEGTGP WIASWEPGPS TEANLARRFL TVSPSSEAKL