ID   Y873_MYCTU              Reviewed;         650 AA.
AC   P9WQF7; 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 40.
DE   RecName: Full=Probable acyl-CoA dehydrogenase FadE10;
DE            EC=1.3.-.-;
GN   Name=fadE10; OrderedLocusNames=Rv0873; ORFNames=MTCY31.01, MTV043.66;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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; AL123456; CCP43621.1; -; Genomic_DNA.
DR   PIR; A70817; A70817.
DR   RefSeq; NP_215388.1; NC_000962.3.
DR   RefSeq; WP_003898626.1; NZ_NVQJ01000001.1.
DR   AlphaFoldDB; P9WQF7; -.
DR   SMR; P9WQF7; -.
DR   STRING; 83332.Rv0873; -.
DR   PaxDb; P9WQF7; -.
DR   DNASU; 885636; -.
DR   GeneID; 885636; -.
DR   KEGG; mtu:Rv0873; -.
DR   TubercuList; Rv0873; -.
DR   eggNOG; COG1960; Bacteria.
DR   OMA; NAFMGLR; -.
DR   PhylomeDB; P9WQF7; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR   GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IBA:GO_Central.
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   1: Evidence at protein level;
KW   FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT   CHAIN           1..650
FT                   /note="Probable acyl-CoA dehydrogenase FadE10"
FT                   /id="PRO_0000201209"
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