ID   ACDC_MYCTU              Reviewed;         388 AA.
AC   P9WQG3; L0T5G1; P71539;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Acyl-CoA dehydrogenase FadE12;
DE            EC=1.3.99.- {ECO:0000269|PubMed:9535763};
DE   AltName: Full=Medium chain acyl-CoA dehydrogenase {ECO:0000303|PubMed:9535763};
DE            Short=MCADH {ECO:0000303|PubMed:9535763};
GN   Name=fadE12; OrderedLocusNames=Rv0972c; ORFNames=MTCY10D7.02;
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   FUNCTION AS AN ACYL-COA DEHYDROGENASE, CATALYTIC ACTIVITY, AND SUBSTRATE
RP   SPECIFICITY.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9535763; DOI=10.1006/bbrc.1998.8354;
RA   Mahadevan U., Padmanaban G.;
RT   "Cloning and expression of an acyl-CoA dehydrogenase from Mycobacterium
RT   tuberculosis.";
RL   Biochem. Biophys. Res. Commun. 244:893-897(1998).
RN   [3]
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   -!- FUNCTION: Has acyl-CoA dehydrogenase activity on a number of
CC       substrates. N-octanoyl-CoA is the best tested, but n-lauroyl-CoA, n-
CC       palmitoyl-CoA and isovaleryl-CoA were also used.
CC       {ECO:0000269|PubMed:9535763}.
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         Evidence={ECO:0000269|PubMed:9535763};
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; CCP43721.1; -; Genomic_DNA.
DR   PIR; B70719; B70719.
DR   RefSeq; NP_215487.1; NC_000962.3.
DR   RefSeq; WP_003898667.1; NZ_NVQJ01000001.1.
DR   AlphaFoldDB; P9WQG3; -.
DR   SMR; P9WQG3; -.
DR   STRING; 83332.Rv0972c; -.
DR   PaxDb; P9WQG3; -.
DR   DNASU; 885237; -.
DR   GeneID; 885237; -.
DR   KEGG; mtu:Rv0972c; -.
DR   TubercuList; Rv0972c; -.
DR   eggNOG; COG1960; Bacteria.
DR   OMA; MMQKAAT; -.
DR   PhylomeDB; P9WQG3; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IDA:MTBBASE.
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..388
FT                   /note="Acyl-CoA dehydrogenase FadE12"
FT                   /id="PRO_0000201185"
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