ID   ACDP_MYCTU              Reviewed;         389 AA.
AC   P9WQG1; 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 43.
DE   RecName: Full=Probable acyl-CoA dehydrogenase FadE25;
DE            EC=1.3.99.-;
GN   Name=fadE25; Synonyms=acd; OrderedLocusNames=Rv3274c; ORFNames=MTCY71.14c;
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;
CC         Evidence={ECO:0000250|UniProtKB:Q2LQN9};
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AL123456; CCP46093.1; -; Genomic_DNA.
DR   PIR; C70979; C70979.
DR   RefSeq; NP_217791.1; NC_000962.3.
DR   RefSeq; WP_003417122.1; NZ_NVQJ01000003.1.
DR   AlphaFoldDB; P9WQG1; -.
DR   SMR; P9WQG1; -.
DR   STRING; 83332.Rv3274c; -.
DR   PaxDb; P9WQG1; -.
DR   DNASU; 888731; -.
DR   GeneID; 888731; -.
DR   KEGG; mtu:Rv3274c; -.
DR   TubercuList; Rv3274c; -.
DR   eggNOG; COG1960; Bacteria.
DR   OMA; NMATWML; -.
DR   PhylomeDB; P9WQG1; -.
DR   Proteomes; UP000001584; Chromosome.
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   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   1: Evidence at protein level;
KW   FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT   CHAIN           1..389
FT                   /note="Probable acyl-CoA dehydrogenase FadE25"
FT                   /id="PRO_0000201188"
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