ACDP_MYCTO
ID ACDP_MYCTO Reviewed; 389 AA.
AC P9WQG0; 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 38.
DE RecName: Full=Probable acyl-CoA dehydrogenase fadE25;
DE EC=1.3.99.-;
GN Name=fadE25; Synonyms=acd; OrderedLocusNames=MT3374;
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; AAK47715.1; -; Genomic_DNA.
DR PIR; C70979; C70979.
DR RefSeq; WP_003417122.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WQG0; -.
DR SMR; P9WQG0; -.
DR PRIDE; P9WQG0; -.
DR EnsemblBacteria; AAK47715; AAK47715; MT3374.
DR KEGG; mtc:MT3374; -.
DR PATRIC; fig|83331.31.peg.3631; -.
DR HOGENOM; CLU_018204_0_2_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
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 3: Inferred from homology;
KW FAD; Flavoprotein; Oxidoreductase.
FT CHAIN 1..389
FT /note="Probable acyl-CoA dehydrogenase fadE25"
FT /id="PRO_0000426782"
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