ACDC_MYCBO
ID ACDC_MYCBO Reviewed; 388 AA.
AC Q7U0Y2; A0A1R3XWZ6; X2BGF7;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Acyl-CoA dehydrogenase fadE12;
DE EC=1.3.99.-;
GN Name=fadE12; OrderedLocusNames=BQ2027_MB0997C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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 -!- MISCELLANEOUS: Maximum activity is obtained with n-octanol-CoA.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; LT708304; SIT99596.1; -; Genomic_DNA.
DR RefSeq; NP_854654.1; NC_002945.3.
DR RefSeq; WP_010950473.1; NC_002945.4.
DR AlphaFoldDB; Q7U0Y2; -.
DR SMR; Q7U0Y2; -.
DR EnsemblBacteria; SIT99596; SIT99596; BQ2027_MB0997C.
DR PATRIC; fig|233413.5.peg.1086; -.
DR OMA; MMQKAAT; -.
DR Proteomes; UP000001419; 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..388
FT /note="Acyl-CoA dehydrogenase fadE12"
FT /id="PRO_0000201184"
SQ SEQUENCE 388 AA; 41524 MW; A57E5AD6F1B74384 CRC64;
MTDTSFIESE ERQALRKAVA SWVANYGHEY YLDKARKHEH TSELWAEAGK LGFLGVNLPE
EYGGGGAGMY ELSLVMEEMA AAGSALLLMV VSPAINGTII AKFGTDDQKK RWLPGIADGS
LTMAFAITEP DAGSNSHKIT TTARRDGSDW IIKGQKVFIS GIDQAQAVLV VGRSEEAKTG
KLRPALFVVP TDAPGFSYTP IEMELVSPER QFQVFLDDVR LPADALVGAE DAAIAHLFAG
LNPERIMGAA SAVGMGRFAL GRAVDYVKTR KVWSTPIGAH QGLAHPLAQC HIEVELAKLM
TQKAATLYDH GDDFGAAEAA NMAKYAAAEA SSRAVDQAVQ SMGGNGLTKE YGVAAMMTSA
RLARIAPISR EMVLNFVAQT SLGLPRSY