Y897_MYCBO
ID Y897_MYCBO Reviewed; 650 AA.
AC P63430; A0A1R3XX23; O53885; Q10535; X2BGE3;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Probable acyl-CoA dehydrogenase FadE10;
DE EC=1.3.-.-;
GN Name=fadE10; OrderedLocusNames=BQ2027_MB0897;
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 -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; LT708304; SIT99495.1; -; Genomic_DNA.
DR RefSeq; NP_854554.1; NC_002945.3.
DR RefSeq; WP_003898626.1; NC_002945.4.
DR AlphaFoldDB; P63430; -.
DR SMR; P63430; -.
DR EnsemblBacteria; SIT99495; SIT99495; BQ2027_MB0897.
DR PATRIC; fig|233413.5.peg.976; -.
DR OMA; NAFMGLR; -.
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..650
FT /note="Probable acyl-CoA dehydrogenase FadE10"
FT /id="PRO_0000201210"
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