ID   FADE_YERPE              Reviewed;         815 AA.
AC   Q8ZBY6; Q0WC42;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Acyl-coenzyme A dehydrogenase {ECO:0000250|UniProtKB:Q8ZRJ7};
DE            Short=ACDH {ECO:0000250|UniProtKB:Q8ZRJ7};
DE            Short=Acyl-CoA dehydrogenase {ECO:0000250|UniProtKB:Q8ZRJ7};
DE            EC=1.3.8.7 {ECO:0000250|UniProtKB:Q8ZRJ7};
DE            EC=1.3.8.8 {ECO:0000250|UniProtKB:Q8ZRJ7};
GN   Name=fadE; OrderedLocusNames=YPO3244, y0946, YP_0688;
OS   Yersinia pestis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO-92 / Biovar Orientalis;
RX   PubMed=11586360; DOI=10.1038/35097083;
RA   Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA   Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA   Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA   Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA   Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA   Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA   Stevens K., Whitehead S., Barrell B.G.;
RT   "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL   Nature 413:523-527(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIM10+ / Biovar Mediaevalis;
RX   PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA   Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA   Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA   Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA   Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT   "Genome sequence of Yersinia pestis KIM.";
RL   J. Bacteriol. 184:4601-4611(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=91001 / Biovar Mediaevalis;
RX   PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA   Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA   Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA   Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA   Wang J., Huang P., Yang R.;
RT   "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT   avirulent to humans.";
RL   DNA Res. 11:179-197(2004).
CC   -!- FUNCTION: Catalyzes the dehydrogenation of acyl-coenzymes A (acyl-CoAs)
CC       to 2-enoyl-CoAs, the first step of the beta-oxidation cycle of fatty
CC       acid degradation. Is required for the utilization of medium- and long-
CC       chain fatty acids as sole carbon sources for growth.
CC       {ECO:0000250|UniProtKB:Q8ZRJ7}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a medium-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized
CC         [electron-transfer flavoprotein] = a medium-chain (2E)-enoyl-CoA +
CC         reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:14477,
CC         Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:83723,
CC         ChEBI:CHEBI:83726; EC=1.3.8.7;
CC         Evidence={ECO:0000250|UniProtKB:Q8ZRJ7};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a long-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized
CC         [electron-transfer flavoprotein] = a long-chain (2E)-enoyl-CoA +
CC         reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:17721,
CC         Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:83721,
CC         ChEBI:CHEBI:83727; EC=1.3.8.8;
CC         Evidence={ECO:0000250|UniProtKB:Q8ZRJ7};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P15651};
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000250|UniProtKB:Q8ZRJ7}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AL590842; CAL21838.1; -; Genomic_DNA.
DR   EMBL; AE009952; AAM84527.1; -; Genomic_DNA.
DR   EMBL; AE017042; AAS60954.1; -; Genomic_DNA.
DR   PIR; AC0394; AC0394.
DR   RefSeq; WP_002214691.1; NZ_WUCM01000034.1.
DR   RefSeq; YP_002348146.1; NC_003143.1.
DR   AlphaFoldDB; Q8ZBY6; -.
DR   SMR; Q8ZBY6; -.
DR   IntAct; Q8ZBY6; 1.
DR   STRING; 214092.YPO3244; -.
DR   PaxDb; Q8ZBY6; -.
DR   DNASU; 1145893; -.
DR   EnsemblBacteria; AAM84527; AAM84527; y0946.
DR   EnsemblBacteria; AAS60954; AAS60954; YP_0688.
DR   GeneID; 57975475; -.
DR   KEGG; ype:YPO3244; -.
DR   KEGG; ypk:y0946; -.
DR   KEGG; ypm:YP_0688; -.
DR   PATRIC; fig|214092.21.peg.3705; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_012192_0_0_6; -.
DR   OMA; SAYAHSQ; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000000815; Chromosome.
DR   Proteomes; UP000001019; Chromosome.
DR   Proteomes; UP000002490; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004466; F:long-chain-acyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
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; 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   InterPro; IPR015396; DUF1974.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR   Pfam; PF09317; DUF1974; 1.
DR   SUPFAM; SSF47203; SSF47203; 1.
DR   SUPFAM; SSF56645; SSF56645; 1.
PE   3: Inferred from homology;
KW   FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..815
FT                   /note="Acyl-coenzyme A dehydrogenase"
FT                   /id="PRO_0000201204"
FT   ACT_SITE        497
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P15651"
SQ   SEQUENCE   815 AA;  88968 MW;  C0CCCDB8A0C4CCC5 CRC64;
     MIVLSIIALL VLISVLFYHR VNLYLSSLIL LVYTAALSAS QLWSFWVLLP LVIMLLPLIL
     TPLRKSLFSA PALRIFRSVM PAMSRTEKEA IDAGTTWWEG DLFRGAPDWK KLHNYPKPQL
     TAEEQAFIDG PVEEACRMAN DFQITHELAD LPPELWDYLK EKRFFAMIIK KEYGGLEFSA
     YAQARVLQKL AGVSGILAIT VGVPNSLGPG ELLQHYGTEE QKNHYLPRLA RGDEIPCFAL
     TSPEAGSDAG AIPDVGIVCM GEWQGKQVLG MRLTWNKRYI TLAPIATVLG LAFKLSDPEH
     LLGDTVDLGI TCALIPTHTP GVEIGHRHFP LNIPFQNGPT RGNDIFVPID YIIGGPQMAG
     QGWRMLVECL SVGRGITLPS NATGSLKSVA MGIGAYAYIR RQFKISIGKM EGIEEPLARI
     AGNTYVMDAA ATLITSGIMM GEKPAVLSAI VKYHCTHRGQ RAVMDAMDIA GGKGICLGPA
     NFVARGYQGA PIGITVEGAN ILTRSMIIFG QGAIRCHPFV LDEMAAAQSN DVAAFDKALF
     GHLGHVGSSM VRSFWLGLTN GRTSATPVKD STRRYYQQLN RLSANLALLS DVSMGVLGGS
     LKRRERISAR LGDILSQLYL ASATLKRYED EGRQKEDLPL VHWGVQDALY QAEQALDDLL
     RNFPNSVIAG LMRVVVFPLG RVHRAPSDHL DHQLAQLLQV PSATRSRIGR GQYLTPSEFN
     PVGLLEAALL DVIAAEPIHK RLSKEAGKSL PFTRLDQLAK HALAEGKISA EEAALLTKAE
     NSRLRSINVD EFDASALAAN PVVKKPAKQQ QTEAA