(data stored in ACNUC7421 zone)

SWISSPROT: FADE_ECO57

ID   FADE_ECO57              Reviewed;         814 AA.
AC   Q8X7R2;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-2002, sequence version 2.
DT   05-JUL-2017, entry version 88.
DE   RecName: Full=Acyl-coenzyme A dehydrogenase;
DE            Short=ACDH;
DE            EC=1.3.99.-;
GN   Name=fadE; OrderedLocusNames=Z0278, ECs0248;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Catalyzes the dehydrogenation of acyl-CoA.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: An acyl-CoA + FAD = a dehydrogenated acyl-CoA
CC       + FADH(2).
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG54546.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAB33671.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AE005174; AAG54546.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BA000007; BAB33671.1; ALT_INIT; Genomic_DNA.
DR   PIR; F85510; F85510.
DR   PIR; H90659; H90659.
DR   RefSeq; NP_308275.2; NC_002695.1.
DR   RefSeq; WP_000973071.1; NZ_MWVM01000023.1.
DR   ProteinModelPortal; Q8X7R2; -.
DR   STRING; 155864.Z0278; -.
DR   PRIDE; Q8X7R2; -.
DR   EnsemblBacteria; AAG54546; AAG54546; Z0278.
DR   EnsemblBacteria; BAB33671; BAB33671; BAB33671.
DR   GeneID; 914334; -.
DR   KEGG; ece:Z0278; -.
DR   KEGG; ecs:ECs0248; -.
DR   PATRIC; fig|386585.9.peg.348; -.
DR   eggNOG; ENOG4107QPN; Bacteria.
DR   eggNOG; COG1960; LUCA.
DR   HOGENOM; HOG000274434; -.
DR   KO; K06445; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IEA:InterPro.
DR   Gene3D; 1.10.540.10; -; 1.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR013786; AcylCoA_DH/ox_N.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR   InterPro; IPR015396; DUF1974.
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   Pfam; PF09317; DUF1974; 1.
DR   SUPFAM; SSF47203; SSF47203; 1.
DR   SUPFAM; SSF56645; SSF56645; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q8X7R2.
DR   SWISS-2DPAGE; Q8X7R2.
KW   Complete proteome; FAD; Fatty acid metabolism; Flavoprotein;
KW   Lipid metabolism; Oxidoreductase.
FT   CHAIN         1    814       Acyl-coenzyme A dehydrogenase.
FT                                /FTId=PRO_0000201201.
SQ   SEQUENCE   814 AA;  89181 MW;  BBE2AA441B01C080 CRC64;
     MMILSILATV VLLGALFYHR VSLFISSLIL LAWTAALGVA GLWSAWVLVP LAIILVPFNF
     APMRKSMISA PVFRGFRKVM PPMSRTEKEA IDAGTTWWEG DLFQGKPDWK KLHNYPQPRL
     TAEEQAFLDG PVEEACRMAN DFQITHELAD LPPELWAYLK EHRFFAMIIK KEYGGLEFSA
     YAQSRVLQKL SGVSGILAIT VGVPNSLGPG ELLQHYGTDE QKDHYLPRLA RGQEIPCFAL
     TSPEAGSDAG AIPDTGIVCM GEWQGQQVLG MRLTWNKRYI TLAPIATVLG LAFKLSDPEK
     LLGGAEDLGI TCALIPTTTP GVEIGRRHFP LNVPFQNGPT LGKDVFVPID YIIGGPKMAG
     QGWRMLVECL SVGRGITLPS NSTGGVKSVA LATGAYAHIR RQFKISIGKM EGIEEPLARI
     AGNAYVMDAA ASLITYGIML GEKPAVLSAI VKYHCTHRGQ QSIIDAMDIT GGKGIMLGQS
     NFLARAYQGA PIAITVEGAN ILTRSMMIFG QGAIRCHPYV LEEMEAAKNN DVNVFDKLLF
     KHIGHVGSNK VRSFWLGLTR GLTSSTPTGD ATKRYYQHLN RLSANLALLS DVSMAVLGGS
     LKRRERISAR LGDILSQLYL ASAVLKRYDD EGRNEADLPL VHWGVQDALY QAEQAMDDLL
     QNFPNRVVAG LLNVVIFPTG RHYLAPSDKL DHKVAKILQV PNATRSRIGR GQYLTPSEHN
     PVGLLEEALV DVIAADPIHQ RICKELGKNL PFTRLDELAH NALAKGLIDK DEAAILVKAE
     ESRLRSINVD DFDPEELATK PVKLPEKVRK VEAA
//

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