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 03-AUG-2022, entry version 106.
DE RecName: Full=Acyl-coenzyme A dehydrogenase {ECO:0000250|UniProtKB:Q47146};
DE Short=ACDH;
DE Short=Acyl-CoA dehydrogenase {ECO:0000250|UniProtKB:Q47146};
DE EC=1.3.8.7 {ECO:0000250|UniProtKB:Q47146};
DE EC=1.3.8.8 {ECO:0000250|UniProtKB:Q47146};
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., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA 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., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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:Q47146}.
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:Q47146};
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:Q47146};
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:Q47146}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG54546.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB33671.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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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_SEKU01000036.1.
DR AlphaFoldDB; Q8X7R2; -.
DR SMR; Q8X7R2; -.
DR STRING; 155864.EDL933_0251; -.
DR PRIDE; Q8X7R2; -.
DR EnsemblBacteria; AAG54546; AAG54546; Z0278.
DR EnsemblBacteria; BAB33671; BAB33671; ECs_0248.
DR GeneID; 914334; -.
DR KEGG; ece:Z0278; -.
DR KEGG; ecs:ECs_0248; -.
DR PATRIC; fig|386585.9.peg.348; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_012192_0_0_6; -.
DR OMA; SAYAHSQ; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
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; 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 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;
KW FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..814
FT /note="Acyl-coenzyme A dehydrogenase"
FT /id="PRO_0000201201"
FT ACT_SITE 497
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P15651"
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
