FADE_ECOLI
ID FADE_ECOLI Reviewed; 814 AA.
AC Q47146; P71283; P75673; Q47680;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Acyl-coenzyme A dehydrogenase {ECO:0000303|PubMed:12057976};
DE Short=ACDH;
DE Short=Acyl-CoA dehydrogenase {ECO:0000303|PubMed:12057976};
DE EC=1.3.8.7 {ECO:0000305|PubMed:12057976};
DE EC=1.3.8.8 {ECO:0000305|PubMed:12057976};
GN Name=fadE {ECO:0000303|PubMed:12057976}; Synonyms=yafH;
GN OrderedLocusNames=b0221, JW5020;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0
RT - 6.0 min (189,987 - 281,416bp) region.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-315.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=7596361; DOI=10.1016/0165-7992(95)90024-1;
RA Ohmori H., Hatada E., Qiao Y., Tsuji M., Fukuda R.;
RT "dinP, a new gene in Escherichia coli, whose product shows similarities to
RT UmuC and its homologues.";
RL Mutat. Res. 347:1-7(1995).
RN [6]
RP FUNCTION, PATHWAY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12057976; DOI=10.1128/jb.184.13.3759-3764.2002;
RA Campbell J.W., Cronan J.E. Jr.;
RT "The enigmatic Escherichia coli fadE gene is yafH.";
RL J. Bacteriol. 184:3759-3764(2002).
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 E.coli to utilize dodecanoate or
CC oleate as the sole carbon and energy source for growth.
CC {ECO:0000269|PubMed:12057976}.
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:0000305|PubMed:12057976};
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:0000305|PubMed:12057976};
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:0000269|PubMed:12057976}.
CC -!- INDUCTION: Transcription of fadE is negatively regulated by FadR.
CC Induced in the presence of fatty acids, in a FadR-dependent manner.
CC {ECO:0000269|PubMed:12057976}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow on
CC octanoate, decanoate, dodecanoate, or oleate as the sole carbon and
CC energy source, but grow well on acetate, while the wild-type strain can
CC grow on acetate, dodecanoate, and oleate.
CC {ECO:0000269|PubMed:12057976}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally named fadF. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA07583.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U70214; AAB08643.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73325.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA77891.2; -; Genomic_DNA.
DR EMBL; D38582; BAA07583.1; ALT_INIT; Genomic_DNA.
DR PIR; F64746; F64746.
DR RefSeq; NP_414756.2; NC_000913.3.
DR RefSeq; WP_000973083.1; NZ_SSZK01000029.1.
DR AlphaFoldDB; Q47146; -.
DR SMR; Q47146; -.
DR BioGRID; 4259770; 205.
DR STRING; 511145.b0221; -.
DR jPOST; Q47146; -.
DR PaxDb; Q47146; -.
DR PRIDE; Q47146; -.
DR EnsemblBacteria; AAC73325; AAC73325; b0221.
DR EnsemblBacteria; BAA77891; BAA77891; BAA77891.
DR GeneID; 949007; -.
DR KEGG; ecj:JW5020; -.
DR KEGG; eco:b0221; -.
DR PATRIC; fig|1411691.4.peg.2062; -.
DR EchoBASE; EB2939; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_012192_0_0_6; -.
DR InParanoid; Q47146; -.
DR OMA; SAYAHSQ; -.
DR PhylomeDB; Q47146; -.
DR BioCyc; EcoCyc:ACYLCOADEHYDROG-MON; -.
DR BioCyc; MetaCyc:ACYLCOADEHYDROG-MON; -.
DR UniPathway; UPA00659; -.
DR PRO; PR:Q47146; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoCyc.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IDA:EcoCyc.
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; IMP:EcoCyc.
DR GO; GO:0009062; P:fatty acid catabolic process; IMP:EcoCyc.
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 2: Evidence at transcript level;
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_0000201200"
FT ACT_SITE 497
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P15651"
SQ SEQUENCE 814 AA; 89224 MW; AD9E40ACB44CF781 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 RGKDVFVPID YIIGGPKMAG
QGWRMLVECL SVGRGITLPS NSTGGVKSVA LATGAYAHIR RQFKISIGKM EGIEEPLARI
AGNAYVMDAA ASLITYGIML GEKPAVLSAI VKYHCTHRGQ QSIIDAMDIT GGKGIMLGQS
NFLARAYQGA PIAITVEGAN ILTRSMMIFG QGAIRCHPYV LEEMEAAKNN DVNAFDKLLF
KHIGHVGSNK VRSFWLGLTR GLTSSTPTGD ATKRYYQHLN RLSANLALLS DVSMAVLGGS
LKRRERISAR LGDILSQLYL ASAVLKRYDD EGRNEADLPL VHWGVQDALY QAEQAMDDLL
QNFPNRVVAG LLNVVIFPTG RHYLAPSDKL DHKVAKILQV PNATRSRIGR GQYLTPSEHN
PVGLLEEALV DVIAADPIHQ RICKELGKNL PFTRLDELAH NALVKGLIDK DEAAILVKAE
ESRLRSINVD DFDPEELATK PVKLPEKVRK VEAA
