FADI_ECOLI
ID FADI_ECOLI Reviewed; 436 AA.
AC P76503; P77208; P77230; Q6KCX1;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=3-ketoacyl-CoA thiolase FadI;
DE EC=2.3.1.16 {ECO:0000269|PubMed:12270828};
DE AltName: Full=ACSs;
DE AltName: Full=Acetyl-CoA acyltransferase;
DE AltName: Full=Acyl-CoA ligase;
DE AltName: Full=Beta-ketothiolase;
DE AltName: Full=Fatty acid oxidation complex subunit beta;
GN Name=fadI; Synonyms=yfcY; OrderedLocusNames=b2342, JW2339;
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;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
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 [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=12270828; DOI=10.1128/jb.184.20.5696-5705.2002;
RA Snell K.D., Feng F., Zhong L., Martin D., Madison L.L.;
RT "YfcX enables medium-chain-length poly(3-hydroxyalkanoate) formation from
RT fatty acids in recombinant Escherichia coli fadB strains.";
RL J. Bacteriol. 184:5696-5705(2002).
RN [5]
RP FUNCTION IN ANAEROBIC BETA-OXIDATION PATHWAY.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=12535077; DOI=10.1046/j.1365-2958.2003.03341.x;
RA Campbell J.W., Morgan-Kiss R.M., Cronan J.E. Jr.;
RT "A new Escherichia coli metabolic competency: growth on fatty acids by a
RT novel anaerobic beta-oxidation pathway.";
RL Mol. Microbiol. 47:793-805(2003).
CC -!- FUNCTION: Catalyzes the final step of fatty acid oxidation in which
CC acetyl-CoA is released and the CoA ester of a fatty acid two carbons
CC shorter is formed. Strongly involved in the anaerobic degradation of
CC long and medium-chain fatty acids in the presence of nitrate and weakly
CC involved in the aerobic degradation of long-chain fatty acids.
CC {ECO:0000269|PubMed:12270828, ECO:0000269|PubMed:12535077}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA;
CC Xref=Rhea:RHEA:21564, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:58342, ChEBI:CHEBI:90726; EC=2.3.1.16;
CC Evidence={ECO:0000269|PubMed:12270828};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000305|PubMed:12270828}.
CC -!- SUBUNIT: Heterotetramer of two alpha chains (FadJ) and two beta chains
CC (FadI). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Unlike the aerobic pathway, the anaerobic pathway is not
CC strongly repressed by FadR regulatory protein.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U00096; AAC75402.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16197.2; -; Genomic_DNA.
DR PIR; D65007; D65007.
DR RefSeq; NP_416844.1; NC_000913.3.
DR RefSeq; WP_000531952.1; NZ_LN832404.1.
DR AlphaFoldDB; P76503; -.
DR SASBDB; P76503; -.
DR SMR; P76503; -.
DR BioGRID; 4260534; 173.
DR ComplexPortal; CPX-3966; fadJI fatty acid oxidation complex, anaerobic conditions.
DR DIP; DIP-11991N; -.
DR IntAct; P76503; 12.
DR STRING; 511145.b2342; -.
DR jPOST; P76503; -.
DR PaxDb; P76503; -.
DR PRIDE; P76503; -.
DR EnsemblBacteria; AAC75402; AAC75402; b2342.
DR EnsemblBacteria; BAA16197; BAA16197; BAA16197.
DR GeneID; 948823; -.
DR KEGG; ecj:JW2339; -.
DR KEGG; eco:b2342; -.
DR PATRIC; fig|1411691.4.peg.4390; -.
DR EchoBASE; EB3880; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_2_0_6; -.
DR InParanoid; P76503; -.
DR OMA; MTAFPEP; -.
DR PhylomeDB; P76503; -.
DR BioCyc; EcoCyc:G7213-MON; -.
DR BioCyc; MetaCyc:G7213-MON; -.
DR UniPathway; UPA00659; -.
DR PRO; PR:P76503; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0036125; C:fatty acid beta-oxidation multienzyme complex; IDA:ComplexPortal.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IDA:EcoliWiki.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IDA:EcoliWiki.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IDA:EcoliWiki.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IDA:ComplexPortal.
DR GO; GO:0033542; P:fatty acid beta-oxidation, unsaturated, even number; IMP:EcoliWiki.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR HAMAP; MF_01618; FadI; 1.
DR InterPro; IPR012806; Ac-CoA_C-AcTrfase_FadI.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR InterPro; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1.
DR TIGRFAMs; TIGR02446; FadI; 1.
DR PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Fatty acid metabolism; Lipid degradation;
KW Lipid metabolism; Reference proteome; Transferase.
FT CHAIN 1..436
FT /note="3-ketoacyl-CoA thiolase FadI"
FT /id="PRO_0000206437"
FT ACT_SITE 99
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 392
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 422
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
SQ SEQUENCE 436 AA; 46531 MW; 5B89853172C16299 CRC64;
MGQVLPLVTR QGDRIAIVSG LRTPFARQAT AFHGIPAVDL GKMVVGELLA RSEIPAEVIE
QLVFGQVVQM PEAPNIAREI VLGTGMNVHT DAYSVSRACA TSFQAVANVA ESLMAGTIRA
GIAGGADSSS VLPIGVSKKL ARVLVDVNKA RTMSQRLKLF SRLRLRDLMP VPPAVAEYST
GLRMGDTAEQ MAKTYGITRE QQDALAHRSH QRAAQAWSDG KLKEEVMTAF IPPYKQPLVE
DNNIRGNSSL ADYAKLRPAF DRKHGTVTAA NSTPLTDGAA AVILMTESRA KELGLVPLGY
LRSYAFTAID VWQDMLLGPA WSTPLALERA GLTMSDLTLI DMHEAFAAQT LANIQLLGSE
RFAREALGRA HATGEVDDSK FNVLGGSIAY GHPFAATGAR MITQTLHELR RRGGGFGLVT
ACAAGGLGAA MVLEAE
