ATOB_ECOLI
ID ATOB_ECOLI Reviewed; 394 AA.
AC P76461; P78176;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Acetyl-CoA acetyltransferase;
DE EC=2.3.1.9;
DE AltName: Full=Acetoacetyl-CoA thiolase;
GN Name=atoB; OrderedLocusNames=b2224, JW2218;
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=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
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].
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 acetyl-CoA = acetoacetyl-CoA + CoA; Xref=Rhea:RHEA:21036,
CC ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.9;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10020};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate
CC biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000305}.
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DR EMBL; U00096; AAC75284.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16020.1; -; Genomic_DNA.
DR PIR; F64992; F64992.
DR RefSeq; NP_416728.1; NC_000913.3.
DR RefSeq; WP_000786547.1; NZ_SSZK01000030.1.
DR PDB; 4WYS; X-ray; 2.10 A; A/B/C/D=1-393.
DR PDB; 5F0V; X-ray; 1.80 A; A/B/C/D=1-393.
DR PDB; 5F38; X-ray; 1.90 A; A=1-394, B/C=1-393, D=1-392.
DR PDBsum; 4WYS; -.
DR PDBsum; 5F0V; -.
DR PDBsum; 5F38; -.
DR AlphaFoldDB; P76461; -.
DR SMR; P76461; -.
DR BioGRID; 4263266; 10.
DR IntAct; P76461; 3.
DR STRING; 511145.b2224; -.
DR PaxDb; P76461; -.
DR PRIDE; P76461; -.
DR EnsemblBacteria; AAC75284; AAC75284; b2224.
DR EnsemblBacteria; BAA16020; BAA16020; BAA16020.
DR GeneID; 946727; -.
DR KEGG; ecj:JW2218; -.
DR KEGG; eco:b2224; -.
DR PATRIC; fig|1411691.4.peg.11; -.
DR EchoBASE; EB1623; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_0_0_6; -.
DR InParanoid; P76461; -.
DR OMA; MPEAYVI; -.
DR PhylomeDB; P76461; -.
DR BioCyc; EcoCyc:ACETYL-COA-ACETYLTRANSFER-MON; -.
DR BioCyc; MetaCyc:ACETYL-COA-ACETYLTRANSFER-MON; -.
DR BRENDA; 2.3.1.9; 2026.
DR UniPathway; UPA00058; UER00101.
DR PRO; PR:P76461; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0043442; P:acetoacetic acid catabolic process; IMP:EcoCyc.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 2.
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 PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytoplasm; Fatty acid metabolism;
KW Lipid metabolism; Reference proteome; Transferase.
FT CHAIN 1..394
FT /note="Acetyl-CoA acetyltransferase"
FT /id="PRO_0000206406"
FT ACT_SITE 88
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 349
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT ACT_SITE 379
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:5F0V"
FT TURN 20..23
FT /evidence="ECO:0007829|PDB:5F0V"
FT HELIX 26..41
FT /evidence="ECO:0007829|PDB:5F0V"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:5F0V"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:5F0V"
FT HELIX 65..72
FT /evidence="ECO:0007829|PDB:5F0V"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:5F0V"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:4WYS"
FT HELIX 90..103
FT /evidence="ECO:0007829|PDB:5F0V"
FT STRAND 108..118
FT /evidence="ECO:0007829|PDB:5F0V"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:5F0V"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:5F0V"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:5F0V"
FT HELIX 143..147
FT /evidence="ECO:0007829|PDB:5F0V"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:5F0V"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:5F0V"
FT HELIX 158..169
FT /evidence="ECO:0007829|PDB:5F0V"
FT HELIX 173..193
FT /evidence="ECO:0007829|PDB:5F0V"
FT TURN 194..199
FT /evidence="ECO:0007829|PDB:5F0V"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:5F0V"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:5F0V"
FT HELIX 226..231
FT /evidence="ECO:0007829|PDB:5F0V"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:5F38"
FT STRAND 251..261
FT /evidence="ECO:0007829|PDB:5F0V"
FT HELIX 262..267
FT /evidence="ECO:0007829|PDB:5F0V"
FT STRAND 274..283
FT /evidence="ECO:0007829|PDB:5F0V"
FT HELIX 286..291
FT /evidence="ECO:0007829|PDB:5F0V"
FT HELIX 293..303
FT /evidence="ECO:0007829|PDB:5F0V"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:5F0V"
FT STRAND 312..316
FT /evidence="ECO:0007829|PDB:5F0V"
FT HELIX 321..331
FT /evidence="ECO:0007829|PDB:5F0V"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:5F0V"
FT HELIX 344..347
FT /evidence="ECO:0007829|PDB:5F0V"
FT HELIX 351..368
FT /evidence="ECO:0007829|PDB:5F0V"
FT STRAND 372..380
FT /evidence="ECO:0007829|PDB:5F0V"
FT TURN 381..383
FT /evidence="ECO:0007829|PDB:5F0V"
FT STRAND 384..391
FT /evidence="ECO:0007829|PDB:5F0V"
SQ SEQUENCE 394 AA; 40352 MW; DE27C394C3E6BDFA CRC64;
MKNCVIVSAV RTAIGSFNGS LASTSAIDLG ATVIKAAIER AKIDSQHVDE VIMGNVLQAG
LGQNPARQAL LKSGLAETVC GFTVNKVCGS GLKSVALAAQ AIQAGQAQSI VAGGMENMSL
APYLLDAKAR SGYRLGDGQV YDVILRDGLM CATHGYHMGI TAENVAKEYG ITREMQDELA
LHSQRKAAAA IESGAFTAEI VPVNVVTRKK TFVFSQDEFP KANSTAEALG ALRPAFDKAG
TVTAGNASGI NDGAAALVIM EESAALAAGL TPLARIKSYA SGGVPPALMG MGPVPATQKA
LQLAGLQLAD IDLIEANEAF AAQFLAVGKN LGFDSEKVNV NGGAIALGHP IGASGARILV
TLLHAMQARD KTLGLATLCI GGGQGIAMVI ERLN
