ID   ATOA_ECOLI              Reviewed;         216 AA.
AC   P76459; P94762;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   02-SEP-2026, entry version 155.
DE   RecName: Full=Acetate CoA-transferase subunit beta {ECO:0000305};
DE            EC=2.8.3.8 {ECO:0000269|PubMed:1103739, ECO:0000269|PubMed:1103741, ECO:0000269|PubMed:3025185};
DE   AltName: Full=Acetoacetyl-CoA transferase subunit beta {ECO:0000303|PubMed:3025185};
DE            Short=AA-CoA transferase subunit beta {ECO:0000303|PubMed:3025185};
DE   AltName: Full=Acetyl-CoA:acetoacetate CoA-transferase subunit beta {ECO:0000303|PubMed:1103739};
GN   Name=atoA {ECO:0000303|PubMed:3025185};
GN   OrderedLocusNames=b2222, JW2216;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; 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).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=1103739; DOI=10.1016/0003-9861(75)90002-8;
RA   Sramek S.J., Frerman F.E.;
RT   "Purification and properties of Escherichia coli coenzyme A-transferase.";
RL   Arch. Biochem. Biophys. 171:14-26(1975).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RX   PubMed=1103741; DOI=10.1016/0003-9861(75)90003-x;
RA   Sramek S.J., Frerman F.E.;
RT   "Escherichia coli coenzyme A-transferase: kinetics, catalytic pathway and
RT   structure.";
RL   Arch. Biochem. Biophys. 171:27-35(1975).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC   STRAIN=K12;
RX   PubMed=3025185; DOI=10.1128/jb.169.1.42-52.1987;
RA   Jenkins L.S., Nunn W.D.;
RT   "Genetic and molecular characterization of the genes involved in short-
RT   chain fatty acid degradation in Escherichia coli: the ato system.";
RL   J. Bacteriol. 169:42-52(1987).
RN   [7]
RP   INDUCTION.
RC   STRAIN=K12;
RX   PubMed=2883171; DOI=10.1128/jb.169.5.2096-2102.1987;
RA   Jenkins L.S., Nunn W.D.;
RT   "Regulation of the ato operon by the atoC gene in Escherichia coli.";
RL   J. Bacteriol. 169:2096-2102(1987).
RN   [8] {ECO:0007744|PDB:5DBN}
RP   X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS), AND SUBUNIT.
RA   Arbing M.A., Koo C.W., Shin A., Medrano-Soto A., Eisenberg D.;
RT   "Crystal structure of AtoDA complex.";
RL   Submitted (AUG-2015) to the PDB data bank.
CC   -!- FUNCTION: Coenzyme A transferase which is involved in short-chain fatty
CC       acid degradation and catalyzes the activation of short-chain fatty
CC       acids to their respective CoA thiolesters (PubMed:1103739,
CC       PubMed:3025185). During acetoacetate degradation, catalyzes the
CC       transfer of CoA from acetyl-CoA to acetoacetate by a mechanism
CC       involving a covalent enzyme-CoA compound as a reaction intermediate
CC       (PubMed:1103741). Utilizes a variety of short chain acyl-CoA and
CC       carboxylic acid substrates but exhibits maximal activity with normal
CC       and 3-keto substrates (PubMed:1103739). {ECO:0000269|PubMed:1103739,
CC       ECO:0000269|PubMed:1103741, ECO:0000269|PubMed:3025185}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an acyl-CoA + acetate = a carboxylate + acetyl-CoA;
CC         Xref=Rhea:RHEA:13381, ChEBI:CHEBI:29067, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:58342; EC=2.8.3.8;
CC         Evidence={ECO:0000269|PubMed:1103739, ECO:0000269|PubMed:1103741,
CC         ECO:0000269|PubMed:3025185};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetoacetate + acetyl-CoA = acetoacetyl-CoA + acetate;
CC         Xref=Rhea:RHEA:27806, ChEBI:CHEBI:13705, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:57286, ChEBI:CHEBI:57288;
CC         Evidence={ECO:0000269|PubMed:1103739, ECO:0000269|PubMed:1103741,
CC         ECO:0000269|PubMed:3025185};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=butanoate + acetyl-CoA = butanoyl-CoA + acetate;
CC         Xref=Rhea:RHEA:30071, ChEBI:CHEBI:17968, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:57371;
CC         Evidence={ECO:0000269|PubMed:1103739};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetoacetate + butanoyl-CoA = acetoacetyl-CoA + butanoate;
CC         Xref=Rhea:RHEA:12961, ChEBI:CHEBI:13705, ChEBI:CHEBI:17968,
CC         ChEBI:CHEBI:57286, ChEBI:CHEBI:57371;
CC         Evidence={ECO:0000269|PubMed:1103739};
CC   -!- ACTIVITY REGULATION: Inhibited by p-chloromercuribenzoate.
CC       {ECO:0000269|PubMed:1103739}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.26 mM for acetyl-CoA (for acetoacetyl-CoA formation)
CC         {ECO:0000269|PubMed:1103741};
CC         KM=0.035 mM for acetoacetyl-CoA (for acetyl-CoA formation)
CC         {ECO:0000269|PubMed:1103741};
CC   -!- PATHWAY: Lipid metabolism; short-chain fatty acid metabolism.
CC       {ECO:0000305|PubMed:3025185}.
CC   -!- SUBUNIT: Heterotetramer composed of two alpha subunits (AtoD) and two
CC       beta subunits (AtoA). {ECO:0000269|PubMed:1103739, ECO:0000269|Ref.8,
CC       ECO:0000305|PubMed:3025185}.
CC   -!- INTERACTION:
CC       P76459; P0AC02: bamD; NbExp=2; IntAct=EBI-1128061, EBI-1128087;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1103739}.
CC       Note=Membrane associated. {ECO:0000269|PubMed:1103739}.
CC   -!- INDUCTION: Transcriptionally regulated by the regulatory protein AtoC.
CC       {ECO:0000269|PubMed:2883171}.
CC   -!- DISRUPTION PHENOTYPE: Mutant lacks acetoacetyl-CoA transferase
CC       activity. {ECO:0000269|PubMed:3025185}.
CC   -!- SIMILARITY: Belongs to the 3-oxoacid CoA-transferase subunit B family.
CC       {ECO:0000305}.
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DR   EMBL; U00096; AAC75282.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16018.1; -; Genomic_DNA.
DR   PIR; D64992; D64992.
DR   RefSeq; NP_416726.1; NC_000913.3.
DR   RefSeq; WP_000339065.1; NZ_CP009789.1.
DR   PDB; 5DBN; X-ray; 2.55 A; B/D/F/H=1-216.
DR   AlphaFoldDB; P76459; -.
DR   SMR; P76459; -.
DR   BioGRID; 4262987; 11.
DR   BioGRID; 851060; 1.
DR   FunCoup; P76459; 410.
DR   IntAct; P76459; 4.
DR   STRING; 511145.b2222; -.
DR   PaxDb; 511145-b2222; -.
DR   EnsemblBacteria; AAC75282; AAC75282; b2222.
DR   GeneID; 946719; -.
DR   KEGG; ecj:JW2216; -.
DR   KEGG; eco:b2222; -.
DR   KEGG; ecoc:C3026_12420; -.
DR   PATRIC; fig|1411691.4.peg.13; -.
DR   EchoBASE; EB1621; -.
DR   eggNOG; COG2057; Bacteria.
DR   HOGENOM; CLU_019942_4_1_6; -.
DR   InParanoid; P76459; -.
DR   OMA; VAMMHTN; -.
DR   OrthoDB; 9778604at2; -.
DR   PhylomeDB; P76459; -.
DR   BioCyc; EcoCyc:ATOA-MONOMER; -.
DR   BioCyc; MetaCyc:ATOA-MONOMER; -.
DR   UniPathway; UPA00656; -.
DR   PRO; PR:P76459; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P76459; -.
DR   GO; GO:0005737; C:cytoplasm; EXP:UniProtKB.
DR   GO; GO:0008775; F:acetate CoA-transferase activity; IMP:EcoliWiki.
DR   GO; GO:0047371; F:butyrate-acetoacetate CoA-transferase activity; EXP:UniProtKB.
DR   GO; GO:0046459; P:short-chain fatty acid metabolic process; IEA:UniProtKB-UniPathway.
DR   FunFam; 3.40.1080.10:FF:000001; Succinyl-coa:3-ketoacid-coenzyme a transferase subunit b; 1.
DR   Gene3D; 3.40.1080.10; Glutaconate Coenzyme A-transferase; 1.
DR   InterPro; IPR012791; 3-oxoacid_CoA-transf_B.
DR   InterPro; IPR004165; CoA_trans_fam_I.
DR   InterPro; IPR004164; CoA_transf_AS.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   NCBIfam; TIGR02428; pcaJ_scoB_fam; 1.
DR   PANTHER; PTHR13707; KETOACID-COENZYME A TRANSFERASE; 1.
DR   PANTHER; PTHR13707:SF57; SUCCINYL-COA:3-KETOACID COENZYME A TRANSFERASE SUBUNIT B-RELATED; 1.
DR   Pfam; PF01144; CoA_trans; 1.
DR   SMART; SM00882; CoA_trans; 1.
DR   SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
DR   PROSITE; PS01274; COA_TRANSF_2; 1.
DR   PDBsum; 5DBN; -.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Fatty acid metabolism; Lipid metabolism;
KW   Reference proteome; Transferase.
FT   CHAIN           1..216
FT                   /note="Acetate CoA-transferase subunit beta"
FT                   /id="PRO_0000157915"
FT   ACT_SITE        46
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10034"
FT   HELIX           3..12
FT                   /evidence="ECO:0007829|PDB:5DBN"
FT   STRAND          20..23
FT                   /evidence="ECO:0007829|PDB:5DBN"
FT   HELIX           27..33
FT                   /evidence="ECO:0007829|PDB:5DBN"
FT   STRAND          42..45
FT                   /evidence="ECO:0007829|PDB:5DBN"
FT   TURN            46..48
FT                   /evidence="ECO:0007829|PDB:5DBN"
FT   STRAND          49..53
FT                   /evidence="ECO:0007829|PDB:5DBN"
FT   STRAND          71..78
FT                   /evidence="ECO:0007829|PDB:5DBN"
FT   HELIX           81..89
FT                   /evidence="ECO:0007829|PDB:5DBN"
FT   STRAND          94..98
FT                   /evidence="ECO:0007829|PDB:5DBN"
FT   STRAND          101..104
FT                   /evidence="ECO:0007829|PDB:5DBN"
FT   HELIX           125..131
FT                   /evidence="ECO:0007829|PDB:5DBN"
FT   STRAND          133..138
FT                   /evidence="ECO:0007829|PDB:5DBN"
FT   STRAND          148..153
FT                   /evidence="ECO:0007829|PDB:5DBN"
FT   STRAND          159..162
FT                   /evidence="ECO:0007829|PDB:5DBN"
FT   STRAND          166..168
FT                   /evidence="ECO:0007829|PDB:5DBN"
FT   STRAND          170..177
FT                   /evidence="ECO:0007829|PDB:5DBN"
FT   STRAND          180..186
FT                   /evidence="ECO:0007829|PDB:5DBN"
FT   HELIX           192..197
FT                   /evidence="ECO:0007829|PDB:5DBN"
FT   TURN            207..210
FT                   /evidence="ECO:0007829|PDB:5DBN"
SQ   SEQUENCE   216 AA;  22960 MW;  3F3916D024614BAE CRC64;
     MDAKQRIARR VAQELRDGDI VNLGIGLPTM VANYLPEGIH ITLQSENGFL GLGPVTTAHP
     DLVNAGGQPC GVLPGAAMFD SAMSFALIRG GHIDACVLGG LQVDEEANLA NWVVPGKMVP
     GMGGAMDLVT GSRKVIIAME HCAKDGSAKI LRRCTMPLTA QHAVHMLVTE LAVFRFIDGK
     MWLTEIADGC DLATVRAKTE ARFEVAADLN TQRGDL
//