ID   ATOD_ECOLI              Reviewed;         220 AA.
AC   P76458;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 159.
DE   RecName: Full=Acetate CoA-transferase subunit alpha {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 alpha {ECO:0000303|PubMed:3025185};
DE            Short=AA-CoA transferase subunit alpha {ECO:0000303|PubMed:3025185};
DE   AltName: Full=Acetyl-CoA:acetoacetyl-CoA transferase subunit alpha {ECO:0000303|PubMed:1103739};
GN   Name=atoD {ECO:0000303|PubMed:3025185};
GN   OrderedLocusNames=b2221, JW2215;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; 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).
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:1K6D}
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS).
RX   PubMed=12454473; DOI=10.1107/s0907444902017055;
RA   Korolev S., Koroleva O., Petterson K., Gu M., Collart F., Dementieva I.,
RA   Joachimiak A.;
RT   "Autotracing of Escherichia coli acetate CoA-transferase alpha-subunit
RT   structure using 3.4 A MAD and 1.9 A native data.";
RL   Acta Crystallogr. D 58:2116-2121(2002).
RN   [9] {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=acetate + an acyl-CoA = 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 = acetate + acetoacetyl-CoA;
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=acetyl-CoA + butanoate = acetate + butanoyl-CoA;
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.9,
CC       ECO:0000305|PubMed:3025185}.
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 A family.
CC       {ECO:0000305}.
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DR   EMBL; U00096; AAC75281.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16017.1; -; Genomic_DNA.
DR   PIR; C64992; C64992.
DR   RefSeq; NP_416725.1; NC_000913.3.
DR   RefSeq; WP_000850540.1; NZ_STEB01000002.1.
DR   PDB; 1K6D; X-ray; 1.90 A; A/B=1-220.
DR   PDB; 5DBN; X-ray; 2.55 A; A/C/E/G=1-220.
DR   PDBsum; 1K6D; -.
DR   PDBsum; 5DBN; -.
DR   AlphaFoldDB; P76458; -.
DR   SMR; P76458; -.
DR   BioGRID; 4259179; 16.
DR   DIP; DIP-9191N; -.
DR   IntAct; P76458; 3.
DR   STRING; 511145.b2221; -.
DR   PaxDb; 511145-b2221; -.
DR   EnsemblBacteria; AAC75281; AAC75281; b2221.
DR   GeneID; 75172349; -.
DR   GeneID; 947525; -.
DR   KEGG; ecj:JW2215; -.
DR   KEGG; eco:b2221; -.
DR   PATRIC; fig|1411691.4.peg.14; -.
DR   EchoBASE; EB1620; -.
DR   eggNOG; COG1788; Bacteria.
DR   HOGENOM; CLU_019942_2_1_6; -.
DR   InParanoid; P76458; -.
DR   OMA; AFFCPTA; -.
DR   OrthoDB; 9777193at2; -.
DR   PhylomeDB; P76458; -.
DR   BioCyc; EcoCyc:ATOD-MONOMER; -.
DR   BioCyc; MetaCyc:ATOD-MONOMER; -.
DR   BRENDA; 2.8.3.8; 2026.
DR   UniPathway; UPA00656; -.
DR   EvolutionaryTrace; P76458; -.
DR   PRO; PR:P76458; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008775; F:acetate CoA-transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047371; F:butyrate-acetoacetate CoA-transferase activity; IEA:RHEA.
DR   GO; GO:0008410; F:CoA-transferase activity; IBA:GO_Central.
DR   GO; GO:0046459; P:short-chain fatty acid metabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.1080.10; Glutaconate Coenzyme A-transferase; 1.
DR   InterPro; IPR012792; 3-oxoacid_CoA-transf_A.
DR   InterPro; IPR004165; CoA_trans_fam_I.
DR   InterPro; IPR004163; CoA_transf_BS.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   NCBIfam; TIGR02429; pcaI_scoA_fam; 1.
DR   PANTHER; PTHR13707; KETOACID-COENZYME A TRANSFERASE; 1.
DR   PANTHER; PTHR13707:SF23; SUCCINYL-COA:3-KETOACID-COENZYME A TRANSFERASE; 1.
DR   Pfam; PF01144; CoA_trans; 1.
DR   SMART; SM00882; CoA_trans; 1.
DR   SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
DR   PROSITE; PS01273; COA_TRANSF_1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Fatty acid metabolism; Lipid metabolism;
KW   Reference proteome; Transferase.
FT   CHAIN           1..220
FT                   /note="Acetate CoA-transferase subunit alpha"
FT                   /id="PRO_0000157904"
FT   BINDING         24..30
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255"
FT   STRAND          4..6
FT                   /evidence="ECO:0007829|PDB:1K6D"
FT   HELIX           8..11
FT                   /evidence="ECO:0007829|PDB:1K6D"
FT   HELIX           12..14
FT                   /evidence="ECO:0007829|PDB:1K6D"
FT   STRAND          20..23
FT                   /evidence="ECO:0007829|PDB:1K6D"
FT   HELIX           33..42
FT                   /evidence="ECO:0007829|PDB:1K6D"
FT   STRAND          46..50
FT                   /evidence="ECO:0007829|PDB:1K6D"
FT   HELIX           62..66
FT                   /evidence="ECO:0007829|PDB:1K6D"
FT   STRAND          70..77
FT                   /evidence="ECO:0007829|PDB:1K6D"
FT   HELIX           82..89
FT                   /evidence="ECO:0007829|PDB:1K6D"
FT   STRAND          92..97
FT                   /evidence="ECO:0007829|PDB:1K6D"
FT   HELIX           100..111
FT                   /evidence="ECO:0007829|PDB:1K6D"
FT   STRAND          116..120
FT                   /evidence="ECO:0007829|PDB:1K6D"
FT   TURN            121..124
FT                   /evidence="ECO:0007829|PDB:1K6D"
FT   HELIX           126..128
FT                   /evidence="ECO:0007829|PDB:5DBN"
FT   STRAND          133..136
FT                   /evidence="ECO:0007829|PDB:1K6D"
FT   STRAND          139..144
FT                   /evidence="ECO:0007829|PDB:1K6D"
FT   STRAND          149..160
FT                   /evidence="ECO:0007829|PDB:1K6D"
FT   HELIX           169..172
FT                   /evidence="ECO:0007829|PDB:1K6D"
FT   HELIX           175..181
FT                   /evidence="ECO:0007829|PDB:1K6D"
FT   STRAND          182..193
FT                   /evidence="ECO:0007829|PDB:1K6D"
FT   HELIX           200..202
FT                   /evidence="ECO:0007829|PDB:1K6D"
FT   HELIX           207..209
FT                   /evidence="ECO:0007829|PDB:1K6D"
FT   STRAND          212..214
FT                   /evidence="ECO:0007829|PDB:1K6D"
SQ   SEQUENCE   220 AA;  23526 MW;  D1DD69ECEBB2676D CRC64;
     MKTKLMTLQD ATGFFRDGMT IMVGGFMGIG TPSRLVEALL ESGVRDLTLI ANDTAFVDTG
     IGPLIVNGRV RKVIASHIGT NPETGRRMIS GEMDVVLVPQ GTLIEQIRCG GAGLGGFLTP
     TGVGTVVEEG KQTLTLDGKT WLLERPLRAD LALIRAHRCD TLGNLTYQLS ARNFNPLIAL
     AADITLVEPD ELVETGELQP DHIVTPGAVI DHIIVSQESK
//