ATOD_ECOLI
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 03-AUG-2022, entry version 151.
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}; OrderedLocusNames=b2221, JW2215;
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).
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; P76458; -.
DR PRIDE; P76458; -.
DR EnsemblBacteria; AAC75281; AAC75281; b2221.
DR EnsemblBacteria; BAA16017; BAA16017; BAA16017.
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; CGTTEYG; -.
DR PhylomeDB; P76458; -.
DR BioCyc; EcoCyc:ATOD-MON; -.
DR BioCyc; MetaCyc:ATOD-MON; -.
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:0008775; F:acetate CoA-transferase activity; IEA:UniProtKB-EC.
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 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 PANTHER; PTHR13707; PTHR13707; 1.
DR Pfam; PF01144; CoA_trans; 1.
DR SMART; SM00882; CoA_trans; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
DR TIGRFAMs; TIGR02429; pcaI_scoA_fam; 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
