ATOA_ECOLI
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 03-AUG-2022, entry version 139.
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}; OrderedLocusNames=b2222, JW2216;
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: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.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_SSZK01000030.1.
DR PDB; 5DBN; X-ray; 2.55 A; B/D/F/H=1-216.
DR PDBsum; 5DBN; -.
DR AlphaFoldDB; P76459; -.
DR SMR; P76459; -.
DR BioGRID; 4262987; 8.
DR BioGRID; 851060; 1.
DR IntAct; P76459; 4.
DR STRING; 511145.b2222; -.
DR PaxDb; P76459; -.
DR PRIDE; P76459; -.
DR EnsemblBacteria; AAC75282; AAC75282; b2222.
DR EnsemblBacteria; BAA16018; BAA16018; BAA16018.
DR GeneID; 58461276; -.
DR GeneID; 946719; -.
DR KEGG; ecj:JW2216; -.
DR KEGG; eco:b2222; -.
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; NWMVPGS; -.
DR PhylomeDB; P76459; -.
DR BioCyc; EcoCyc:ATOA-MON; -.
DR BioCyc; MetaCyc:ATOA-MON; -.
DR UniPathway; UPA00656; -.
DR PRO; PR:P76459; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0008775; F:acetate CoA-transferase activity; IMP:EcoliWiki.
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; 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 PANTHER; PTHR13707; PTHR13707; 1.
DR Pfam; PF01144; CoA_trans; 1.
DR SMART; SM00882; CoA_trans; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
DR TIGRFAMs; TIGR02428; pcaJ_scoB_fam; 1.
DR PROSITE; PS01274; COA_TRANSF_2; 1.
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
