ID   YDIF_ECOLI              Reviewed;         531 AA.
AC   P37766; P76199; P76898;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 3.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Acetate CoA-transferase YdiF {ECO:0000250|UniProtKB:Q8X5X6};
DE            EC=2.8.3.8 {ECO:0000250|UniProtKB:Q8X5X6};
DE   AltName: Full=Short-chain acyl-CoA:acetate CoA-transferase;
GN   Name=ydiF; OrderedLocusNames=b1694, JW1684;
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=9097039; DOI=10.1093/dnares/3.6.363;
RA   Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA   Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA   Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA   Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA   Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 28.0-40.1 min region on the linkage map.";
RL   DNA Res. 3:363-377(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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64.
RX   PubMed=3541912; DOI=10.1042/bj2380475;
RA   Duncan K., Chaudhuri S., Campbell M.S., Coggins J.R.;
RT   "The overexpression and complete amino acid sequence of Escherichia coli 3-
RT   dehydroquinase.";
RL   Biochem. J. 238:475-483(1986).
RN   [5]
RP   IDENTIFICATION.
RX   PubMed=7984428; DOI=10.1093/nar/22.22.4756;
RA   Borodovsky M., Rudd K.E., Koonin E.V.;
RT   "Intrinsic and extrinsic approaches for detecting genes in a bacterial
RT   genome.";
RL   Nucleic Acids Res. 22:4756-4767(1994).
CC   -!- FUNCTION: CoA transferase having broad substrate specificity for short-
CC       chain acyl-CoA thioesters with the activity decreasing when the length
CC       of the carboxylic acid chain exceeds four carbons. May play a role in
CC       short-chain fatty acid metabolism in E.coli.
CC       {ECO:0000250|UniProtKB:Q8X5X6}.
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:0000250|UniProtKB:Q8X5X6};
CC   -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000250|UniProtKB:Q8X5X6}.
CC   -!- MISCELLANEOUS: Formation of the covalent enzyme-CoA thioester
CC       intermediate proceeds via an unstable anhydride species formed between
CC       the carboxylate group of the catalytic glutamate of the enzyme and the
CC       carbonyl carbon of the thioester linkage of the substrate.
CC       {ECO:0000250|UniProtKB:Q8X5X6}.
CC   -!- SIMILARITY: Belongs to the 3-oxoacid CoA-transferase family.
CC       {ECO:0000305}.
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DR   EMBL; U00096; AAC74764.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15447.2; -; Genomic_DNA.
DR   EMBL; X04306; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; F64927; F64927.
DR   RefSeq; NP_416209.1; NC_000913.3.
DR   RefSeq; WP_000805700.1; NZ_SSZK01000001.1.
DR   AlphaFoldDB; P37766; -.
DR   SMR; P37766; -.
DR   BioGRID; 4260290; 22.
DR   BioGRID; 850571; 1.
DR   IntAct; P37766; 2.
DR   STRING; 511145.b1694; -.
DR   PaxDb; P37766; -.
DR   PRIDE; P37766; -.
DR   DNASU; 946211; -.
DR   EnsemblBacteria; AAC74764; AAC74764; b1694.
DR   EnsemblBacteria; BAA15447; BAA15447; BAA15447.
DR   GeneID; 946211; -.
DR   KEGG; ecj:JW1684; -.
DR   KEGG; eco:b1694; -.
DR   PATRIC; fig|1411691.4.peg.564; -.
DR   EchoBASE; EB2328; -.
DR   eggNOG; COG4670; Bacteria.
DR   HOGENOM; CLU_026774_4_0_6; -.
DR   InParanoid; P37766; -.
DR   OMA; GTDYNKR; -.
DR   PhylomeDB; P37766; -.
DR   BioCyc; EcoCyc:EG12432-MON; -.
DR   PRO; PR:P37766; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0008775; F:acetate CoA-transferase activity; ISS:UniProtKB.
DR   GO; GO:0046952; P:ketone body catabolic process; IEA:InterPro.
DR   GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR   GO; GO:0046459; P:short-chain fatty acid metabolic process; ISS:UniProtKB.
DR   InterPro; IPR014388; 3-oxoacid_CoA-transferase.
DR   InterPro; IPR004165; CoA_trans_fam_I.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   Pfam; PF01144; CoA_trans; 1.
DR   PIRSF; PIRSF000858; SCOT-t; 1.
DR   SMART; SM00882; CoA_trans; 1.
DR   SUPFAM; SSF100950; SSF100950; 2.
PE   3: Inferred from homology;
KW   Reference proteome; Transferase.
FT   CHAIN           1..531
FT                   /note="Acetate CoA-transferase YdiF"
FT                   /id="PRO_0000168990"
FT   ACT_SITE        333
FT                   /note="5-glutamyl coenzyme A thioester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8X5X6"
SQ   SEQUENCE   531 AA;  57562 MW;  E07A0D445015030D CRC64;
     MKPVKPPRIN GRVPVLSAQE AVNYIPDEAT LCVLGAGGGI LEATTLITAL ADKYKQTQTP
     RNLSIISPTG LGDRADRGIS PLAQEGLVKW ALCGHWGQSP RISELAEQNK IIAYNYPQGV
     LTQTLRAAAA HQPGIISDIG IGTFVDPRQQ GGKLNEVTKE DLIKLVEFDN KEYLYYKAIA
     PDIAFIRATT CDSEGYATFE DEVMYLDALV IAQAVHNNGG IVMMQVQKMV KKATLHPKSV
     RIPGYLVDIV VVDPDQTQLY GGAPVNRFIS GDFTLDDSTK LSLPLNQRKL VARRALFEMR
     KGAVGNVGVG IADGIGLVAR EEGCADDFIL TVETGPIGGI TSQGIAFGAN VNTRAILDMT
     SQFDFYHGGG LDVCYLSFAE VDQHGNVGVH KFNGKIMGTG GFIDISATSK KIIFCGTLTA
     GSLKTEITDG KLNIVQEGRV KKFIRELPEI TFSGKIALER GLDVRYITER AVFTLKEDGL
     HLIEIAPGVD LQKDILDKMD FTPVISPELK LMDERLFIDA AMGFVLPEAA H