ID B7MLL4_ECO45 Unreviewed; 513 AA.
AC B7MLL4;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Acetate CoA-transferase YdiF {ECO:0000256|PIRNR:PIRNR000858};
DE EC=2.8.3.8 {ECO:0000256|PIRNR:PIRNR000858};
GN OrderedLocusNames=ECS88_4795 {ECO:0000313|EMBL:CAR05944.1};
OS Escherichia coli O45:K1 (strain S88 / ExPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585035 {ECO:0000313|EMBL:CAR05944.1, ECO:0000313|Proteomes:UP000000747};
RN [1] {ECO:0000313|Proteomes:UP000000747}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S88 / ExPEC {ECO:0000313|Proteomes:UP000000747};
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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.
CC {ECO:0000256|PIRNR:PIRNR000858}.
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:0000256|PIRNR:PIRNR000858};
CC -!- SIMILARITY: Belongs to the 3-oxoacid CoA-transferase family.
CC {ECO:0000256|ARBA:ARBA00007154, ECO:0000256|PIRNR:PIRNR000858}.
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DR EMBL; CU928161; CAR05944.1; -; Genomic_DNA.
DR RefSeq; WP_001228960.1; NC_011742.1.
DR AlphaFoldDB; B7MLL4; -.
DR KEGG; ecz:ECS88_4795; -.
DR HOGENOM; CLU_026774_4_0_6; -.
DR Proteomes; UP000000747; Chromosome.
DR GO; GO:0008775; F:acetate CoA-transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046952; P:ketone body catabolic process; IEA:InterPro.
DR Gene3D; 3.40.1080.10; Glutaconate Coenzyme A-transferase; 2.
DR InterPro; IPR014388; 3-oxoacid_CoA-transferase.
DR InterPro; IPR004165; CoA_trans_fam_I.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR PANTHER; PTHR43293; ACETATE COA-TRANSFERASE YDIF; 1.
DR PANTHER; PTHR43293:SF1; ACETATE COA-TRANSFERASE YDIF; 1.
DR Pfam; PF01144; CoA_trans; 1.
DR PIRSF; PIRSF000858; SCOT-t; 1.
DR SMART; SM00882; CoA_trans; 1.
DR SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000000747};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000858}.
FT ACT_SITE 324
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000858-1"
SQ SEQUENCE 513 AA; 55602 MW; AE7F3CF8122DC15C CRC64;
MRKLSTAETL AAQIQDGATI AISGNGGGMV EADHIMAAIE ERFLQTGHPR DLTLIHSLGI
GDRDSKGTNR FAHAEMLKRI IAGHFTWSPK MQELVKSNAI EAYCFPGGVI QALLREIGAG
RPGLFTHVGL GSFVDPRNGG GKSNECTTED LVELIEIDGE TKLRYRPFKV DYAILRGTYA
DPRGNVSLEE EAIDMDSYSM ALAAHNSGGK VFVQVRDVLE AGTIEPRKVK LPGILVDGIV
EHREQPQTYL GGYDLTISGQ HRRLSSNDAI ELVSHPVRRL IARRAARELA AGASTNFGFG
IPGGIPGVAL REGVPYQSLW LSVEQGVHNG MMLDDALFGC ARNADAIIPS LDQFEFYSGG
GIDITFLGMG EMDQYGNVNV SHLNGNLIGP GGFLEIAQNA RKVVFCGTFD AKGSKIDVTP
DGLHIAQSGQ IPKLVTQVEK ITFSAAYAQQ SGQEVLYITE RAVFQLTAEG VELIEIAPGV
EIERDILPFM AFRPIIKHPR LMESSLFTPM EDA
//
