ID Q1R3N3_ECOUT Unreviewed; 523 AA.
AC Q1R3N3;
DT 16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Acetate CoA-transferase YdiF {ECO:0000256|PIRNR:PIRNR000858};
DE EC=2.8.3.8 {ECO:0000256|PIRNR:PIRNR000858};
GN OrderedLocusNames=UTI89_C4623 {ECO:0000313|EMBL:ABE10031.1};
OS Escherichia coli (strain UTI89 / UPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=364106 {ECO:0000313|EMBL:ABE10031.1, ECO:0000313|Proteomes:UP000001952};
RN [1] {ECO:0000313|EMBL:ABE10031.1, ECO:0000313|Proteomes:UP000001952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTI89 / UPEC {ECO:0000313|Proteomes:UP000001952};
RX PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA Chen S.L., Hung C.S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA Gordon J.I.;
RT "Identification of genes subject to positive selection in uropathogenic
RT strains of Escherichia coli: a comparative genomics approach.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
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; CP000243; ABE10031.1; -; Genomic_DNA.
DR RefSeq; WP_000337269.1; NZ_CP064825.1.
DR AlphaFoldDB; Q1R3N3; -.
DR KEGG; eci:UTI89_C4623; -.
DR HOGENOM; CLU_026774_4_0_6; -.
DR Proteomes; UP000001952; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000858}.
FT ACT_SITE 330
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000858-1"
SQ SEQUENCE 523 AA; 56275 MW; 4FDC69D828FB6B98 CRC64;
MCSVRTITAP EAADLIVDGA VVTVSSSSGM GCPDAVLAAI GERFQRAGHP QNITSIHPIA
AGDMYGVKGI DHLAQPGLLA KVIAGSYPSG PSSMAPPLIW QMINDNAIPA RNLPSGILFD
MHREAAAHRP GVLTQTGMDT YVDPLLQGGA MNEKAAQQSL VERVRFANDD WLFFPSIVPQ
VAIIRATTAD ERGNLTYEHE GAYLGPLEQA TAVRNNGGII IAQVKRQVAA GSLKPKEVRI
PGVLVDYIVI APEQTQTTQT QYEPAISGEI SRPLSAFRYM EHGPARVIAQ RVAQELQSGD
AVNIGFGISA NVPRILLEQG RHGDVTWLLE QGAIGGVPLL EFQFGCASNA EAFLPSPQQF
TYFQGGGFDL TLMSFLQIGA DGSVNVSHLP ARPHVTAGCG GFIDITSHAK RIIFSGFFNA
GAQLQLEEGQ LRIIKEGKAK KLVQDVAHVT FSGKRAIRLG QQVQYITERC VLELTPDGLL
VTEIAPGIDP ERDILAQSNA PLRLADDLKL MNPHYFQQGR HHE
//
