YDIF_ECO57
ID YDIF_ECO57 Reviewed; 531 AA.
AC Q8X5X6; Q7ADH3;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Acetate CoA-transferase YdiF {ECO:0000305};
DE EC=2.8.3.8 {ECO:0000269|PubMed:16253988};
DE AltName: Full=Short-chain acyl-CoA:acetate CoA-transferase;
GN Name=ydiF {ECO:0000312|EMBL:AAG56681.1}; OrderedLocusNames=Z2722, ECs2401;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1] {ECO:0000312|EMBL:AAG56681.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2] {ECO:0000312|EMBL:BAB35824.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
RN [3] {ECO:0000305, ECO:0000312|PDB:2AHW}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH
RP COENZYME A VIA A GAMMA-GLUTAMYL-THIOESTER COVALENT LINKAGE, FUNCTION,
RP SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBUNIT, MASS SPECTROMETRY, AND
RP REACTION MECHANISM.
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=16253988; DOI=10.1074/jbc.m510522200;
RA Rangarajan E.S., Li Y., Ajamian E., Iannuzzi P., Kernaghan S.D.,
RA Fraser M.E., Cygler M., Matte A.;
RT "Crystallographic trapping of the glutamyl-CoA thioester intermediate of
RT family I CoA transferases.";
RL J. Biol. Chem. 280:42919-42928(2005).
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. Exhibits high
CC activity with acetoacetyl-CoA, propionyl-CoA, crotonoyl-CoA or butyryl-
CC CoA as donors, with acetate as an acceptor. When acetyl-CoA is used as
CC the donor, propionate, acetoacetate, butyrate, isobutyrate, and 4-
CC hydroxybutyrate can be utilized as acceptors but not isovalerate. May
CC play a role in short-chain fatty acid metabolism in E.coli.
CC {ECO:0000269|PubMed:16253988}.
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:16253988};
CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000269|PubMed:16253988}.
CC -!- MASS SPECTROMETRY: Mass=59628; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:16253988};
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:0000269|PubMed:16253988}.
CC -!- SIMILARITY: Belongs to the 3-oxoacid CoA-transferase family.
CC {ECO:0000255}.
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DR EMBL; AE005174; AAG56681.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB35824.1; -; Genomic_DNA.
DR PIR; A90929; A90929.
DR PIR; E85777; E85777.
DR RefSeq; NP_310428.1; NC_002695.1.
DR RefSeq; WP_000805650.1; NZ_SEKU01000008.1.
DR PDB; 2AHU; X-ray; 1.90 A; A/B/C/D=1-531.
DR PDB; 2AHV; X-ray; 2.00 A; A/B/C/D=1-531.
DR PDB; 2AHW; X-ray; 2.15 A; A/B/C/D=1-531.
DR PDBsum; 2AHU; -.
DR PDBsum; 2AHV; -.
DR PDBsum; 2AHW; -.
DR AlphaFoldDB; Q8X5X6; -.
DR SMR; Q8X5X6; -.
DR STRING; 155864.EDL933_2651; -.
DR EnsemblBacteria; AAG56681; AAG56681; Z2722.
DR EnsemblBacteria; BAB35824; BAB35824; ECs_2401.
DR GeneID; 912561; -.
DR KEGG; ece:Z2722; -.
DR KEGG; ecs:ECs_2401; -.
DR PATRIC; fig|386585.9.peg.2514; -.
DR eggNOG; COG4670; Bacteria.
DR HOGENOM; CLU_026774_4_0_6; -.
DR OMA; GTDYNKR; -.
DR EvolutionaryTrace; Q8X5X6; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0008775; F:acetate CoA-transferase activity; IDA:UniProtKB.
DR GO; GO:0046952; P:ketone body catabolic process; IEA:InterPro.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR GO; GO:0046459; P:short-chain fatty acid metabolic process; IDA: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 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Transferase.
FT CHAIN 1..531
FT /note="Acetate CoA-transferase YdiF"
FT /id="PRO_0000418373"
FT ACT_SITE 333
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000305|PubMed:16253988"
FT HELIX 18..22
FT /evidence="ECO:0007829|PDB:2AHU"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:2AHU"
FT TURN 38..41
FT /evidence="ECO:0007829|PDB:2AHU"
FT HELIX 44..57
FT /evidence="ECO:0007829|PDB:2AHU"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:2AHU"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:2AHU"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:2AHU"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:2AHU"
FT STRAND 88..95
FT /evidence="ECO:0007829|PDB:2AHU"
FT HELIX 100..107
FT /evidence="ECO:0007829|PDB:2AHU"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:2AHU"
FT HELIX 118..129
FT /evidence="ECO:0007829|PDB:2AHU"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:2AHU"
FT TURN 139..142
FT /evidence="ECO:0007829|PDB:2AHU"
FT TURN 147..152
FT /evidence="ECO:0007829|PDB:2AHU"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:2AHU"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:2AHU"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:2AHU"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:2AHU"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:2AHU"
FT HELIX 208..216
FT /evidence="ECO:0007829|PDB:2AHU"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:2AHU"
FT STRAND 221..230
FT /evidence="ECO:0007829|PDB:2AHU"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:2AHU"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:2AHU"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:2AHU"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:2AHU"
FT TURN 267..271
FT /evidence="ECO:0007829|PDB:2AHU"
FT HELIX 287..296
FT /evidence="ECO:0007829|PDB:2AHU"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:2AHU"
FT TURN 311..314
FT /evidence="ECO:0007829|PDB:2AHU"
FT HELIX 315..321
FT /evidence="ECO:0007829|PDB:2AHU"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:2AHU"
FT STRAND 328..331
FT /evidence="ECO:0007829|PDB:2AHU"
FT STRAND 335..338
FT /evidence="ECO:0007829|PDB:2AHU"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:2AHU"
FT HELIX 359..367
FT /evidence="ECO:0007829|PDB:2AHU"
FT STRAND 372..377
FT /evidence="ECO:0007829|PDB:2AHU"
FT STRAND 379..382
FT /evidence="ECO:0007829|PDB:2AHU"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:2AHU"
FT HELIX 402..406
FT /evidence="ECO:0007829|PDB:2AHU"
FT STRAND 410..415
FT /evidence="ECO:0007829|PDB:2AHU"
FT STRAND 418..422
FT /evidence="ECO:0007829|PDB:2AHU"
FT STRAND 424..427
FT /evidence="ECO:0007829|PDB:2AHU"
FT STRAND 432..436
FT /evidence="ECO:0007829|PDB:2AHU"
FT STRAND 439..445
FT /evidence="ECO:0007829|PDB:2AHU"
FT HELIX 454..459
FT /evidence="ECO:0007829|PDB:2AHU"
FT STRAND 463..467
FT /evidence="ECO:0007829|PDB:2AHU"
FT STRAND 469..476
FT /evidence="ECO:0007829|PDB:2AHU"
FT STRAND 479..485
FT /evidence="ECO:0007829|PDB:2AHU"
FT HELIX 491..494
FT /evidence="ECO:0007829|PDB:2AHU"
FT HELIX 496..498
FT /evidence="ECO:0007829|PDB:2AHU"
FT STRAND 499..501
FT /evidence="ECO:0007829|PDB:2AHU"
FT STRAND 504..511
FT /evidence="ECO:0007829|PDB:2AHU"
FT HELIX 514..517
FT /evidence="ECO:0007829|PDB:2AHU"
FT STRAND 518..520
FT /evidence="ECO:0007829|PDB:2AHU"
SQ SEQUENCE 531 AA; 57504 MW; FC70D164D28A4E3E CRC64;
MKPVKPPRIN GRVPVLSAQE AVNYIPDEAT LCVLGAGGGI LEATTLITAL ADKYKQTQTP
RNLSIISPTG LGDRADRGIS PLAQEGLVKW ALCGHWGQSP RISDLAEQNK IIAYNYPQGV
LTQTLRAAAA HQPGIISDIG IGTFVDPRQQ GGKLNEVTKE DLIKLVEFDN KEYLYYKAIA
PDIAFIRATT CDSEGYATFE DEVMYLDALV IAQAVHNNGG IVMMQVQKMV KKATLHPKSV
RIPGYLVDIV VVDPDQSQLY GGAPVNRFIS GDFTLDDSTK LSLPLNQRKL VARRALFEMR
KGAVGNVGVG IADGIGLVAR EEGCADDFIL TVETGPIGGI TSQGIAFGAN VNTRAILDMT
SQFDFYHGGG LDVCYLSFAE VDQHGNVGVH KFNGKIMGTG GFIDISATSK KIIFCGTLTA
GSLKTEIADG KLNIVQEGRV KKFIRELPEI TFSGKIALER GLDVRYITER AVFTLKEDGL
HLIEIAPGVD LQKDILDKMD FTPVISPELK LMDERLFIDA AMGFVLPEAA H
