ACOCT_ECOLI
ID ACOCT_ECOLI Reviewed; 381 AA.
AC P76518; P76946;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Acetyl-CoA:oxalate CoA-transferase;
DE Short=ACOCT;
DE EC=2.8.3.19;
DE AltName: Full=Acetyl-coenzyme A transferase;
DE AltName: Full=CoA:oxalate CoA-transferase;
GN Name=yfdE; OrderedLocusNames=b2371, JW2368;
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=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
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 259-381.
RC STRAIN=K12;
RX PubMed=8125343; DOI=10.1016/0378-1119(94)90733-1;
RA Utsumi R., Katayama S., Taniguchi M., Horie T., Ikeda M., Igaki S.,
RA Nakagawa H., Miwa A., Tanabe H., Noda M.;
RT "Newly identified genes involved in the signal transduction of Escherichia
RT coli K-12.";
RL Gene 140:73-77(1994).
RN [5]
RP INDUCTION.
RX PubMed=12694615; DOI=10.1046/j.1365-2958.2003.03477.x;
RA Masuda N., Church G.M.;
RT "Regulatory network of acid resistance genes in Escherichia coli.";
RL Mol. Microbiol. 48:699-712(2003).
RN [6]
RP INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=23335415; DOI=10.1128/jb.01936-12;
RA Fontenot E.M., Ezelle K.E., Gabreski L.N., Giglio E.R., McAfee J.M.,
RA Mills A.C., Qureshi M.N., Salmon K.M., Toyota C.G.;
RT "YfdW and YfdU are required for oxalate-induced acid tolerance in
RT Escherichia coli K-12.";
RL J. Bacteriol. 195:1446-1455(2013).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY, SUBSTRATE SPECIFICITY,
RP AND SUBUNIT.
RC STRAIN=K12 / BW25113;
RX PubMed=23935849; DOI=10.1371/journal.pone.0067901;
RA Mullins E.A., Sullivan K.L., Kappock T.J.;
RT "Function and X-ray crystal structure of Escherichia coli YfdE.";
RL PLoS ONE 8:E67901-E67901(2013).
CC -!- FUNCTION: Involved in the catabolism of oxalate and in the adapatation
CC to low pH. ACOCT serves to prime the oxalate-induced acid tolerance
CC response (ATR) cycle by producing substrate for oxalyl-CoA
CC decarboxylase (OXC) and formyl-coenzyme A transferase (FCOCT).
CC Catalyzes the reversible conversion of acetyl-CoA and oxalate to
CC oxalyl-CoA and acetate. It can also use formyl-CoA and oxalate to
CC produce oxalyl-CoA and formate with significantly reduced specific
CC activity. {ECO:0000269|PubMed:23935849}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + oxalate = acetate + oxalyl-CoA;
CC Xref=Rhea:RHEA:37883, ChEBI:CHEBI:30089, ChEBI:CHEBI:30623,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57388; EC=2.8.3.19;
CC Evidence={ECO:0000269|PubMed:23935849};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=17 uM for acetyl-CoA (at pH 6.7 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:23935849};
CC KM=22 mM for oxalate (at pH 6.7 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:23935849};
CC Note=kcat is 11 sec(-1) for the CoA-transferase activity with acetyl-
CC CoA as substrate (at pH 6.7 and 25 degrees Celsius). kcat is 15 sec(-
CC 1) for the CoA-transferase activity with oxalate as substrate (at pH
CC 6.7 and 25 degrees Celsius).;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:23935849}.
CC -!- INDUCTION: By the acid response regulator EvgA.
CC {ECO:0000269|PubMed:12694615, ECO:0000269|PubMed:23335415}.
CC -!- SIMILARITY: Belongs to the CoA-transferase III family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=D14008; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U00096; AAC75430.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA16242.1; -; Genomic_DNA.
DR EMBL; D14008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; H65010; H65010.
DR RefSeq; NP_416872.4; NC_000913.3.
DR RefSeq; WP_001296867.1; NZ_LN832404.1.
DR PDB; 4HL6; X-ray; 2.12 A; A/B/C/D/E/F=1-381.
DR PDBsum; 4HL6; -.
DR AlphaFoldDB; P76518; -.
DR SMR; P76518; -.
DR BioGRID; 4259190; 3.
DR DIP; DIP-11994N; -.
DR IntAct; P76518; 7.
DR STRING; 511145.b2371; -.
DR PaxDb; P76518; -.
DR PRIDE; P76518; -.
DR EnsemblBacteria; AAC75430; AAC75430; b2371.
DR EnsemblBacteria; BAA16242; BAA16242; BAA16242.
DR GeneID; 66673759; -.
DR GeneID; 946432; -.
DR KEGG; ecj:JW2368; -.
DR KEGG; eco:b2371; -.
DR PATRIC; fig|1411691.4.peg.4358; -.
DR EchoBASE; EB3069; -.
DR eggNOG; COG1804; Bacteria.
DR HOGENOM; CLU_033975_0_0_6; -.
DR InParanoid; P76518; -.
DR OMA; NRERHGV; -.
DR PhylomeDB; P76518; -.
DR BioCyc; EcoCyc:G7234-MON; -.
DR BioCyc; MetaCyc:G7234-MON; -.
DR BRENDA; 2.8.3.19; 2026.
DR PRO; PR:P76518; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0036412; F:acetyl-CoA:oxalate CoA-transferase; IDA:EcoCyc.
DR Gene3D; 3.30.1540.10; -; 1.
DR Gene3D; 3.40.50.10540; -; 1.
DR InterPro; IPR003673; CoA-Trfase_fam_III.
DR InterPro; IPR044855; CoA-Trfase_III_dom3_sf.
DR InterPro; IPR023606; CoA-Trfase_III_dom_1_sf.
DR Pfam; PF02515; CoA_transf_3; 1.
DR SUPFAM; SSF89796; SSF89796; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Transferase.
FT CHAIN 1..381
FT /note="Acetyl-CoA:oxalate CoA-transferase"
FT /id="PRO_0000194725"
FT ACT_SITE 233
FT /evidence="ECO:0000250"
FT CONFLICT 294
FT /note="I -> T (in Ref. 4; D14008)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="Q -> E (in Ref. 4; D14008)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="A -> T (in Ref. 4; D14008)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="L -> S (in Ref. 4; D14008)"
FT /evidence="ECO:0000305"
FT TURN 9..12
FT /evidence="ECO:0007829|PDB:4HL6"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:4HL6"
FT HELIX 23..33
FT /evidence="ECO:0007829|PDB:4HL6"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:4HL6"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:4HL6"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:4HL6"
FT HELIX 62..68
FT /evidence="ECO:0007829|PDB:4HL6"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:4HL6"
FT HELIX 81..93
FT /evidence="ECO:0007829|PDB:4HL6"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:4HL6"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:4HL6"
FT HELIX 113..119
FT /evidence="ECO:0007829|PDB:4HL6"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:4HL6"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:4HL6"
FT TURN 136..139
FT /evidence="ECO:0007829|PDB:4HL6"
FT HELIX 144..151
FT /evidence="ECO:0007829|PDB:4HL6"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:4HL6"
FT HELIX 171..194
FT /evidence="ECO:0007829|PDB:4HL6"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:4HL6"
FT HELIX 204..209
FT /evidence="ECO:0007829|PDB:4HL6"
FT HELIX 214..222
FT /evidence="ECO:0007829|PDB:4HL6"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:4HL6"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:4HL6"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:4HL6"
FT HELIX 256..266
FT /evidence="ECO:0007829|PDB:4HL6"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:4HL6"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:4HL6"
FT HELIX 280..285
FT /evidence="ECO:0007829|PDB:4HL6"
FT HELIX 287..298
FT /evidence="ECO:0007829|PDB:4HL6"
FT HELIX 303..312
FT /evidence="ECO:0007829|PDB:4HL6"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:4HL6"
FT HELIX 323..326
FT /evidence="ECO:0007829|PDB:4HL6"
FT HELIX 330..334
FT /evidence="ECO:0007829|PDB:4HL6"
FT STRAND 338..341
FT /evidence="ECO:0007829|PDB:4HL6"
FT STRAND 344..347
FT /evidence="ECO:0007829|PDB:4HL6"
FT STRAND 350..353
FT /evidence="ECO:0007829|PDB:4HL6"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:4HL6"
FT TURN 368..371
FT /evidence="ECO:0007829|PDB:4HL6"
FT HELIX 372..379
FT /evidence="ECO:0007829|PDB:4HL6"
SQ SEQUENCE 381 AA; 41671 MW; 9C6801BCACFA5AE8 CRC64;
MTNNESKGPF EGLLVIDMTH VLNGPFGTQL LCNMGARVIK VEPPGHGDDT RTFGPYVDGQ
SLYYSFINHG KESVVLDLKN DHDKSIFINM LKQADVLAEN FRPGTMEKLG FSWETLQEIN
PRLIYASSSG FGHTGPLKDA PAYDTIIQAM SGIMMETGYP DAPPVRVGTS LADLCGGVYL
FSGIVSALYG REKSQRGAHV DIAMFDATLS FLEHGLMAYI ATGKSPQRLG NRHPYMAPFD
VFNTQDKPIT ICCGNDKLFS ALCQALELTE LVNDPRFSSN ILRVQNQAIL KQYIERTLKT
QAAEVWLARI HEVGVPVAPL LSVAEAIKLP QTQARNMLIE AGGIMMPGNP IKISGCADPH
VMPGAATLDQ HGEQIRQEFS S
