ID   ACOCT_ACEAC             Reviewed;         389 AA.
AC   A9X6P9;
DT   01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 40.
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;
DE   AltName: Full=CoAT3;
GN   Name=uctC;
OS   Acetobacter aceti.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acetobacter; Acetobacter subgen. Acetobacter.
OX   NCBI_TaxID=435;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=1023;
RX   PubMed=18502856; DOI=10.1128/jb.00405-08;
RA   Mullins E.A., Francois J.A., Kappock T.J.;
RT   "A specialized citric acid cycle requiring succinyl-coenzyme A
RT   (CoA):acetate CoA-transferase (AarC) confers acetic acid resistance on the
RT   acidophile Acetobacter aceti.";
RL   J. Bacteriol. 190:4933-4940(2008).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MASS
RP   SPECTROMETRY, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RC   STRAIN=1023;
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=1 mM for oxalate (at pH 6.7 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:23935849};
CC         KM=81 uM for acetyl-CoA (at pH 6.7 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:23935849};
CC         Note=kcat is 1.8 sec(-1) for the CoA-transferase activity with
CC         oxalate as substrate (at pH 6.7 and 25 degrees Celsius). kcat is 2
CC         sec(-1) for the CoA-transferase activity with acetyl-CoA as substrate
CC         (at pH 6.7 and 25 degrees Celsius).;
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:23935849}.
CC   -!- MASS SPECTROMETRY: Mass=41708; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:23935849};
CC   -!- SIMILARITY: Belongs to the CoA-transferase III family. {ECO:0000305}.
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DR   EMBL; DQ668372; ABG35152.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9X6P9; -.
DR   SMR; A9X6P9; -.
DR   KEGG; ag:ABG35152; -.
DR   GO; GO:0036412; F:acetyl-CoA:oxalate CoA-transferase; IEA:RHEA.
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   Transferase.
FT   CHAIN           1..389
FT                   /note="Acetyl-CoA:oxalate CoA-transferase"
FT                   /id="PRO_0000430298"
FT   ACT_SITE        237
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   389 AA;  41870 MW;  A49C3A940FD07719 CRC64;
     MTETTPAKPK GPFDGLLVID LTHVLNGPFG TTILTDLGAR TIKIEPPGHG DDTRTYGPYV
     GDQSLYFSFV NRGKESIVLN LKDEGDRAIF LEMVRKADVL AENFRPGVMD RLGFNYEELA
     KINPRLIYAS SSGFGQTGPL AHYPAYDTIV QAMSGIMMAT GFPDGPPTRV GGTSLSDLCG
     GVFMFCGIAS ALYARERTGK GAHIDVSMFD GTLAFLQHAL MCWSATGKAP ARIGNRHPYM
     APFDVFQAQD KPFVICCGND HLFKALCDVI GAPELATDPR FVENHDRMAN NDALKAALEK
     ALSKQPAAHW LDVIHKAGVP VGPLLDVAEA ANLPQTAARN MLIKSGGVMM PGNPVKISGY
     DDPHERPGAP KLDEQGAALR KEFAAPEAK