ID   FCTA_ECOLC              Reviewed;         416 AA.
AC   B1IX88;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   28-JAN-2026, entry version 91.
DE   RecName: Full=Formyl-CoA:oxalate CoA-transferase;
DE            Short=FCOCT;
DE            EC=2.8.3.16 {ECO:0000255|HAMAP-Rule:MF_00742};
DE   AltName: Full=Formyl-coenzyme A transferase {ECO:0000255|HAMAP-Rule:MF_00742};
DE            Short=Formyl-CoA transferase {ECO:0000255|HAMAP-Rule:MF_00742};
GN   Name=frc {ECO:0000255|HAMAP-Rule:MF_00742};
GN   OrderedLocusNames=EcolC_1295;
OS   Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS   WDCM 00012 / Crooks).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=481805;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 /
RC   Crooks;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Ingram L., Richardson P.;
RT   "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the catabolism of oxalate and in the adapatation
CC       to low pH via the induction of the oxalate-dependent acid tolerance
CC       response (ATR). Catalyzes the transfer of the CoA moiety from formyl-
CC       CoA to oxalate (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=formyl-CoA + oxalate = oxalyl-CoA + formate;
CC         Xref=Rhea:RHEA:16545, ChEBI:CHEBI:15740, ChEBI:CHEBI:30623,
CC         ChEBI:CHEBI:57376, ChEBI:CHEBI:57388; EC=2.8.3.16;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00742};
CC   -!- PATHWAY: Metabolic intermediate degradation; oxalate degradation; CO(2)
CC       and formate from oxalate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00742}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00742}.
CC   -!- SIMILARITY: Belongs to the CoA-transferase III family. Frc subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00742}.
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DR   EMBL; CP000946; ACA76961.1; -; Genomic_DNA.
DR   RefSeq; WP_000106759.1; NC_010468.1.
DR   AlphaFoldDB; B1IX88; -.
DR   SMR; B1IX88; -.
DR   GeneID; 75172492; -.
DR   GeneID; 75202557; -.
DR   KEGG; ecl:EcolC_1295; -.
DR   HOGENOM; CLU_033975_2_1_6; -.
DR   UniPathway; UPA00540; UER00598.
DR   GO; GO:0033608; F:formyl-CoA transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0033611; P:oxalate catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.10540; Crotonobetainyl-coa:carnitine coa-transferase, domain 1; 1.
DR   Gene3D; 3.30.1540.10; formyl-coa transferase, domain 3; 1.
DR   HAMAP; MF_00742; Formyl_CoA_transfer; 1.
DR   InterPro; IPR050483; CoA-transferase_III_domain.
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   InterPro; IPR017659; Formyl_CoA_transfer.
DR   NCBIfam; TIGR03253; oxalate_frc; 1.
DR   NCBIfam; NF003809; PRK05398.1; 1.
DR   PANTHER; PTHR48207; SUCCINATE--HYDROXYMETHYLGLUTARATE COA-TRANSFERASE; 1.
DR   PANTHER; PTHR48207:SF3; SUCCINATE--HYDROXYMETHYLGLUTARATE COA-TRANSFERASE; 1.
DR   Pfam; PF02515; CoA_transf_3; 1.
DR   SUPFAM; SSF89796; CoA-transferase family III (CaiB/BaiF); 1.
PE   3: Inferred from homology;
KW   Transferase.
FT   CHAIN           1..416
FT                   /note="Formyl-CoA:oxalate CoA-transferase"
FT                   /id="PRO_1000083472"
FT   ACT_SITE        169
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00742"
FT   BINDING         17..18
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         38
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00742"
FT   BINDING         72..75
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         96..98
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00742"
FT   BINDING         137..140
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         248..250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         273..275
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   416 AA;  45828 MW;  97F7FA4001073301 CRC64;
     MSTPLQGIKV LDFTGVQSGP SCTQMLAWFG ADVIKIERPG VGDVTRHQLR DIPDIDALYF
     TMLNSNKRSI ELNTKTAEGK EVMEKLIREA DILVENFHPG AIDHMGFTWE HIQEINPRLI
     FGSIKGFDEC SPYVNVKAYE NVAQAAGGAA STTGFWDGPP LVSAAALGDS NTGMHLLIGL
     LAALLHREKT GRGQRVTMSM QDAVLNLCRV KLRDQQRLDK LGYLEEYPQY PNGTFGDAVP
     RGGNAGGGGQ PGWILKCKGW ETDPNAYIYF TIQEQNWENT CKAIGKPEWI TDPAYSTAHA
     RQPHIFDIFA EIEKYTVTID KHEAVAYLTQ FDIPCAPVLS MKEISLDPSL RQSGSVVEVE
     QPLRGKYLTV GCPMKFSAFT PDIKAAPLLG EHTAAVLQEL GYSDDEIAAM KQNHAI
//