ID   FCTA_RHOP2              Reviewed;         425 AA.
AC   Q2IUI7;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 96.
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}; OrderedLocusNames=RPB_3427;
OS   Rhodopseudomonas palustris (strain HaA2).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HaA2;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A.,
RA   Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris HaA2.";
RL   Submitted (JAN-2006) 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 = formate + oxalyl-CoA;
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; CP000250; ABD08123.1; -; Genomic_DNA.
DR   RefSeq; WP_011442307.1; NC_007778.1.
DR   AlphaFoldDB; Q2IUI7; -.
DR   SMR; Q2IUI7; -.
DR   STRING; 316058.RPB_3427; -.
DR   EnsemblBacteria; ABD08123; ABD08123; RPB_3427.
DR   KEGG; rpb:RPB_3427; -.
DR   eggNOG; COG1804; Bacteria.
DR   HOGENOM; CLU_033975_2_1_5; -.
DR   OMA; FFWSPIN; -.
DR   OrthoDB; 969868at2; -.
DR   UniPathway; UPA00540; UER00598.
DR   Proteomes; UP000008809; Chromosome.
DR   GO; GO:0033608; F:formyl-CoA transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0033611; P:oxalate catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.1540.10; -; 1.
DR   Gene3D; 3.40.50.10540; -; 1.
DR   HAMAP; MF_00742; Formyl_CoA_transfer; 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   InterPro; IPR017659; Formyl_CoA_transfer.
DR   Pfam; PF02515; CoA_transf_3; 1.
DR   SUPFAM; SSF89796; SSF89796; 1.
DR   TIGRFAMs; TIGR03253; oxalate_frc; 1.
PE   3: Inferred from homology;
KW   Transferase.
FT   CHAIN           1..425
FT                   /note="Formyl-CoA:oxalate CoA-transferase"
FT                   /id="PRO_0000300993"
FT   ACT_SITE        168
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         136..139
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         247..249
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   425 AA;  46494 MW;  6DE89559FCD49E17 CRC64;
     MTKALDGVRI LDFTHVQSGP TCTQLLAWFG ADVIKVERPG TGDITRGQLQ DIPKVDSLYF
     TMLNHNKRSI TLDTKNPKGK EVLTALIRSC DVLVENFGPG VLDRMGFTWD KIQEINPRMI
     VASIKGFGPG PYEDCKVYEN VAQCTGGAAS TTGFRDGPPL VTGAQIGDSG TGLHLALGIV
     TALYQRHHTG RGQRVTAAMQ DGVLNLSRVK LRDQQRLAHG PLKEYSQFGE GIPFGDAVPR
     AGNDSGGGQP GRILKCKGWE TDPNAYIYFI AQAPVWEKIC DVIGETGWKT HPDYATPPAR
     LKHLNDIFAR IEQWTMTKTK FEAMDILNRD DIPCGPILSM KELAEDASLR ATGTIVEVDH
     PTRGKYLSVG NPIKLSDSPT HVERSPLLGE HTDEILRDVL GFNDHQVAEI HDSGALAPPR
     KQAAE