ID   FCTA_RHOPT              Reviewed;         425 AA.
AC   B3QBS6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=Rpal_2155;
OS   Rhodopseudomonas palustris (strain TIE-1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=395960;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TIE-1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Emerson D.,
RA   Newman D.K., Roden E., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris TIE-1.";
RL   Submitted (MAY-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 = 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001096; ACF00676.1; -; Genomic_DNA.
DR   RefSeq; WP_012495477.1; NC_011004.1.
DR   AlphaFoldDB; B3QBS6; -.
DR   SMR; B3QBS6; -.
DR   EnsemblBacteria; ACF00676; ACF00676; Rpal_2155.
DR   KEGG; rpt:Rpal_2155; -.
DR   HOGENOM; CLU_033975_2_1_5; -.
DR   OMA; FFWSPIN; -.
DR   OrthoDB; 969868at2; -.
DR   BioCyc; RPAL395960:RPAL_RS10705-MON; -.
DR   UniPathway; UPA00540; UER00598.
DR   Proteomes; UP000001725; 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_1000189583"
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;  46512 MW;  8DCAE0B771C5F625 CRC64;
     MTKALDGVRV LDFTHVQSGP TCTQLLAWFG ADVIKVERPG SGDITRGQLQ DIPKVDSLYF
     TMLNHNKRSI TLDTKNPKGK EVLTALIRTC DVLVENFGPG VLDRMGFTWE KIQEINPRMI
     VASIKGFGPG PYEDCKVYEN VAQCTGGAAS TTGFREGLPL VTGAQIGDSG TGLHLALGIV
     TALYQRHHTG RGQRVTAAMQ DGVLNLCRVK LRDQQRLDHG PLKEYSQFGE GIPFGDAVPR
     AGNDSGGGQP GRILKCKGWE QDPNAYIYVI TQAPVWEKIC DVIGETGWKM HPDYATPPAR
     LSRLNEIFAR IEQWTMTKTK FEAMEILNAD DIPCGPILSM KELAEDQSLR ATGTIVEVDH
     PTRGKYLSVG NPIKLSDSPT EVKRSPLLGE HTDEILRDVL GYSDAHVAEI HDSGATAPPR
     KQAAE