ID   B8IFZ2_METNO            Unreviewed;       416 AA.
AC   B8IFZ2;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   08-OCT-2025, entry version 82.
DE   RecName: Full=Formyl-CoA:oxalate CoA-transferase {ECO:0000256|HAMAP-Rule:MF_00742};
DE            Short=FCOCT {ECO:0000256|HAMAP-Rule:MF_00742};
DE            EC=2.8.3.16 {ECO:0000256|HAMAP-Rule:MF_00742};
DE   AltName: Full=Formyl-coenzyme A transferase {ECO:0000256|HAMAP-Rule:MF_00742};
DE            Short=Formyl-CoA transferase {ECO:0000256|HAMAP-Rule:MF_00742};
GN   Name=frc {ECO:0000256|HAMAP-Rule:MF_00742};
GN   OrderedLocusNames=Mnod_4840 {ECO:0000313|EMBL:ACL59702.1};
OS   Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=460265 {ECO:0000313|EMBL:ACL59702.1, ECO:0000313|Proteomes:UP000008207};
RN   [1] {ECO:0000313|EMBL:ACL59702.1, ECO:0000313|Proteomes:UP000008207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060
RC   {ECO:0000313|Proteomes:UP000008207};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Marx C.J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium nodulans ORS 2060.";
RL   Submitted (JAN-2009) 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. {ECO:0000256|ARBA:ARBA00025298, ECO:0000256|HAMAP-
CC       Rule:MF_00742}.
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:0000256|HAMAP-Rule:MF_00742};
CC   -!- PATHWAY: Metabolic intermediate degradation; oxalate degradation; CO(2)
CC       and formate from oxalate: step 1/2. {ECO:0000256|HAMAP-Rule:MF_00742}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00742}.
CC   -!- SIMILARITY: Belongs to the CoA-transferase III family. Frc subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00742}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00742}.
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DR   EMBL; CP001349; ACL59702.1; -; Genomic_DNA.
DR   RefSeq; WP_015931332.1; NC_011894.1.
DR   AlphaFoldDB; B8IFZ2; -.
DR   STRING; 460265.Mnod_4840; -.
DR   KEGG; mno:Mnod_4840; -.
DR   eggNOG; COG1804; Bacteria.
DR   HOGENOM; CLU_033975_2_1_5; -.
DR   OrthoDB; 9806585at2; -.
DR   UniPathway; UPA00540; UER00598.
DR   Proteomes; UP000008207; Chromosome.
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   Reference proteome {ECO:0000313|Proteomes:UP000008207};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00742}.
FT   ACT_SITE        169
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00742"
FT   BINDING         15..18
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00742"
FT   BINDING         38
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00742"
FT   BINDING         72..75
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00742"
FT   BINDING         96..98
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00742"
FT   BINDING         104
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00742"
FT   BINDING         137..140
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00742"
FT   BINDING         248..250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00742"
SQ   SEQUENCE   416 AA;  45705 MW;  FF1042007A4F4A0E CRC64;
     MSKPLEGIKI IDFTHVQAGP ACTQLLAWFG ADVIKVERPG AGDVTRTQLR HVDDADALYF
     TMLNSNKRSL TLDTKTPQGK EVLEKLIRES DVLVENFGPG ALDRMGFSWA RINELNPGMI
     VASVKGFSEG HHYEDLKVYE NVAQCAGGAA STTGFWDGPP TVSGAALGDS NTGMHLAIGI
     LTALHQRNKT GKGQKVAVSM QDAVLNLCRV KLRDQQRLDA IGYLEEYPQY PHGTFTDVVP
     RGGNAGGGGQ PGWVLKCKGW ETDPNAYIYF TIQGHAWAPI CRALGKEEWI DDPAYNTPRA
     RQDKIFDIFA VIEGWLADKT KYEAVDILRK YDIPCAPVLS MKEIAEDKSL RASGSIVEVP
     HPQLGKYLTV GSPIKFSDLT IDVMPSPLLG EHTDEVLRGL GYTEQQIEML HQERAV
//