FCTA_AFIC5
ID FCTA_AFIC5 Reviewed; 424 AA.
AC B6JE29; F8BYN2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=OCAR_6550, OCA5_c15110;
OS Afipia carboxidovorans (strain ATCC 49405 / DSM 1227 / KCTC 32145 / OM5)
OS (Oligotropha carboxidovorans).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Afipia.
OX NCBI_TaxID=504832;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5;
RX PubMed=18539730; DOI=10.1128/jb.00614-08;
RA Paul D., Bridges S., Burgess S.C., Dandass Y., Lawrence M.L.;
RT "Genome sequence of the chemolithoautotrophic bacterium Oligotropha
RT carboxidovorans OM5T.";
RL J. Bacteriol. 190:5531-5532(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5;
RX PubMed=21742883; DOI=10.1128/jb.05619-11;
RA Volland S., Rachinger M., Strittmatter A., Daniel R., Gottschalk G.,
RA Meyer O.;
RT "Complete genome sequences of the chemolithoautotrophic Oligotropha
RT carboxidovorans strains OM4 and OM5.";
RL J. Bacteriol. 193:5043-5043(2011).
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; CP001196; ACI93662.1; -; Genomic_DNA.
DR EMBL; CP002826; AEI06227.1; -; Genomic_DNA.
DR RefSeq; WP_012563688.1; NC_015684.1.
DR AlphaFoldDB; B6JE29; -.
DR SMR; B6JE29; -.
DR STRING; 504832.OCAR_6550; -.
DR PRIDE; B6JE29; -.
DR EnsemblBacteria; AEI06227; AEI06227; OCA5_c15110.
DR KEGG; oca:OCAR_6550; -.
DR KEGG; ocg:OCA5_c15110; -.
DR PATRIC; fig|504832.7.peg.1608; -.
DR eggNOG; COG1804; Bacteria.
DR HOGENOM; CLU_033975_2_1_5; -.
DR OMA; FFWSPIN; -.
DR OrthoDB; 969868at2; -.
DR UniPathway; UPA00540; UER00598.
DR Proteomes; UP000007730; 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 Reference proteome; Transferase.
FT CHAIN 1..424
FT /note="Formyl-CoA:oxalate CoA-transferase"
FT /id="PRO_1000189582"
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 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 424 AA; 46189 MW; 01E771BC56F5F401 CRC64;
MAKALNGVRI LDFTHVQSGP TCTQLLAWFG ADVIKVERPG TGDITRGQLQ DVPNADSLYF
TMLNHNKRSI TLDAKNPKGK EVLTALIKSC DVMVENFAPG VLDRMGFSWE NIQKINPKLI
VASIKGFGPG PFEDCKVYEN VAQCTGGSAS TTGFRDGLPL VTGAQIGDSG TGLHLALGIV
TALFHRTHSG KGQRVTVAMQ DSVLNLCRVK MRDQQRLAHG PLKEYSQFGE GIPFGDATPR
AGNDSGGGQP GRILKCKGWE TDPNAYIYFI TQAAVWEKIC DVIGEPTWKT DPNYAKPGAR
LPRLNEIFGR IEQWTMTKTK FEVMNICNPF DIPCGPILSM KEIAEDKSLY ATGTLVEVDH
PTRGKYISVG NPIKLSDSPA DVRRSPLLGE HTDEILRDVL KFSESQVSDI RSSGALGEVP
LAAE