FCTA_BRASB
ID FCTA_BRASB Reviewed; 425 AA.
AC A5EGD7;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=BBta_3113;
OS Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium; unclassified Bradyrhizobium.
OX NCBI_TaxID=288000;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTAi1 / ATCC BAA-1182;
RX PubMed=17540897; DOI=10.1126/science.1139548;
RA Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.-C.,
RA Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.-S., Saunders E.,
RA Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL Science 316:1307-1312(2007).
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; CP000494; ABQ35231.1; -; Genomic_DNA.
DR RefSeq; WP_012043249.1; NC_009485.1.
DR AlphaFoldDB; A5EGD7; -.
DR SMR; A5EGD7; -.
DR STRING; 288000.BBta_3113; -.
DR EnsemblBacteria; ABQ35231; ABQ35231; BBta_3113.
DR KEGG; bbt:BBta_3113; -.
DR eggNOG; COG1804; Bacteria.
DR HOGENOM; CLU_033975_2_1_5; -.
DR OMA; FFWSPIN; -.
DR OrthoDB; 969868at2; -.
DR BRENDA; 2.8.3.16; 930.
DR UniPathway; UPA00540; UER00598.
DR Proteomes; UP000000246; 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_0000300985"
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; 46639 MW; 23FA62E1131A035F CRC64;
MTKALEGVRI LDFTHVQSGP TCTQLLAWFG ADVIKVERPG VGDITRGQLQ DIPNVDSLYF
TMLNHNKRSI TLDTKNPKGK EVLTELIKKC DVLVENFGPG VLDRMGFPWE KIQAINPKMI
VASIKGFGPG PYEDCKVYEN VAQCTGGAAS TTGFRDGLPL VTGAQIGDSG TGLHLALGIV
TALYQRTHTG KGQRVTAAMQ DGVLNLCRVK LRDQQRLERG PLKEYSQFGE GVPFGDAVPR
AGNDSGGGQP GRILKCKGWE TDPNAYIYFI TQAPVWEKIC DVIGEPTWKT DPNYAKPAAR
LPRLNEIFGR IEQWTMTKTK FEAMDILNEF DIPCGPILSM KEIAEDESLR KTGTLVEVDH
PTRGKYLSVG NPIKLSDSPA EVTRSPLLGE HTDEILRQVL GFSDHQVAEI HDSGALDPPR
KEAAE