ID E1TF03_BURSG Unreviewed; 415 AA.
AC E1TF03;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
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=BC1003_4299 {ECO:0000313|EMBL:ADN60233.1};
OS Burkholderia sp. (strain CCGE1003).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=640512 {ECO:0000313|EMBL:ADN60233.1};
RN [1] {ECO:0000313|EMBL:ADN60233.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCGE1003 {ECO:0000313|EMBL:ADN60233.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Daligault H., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Martinez-Romero E., Rogel M.A., Auchtung J., Tiedje J.M., Woyke T.;
RT "Complete sequence of chromosome2 of Burkholderia sp. CCGE1003.";
RL Submitted (SEP-2010) 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|HAMAP-Rule:MF_00742}.
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: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; CP002218; ADN60233.1; -; Genomic_DNA.
DR AlphaFoldDB; E1TF03; -.
DR STRING; 640512.BC1003_4299; -.
DR KEGG; bgf:BC1003_4299; -.
DR eggNOG; COG1804; Bacteria.
DR HOGENOM; CLU_033975_2_1_4; -.
DR OrthoDB; 5294844at2; -.
DR UniPathway; UPA00540; UER00598.
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; formyl-coa transferase, domain 3; 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 NCBIfam; TIGR03253; oxalate_frc; 1.
DR PANTHER; PTHR48207:SF2; FORMYL-COA:OXALATE COA-TRANSFERASE; 1.
DR PANTHER; PTHR48207; 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 Transferase {ECO:0000256|HAMAP-Rule:MF_00742, ECO:0000313|EMBL:ADN60233.1}.
FT ACT_SITE 168
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00742"
FT BINDING 17..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 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 136..139
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00742"
FT BINDING 247..249
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00742"
SQ SEQUENCE 415 AA; 45564 MW; 64F09AF06AC9DBF3 CRC64;
MGKALDGVRI LDFTHVQSGP TCTQLLAWFG ADVIKVERAG AGDITREQLR DIPDVDSLYF
TMLNHNKRSV TIDTKHPEGK QVLEALIQKC DVLVENFAPG ALDRMGFTWE RIQELNPRMI
VASVKGFGPG PYEDCKVYEN VAQCAGGAAS TTGFDDGPPV VTGAQIGDSG TGLHLALGIV
TALYQRTQTG RGQRVLAAMQ DGVLNLCRVK LRDQQRLERT GVMKEYPQYP NGKFGEAVPR
AGNASGGGQP GWILKCKGWE TDPNAYIYFI TQAPVWAKIC NVIGKEEWAT DPDYATPVAR
LPRLKEIFAE IERWTMTKTK FEAMQILNKY DIPCGPILSM KEIAEEPSLR KTGTIVEVDH
PTRGKYLTVG NPIKLSDSPT EVKRSPLLGE HTDEVMAELG YSPEQISALR TAGAI
//
