ID A0A1L6I5K6_9BURK Unreviewed; 415 AA.
AC A0A1L6I5K6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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 ORFNames=BTO02_27015 {ECO:0000313|EMBL:APR39017.1};
OS Paraburkholderia sp. SOS3.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1926494 {ECO:0000313|EMBL:APR39017.1, ECO:0000313|Proteomes:UP000184708};
RN [1] {ECO:0000313|EMBL:APR39017.1, ECO:0000313|Proteomes:UP000184708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SOS3 {ECO:0000313|EMBL:APR39017.1,
RC ECO:0000313|Proteomes:UP000184708};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-2016) 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; CP018812; APR39017.1; -; Genomic_DNA.
DR RefSeq; WP_075160188.1; NZ_CP018812.1.
DR AlphaFoldDB; A0A1L6I5K6; -.
DR STRING; 1926494.BTO02_27015; -.
DR KEGG; para:BTO02_27015; -.
DR OrthoDB; 5294844at2; -.
DR UniPathway; UPA00540; UER00598.
DR Proteomes; UP000184708; Chromosome 2.
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:APR39017.1}.
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; 45318 MW; 9AA8894956287D15 CRC64;
MAKALDGVRI LDFTHVQSGP TCTQLLAWFG ADVIKVERAG TGDVTREQLR DIPDADSLYF
TMLNHNKRSV TIDTKNPEGK KVLETLIKTC DVLVENFAPG ALDRMGFTWE RIQELNPQMI
VASVKGFGPG PYEDCKVYEN VAQCAGGAAS TTGFDDGPPV VTGAQIGDSG TGLHLALGIV
TALFQRTKTN RGQKVLAAMQ DGVLNLCRVK LRDQQRLART GVMKEYPQYP NGTFGEAVPR
AGNASGGGQP GWILKCKGWE ADPNAYIYFI TQAPVWAKIC NVIGKEEWAT DPDYATPAAR
LPHLKEIFAE IERWTMTKTK FEAMDILNKY DIPCGPILSM KEIAEDESLR KTGTIVEVDH
PVRGKYLTVG NPIKLSDSPT DVTRSPLLGE HTDEVMTELG YSAQQIAALR TAGAI
//
