ID A0A1S8FHZ0_9BURK Unreviewed; 415 AA.
AC A0A1S8FHZ0;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=B0B52_09865 {ECO:0000313|EMBL:OOG42951.1};
OS Polaromonas sp. A23.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=1944133 {ECO:0000313|EMBL:OOG42951.1, ECO:0000313|Proteomes:UP000218978};
RN [1] {ECO:0000313|EMBL:OOG42951.1, ECO:0000313|Proteomes:UP000218978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A23 {ECO:0000313|EMBL:OOG42951.1,
RC ECO:0000313|Proteomes:UP000218978};
RA Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA Frostegard A.;
RT "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT isolation strategy.";
RL Submitted (FEB-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OOG42951.1}.
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; MUNO01000018; OOG42951.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S8FHZ0; -.
DR STRING; 1944133.B0B52_09865; -.
DR OrthoDB; 5294844at2; -.
DR UniPathway; UPA00540; UER00598.
DR Proteomes; UP000218978; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000218978};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00742, ECO:0000313|EMBL:OOG42951.1}.
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 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 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; 45229 MW; 113C4FE35D8C1DB6 CRC64;
MSKALDGVRI LDFTHVQSGP TCTQLLAWFG ADVIKVERAG EGDATRGQLA DIPGADSLYF
TMLNHNKRSI TLDMKKPKGK EVLDELIKTC DVMVENFAPG ALDRMGMTWE HIHKINPRMI
VASVKGFGPG PYEDLKVYEN VAQCAGGAAS TTGFEDGPPL VTGAQIGDSG TGLHLALGIV
AALYQRNTTG RGQKVLAPMQ DAVLNLCRVK LRDQQRLART GTMHEYPQYP DGKFGDAVPR
AGNASGGGQP GSVLKCKGWE TDPNAYIYFI TQAAVWPAVC KVIGEEGWIT DEAFDTPAAR
LLHLKPIFAR IEKWTMTKTK FEAMEILNKY DIPCGPILSM KEIADEPALR ATGTIVEVDH
PVRGKYLTVG NPIKMSDSAT EVTRSPLLGE HTDEVLAQLG YSPEYIAELR TERVI
//
