ID A0A411X4E3_9BURK Unreviewed; 415 AA.
AC A0A411X4E3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
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 ECO:0000313|EMBL:QBI03889.1};
GN ORFNames=EYF70_26055 {ECO:0000313|EMBL:QBI03889.1}, GCM10007387_00450
GN {ECO:0000313|EMBL:GGY23036.1};
OS Pseudoduganella albidiflava.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Pseudoduganella.
OX NCBI_TaxID=321983 {ECO:0000313|EMBL:QBI03889.1, ECO:0000313|Proteomes:UP000292307};
RN [1] {ECO:0000313|EMBL:GGY23036.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KCTC 12343 {ECO:0000313|EMBL:GGY23036.1};
RX PubMed=30832757;
RA Wu L., Ma J.;
RT "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT project: providing services to taxonomists for standard genome sequencing
RT and annotation.";
RL Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN [2] {ECO:0000313|EMBL:QBI03889.1, ECO:0000313|Proteomes:UP000292307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17472 {ECO:0000313|EMBL:QBI03889.1,
RC ECO:0000313|Proteomes:UP000292307};
RA Miess H., Frediansyhah A., Gross H.;
RT "Draft Genome Sequences of Six Type Strains of the Genus Massilia.";
RL Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:GGY23036.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KCTC 12343 {ECO:0000313|EMBL:GGY23036.1};
RA Sun Q., Kim S.;
RL Submitted (DEC-2022) 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; BMWV01000001; GGY23036.1; -; Genomic_DNA.
DR EMBL; CP036401; QBI03889.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A411X4E3; -.
DR KEGG; mali:EYF70_26055; -.
DR OrthoDB; 8523055at2; -.
DR UniPathway; UPA00540; UER00598.
DR Proteomes; UP000292307; Chromosome.
DR Proteomes; UP000628442; 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 Transferase {ECO:0000256|HAMAP-Rule:MF_00742, ECO:0000313|EMBL:QBI03889.1}.
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; 45475 MW; D10526AEDEEA16CC CRC64;
MSKALEGIRI LDFTHVQSGP TCTQLLAWFG ADVIKIERAG EGDATRAQLR DIPDVDSLYF
TMLNHNKRSM TLDTKRPAGK AVLETLIRDC DVLVENFAPG AMDRMGFSWE RISELNPRMI
VASVKGFGPG PYEQCKVYEN VAQCAGGSAA TTGFDDGPPV VTGAQIGDSG SGLHLALGIV
TALFQRTATG RGQRVQIAMQ DAVLNLCRVK LRDQQRLERT GVMEEYPQYA NGRFGESVPR
AGNASGGGQP GWILKCKGWE TDPNAYIYFI AQAAVWPAIC RVIGREGWID DPAYATPRAR
LPHLMQIFAT VEEWTKTLTK FEVMEILNRD DIPCGPILSM KELAEEPSLR ATGTIVEVDH
PERGPYLTVG NPIKLSDSPT TVRRSPLLGE HTGEVLSQLG YSDEQIAALR AERVI
//
