ID G7Z846_AZOL4 Unreviewed; 416 AA.
AC G7Z846;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
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 Synonyms=frc1 {ECO:0000313|EMBL:CBS85610.1};
GN OrderedLocusNames=AZOLI_0201 {ECO:0000313|EMBL:CBS85610.1};
OS Azospirillum lipoferum (strain 4B).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS85610.1, ECO:0000313|Proteomes:UP000005667};
RN [1] {ECO:0000313|Proteomes:UP000005667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4B {ECO:0000313|Proteomes:UP000005667};
RX PubMed=22216014; DOI=10.1371/journal.pgen.1002430;
RA Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G.,
RA Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., Robertson J.S.,
RA Barbe V., Calteau A., Rouy Z., Mangenot S., Prigent-Combaret C.,
RA Normand P., Boyer M., Siguier P., Dessaux Y., Elmerich C., Condemine G.,
RA Krishnen G., Kennedy I., Paterson A.H., Gonzalez V., Mavingui P.,
RA Zhulin I.B.;
RT "Azospirillum genomes reveal transition of bacteria from aquatic to
RT terrestrial environments.";
RL PLoS Genet. 7:E1002430-E1002430(2011).
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|ARBA:ARBA00025298, ECO:0000256|HAMAP-
CC 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; FQ311868; CBS85610.1; -; Genomic_DNA.
DR RefSeq; WP_014246676.1; NC_016622.1.
DR AlphaFoldDB; G7Z846; -.
DR STRING; 862719.AZOLI_0201; -.
DR KEGG; ali:AZOLI_0201; -.
DR HOGENOM; CLU_033975_2_1_5; -.
DR OrthoDB; 9781472at2; -.
DR UniPathway; UPA00540; UER00598.
DR Proteomes; UP000005667; 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; 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:CBS85610.1}.
FT ACT_SITE 169
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00742"
FT BINDING 15..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 137..140
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00742"
FT BINDING 248..250
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00742"
SQ SEQUENCE 416 AA; 45532 MW; 06D37FDC3A70FDA4 CRC64;
MTKPLEGIKI IDFTHVQAGP ACTQLLAWYG ADVIKVERPG AGDVTRSQLR DIPGADALYF
TMLNSNKRSL TLDTKTAEGK EVLERLIKES DVLVENFGPG ALDRMGFSWD RIKELNPGMI
VASVKGFSDG HHYQDLKVYE NVAQCAGGAA STTGFWDGPP TVSAAALGDS NTGMHLAIGI
LTALMARTKT GKGQKVAVSM QDSVLNLCRV KLRDQQRLDR VGYLEEYPQY PHGKFTDVVP
RGGNAGGGGQ PGWVLKCKGW ETDPNAYIYF TIQGHAWAPI CKALGREEWI DDPAYNTAEA
RQDKIFDIFA IIEDWLKDKT KFEAVDILRK YDIPCAPVLS MKEIANDPSL RASGTVVEVD
HKVRGKYLTV GSPIKFSDMT VEVTGSPLLG EHTDEVLAQL GYSKDQIAAM HQAKVV
//
