FCTA_STRAW
ID FCTA_STRAW Reviewed; 409 AA.
AC Q82M40;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Formyl-CoA:oxalate CoA-transferase;
DE Short=FCOCT;
DE EC=2.8.3.16 {ECO:0000255|HAMAP-Rule:MF_00742};
DE AltName: Full=Formyl-coenzyme A transferase {ECO:0000255|HAMAP-Rule:MF_00742};
DE Short=Formyl-CoA transferase {ECO:0000255|HAMAP-Rule:MF_00742};
GN Name=frc {ECO:0000255|HAMAP-Rule:MF_00742}; OrderedLocusNames=SAV_1820;
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=227882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT deducing the ability of producing secondary metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(2003).
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 (By similarity). {ECO:0000250}.
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:0000255|HAMAP-Rule:MF_00742};
CC -!- PATHWAY: Metabolic intermediate degradation; oxalate degradation; CO(2)
CC and formate from oxalate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00742}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00742}.
CC -!- SIMILARITY: Belongs to the CoA-transferase III family. Frc subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00742}.
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DR EMBL; BA000030; BAC69531.1; -; Genomic_DNA.
DR RefSeq; WP_010983259.1; NZ_JZJK01000086.1.
DR AlphaFoldDB; Q82M40; -.
DR SMR; Q82M40; -.
DR STRING; 227882.SAV_1820; -.
DR EnsemblBacteria; BAC69531; BAC69531; SAVERM_1820.
DR KEGG; sma:SAVERM_1820; -.
DR eggNOG; COG1804; Bacteria.
DR HOGENOM; CLU_033975_2_1_11; -.
DR OMA; KFDIPCA; -.
DR OrthoDB; 969868at2; -.
DR BRENDA; 2.8.3.16; 5980.
DR UniPathway; UPA00540; UER00598.
DR Proteomes; UP000000428; 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; -; 1.
DR Gene3D; 3.40.50.10540; -; 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 Pfam; PF02515; CoA_transf_3; 1.
DR SUPFAM; SSF89796; SSF89796; 1.
DR TIGRFAMs; TIGR03253; oxalate_frc; 1.
PE 3: Inferred from homology;
KW Reference proteome; Transferase.
FT CHAIN 1..409
FT /note="Formyl-CoA:oxalate CoA-transferase"
FT /id="PRO_0000194723"
FT REGION 221..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 167
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00742"
FT BINDING 17..18
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 71..74
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 95..97
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00742"
FT BINDING 135..138
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 242..244
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 409 AA; 44360 MW; 8204C8A684585A7B CRC64;
MTKALEGIRV LDMTHVQSGP SATQLLAWLG ADVVKLEAPT GDITRGQLRD LPDVDSLYFT
MLNCNKRSIT LNTKTERGKE ILTELIRRSD VMVENFGPGA VDRMGFTWDR IRDINPRIVY
ASIKGFGDGP YTDFKAYEVV AQAMGGSMST TGFEDGPPLA TGAQIGDSGT GIHAVAGILA
ALYQRENTGR GQRVNVAMQH AVLNLCRVKL RDQQRLAHGP LAEYPNDDFG DEVPRSGNAS
GGGQPGWAVK CAPGGPNDYV YVIVQPVGWK PLSELIGRPE LADDPEWATP EARLPQLTKM
FQLIEEWSAT LPKWEVLEKL NAHNIPCGPI LSTKEIVEDA SLVANEMVVT VPHPERGEFV
TVGSPLKLSD SPVDVTSSPL LGEHNAEVYV GELGLGDEEL RLLKSNGVI
