ID   FCTA_STRCO              Reviewed;         410 AA.
AC   O87838;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 119.
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=SCO6583;
GN   ORFNames=SC8A6.04c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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; AL939128; CAA19776.1; -; Genomic_DNA.
DR   PIR; T35771; T35771.
DR   RefSeq; NP_630662.1; NC_003888.3.
DR   RefSeq; WP_003972395.1; NZ_VNID01000002.1.
DR   AlphaFoldDB; O87838; -.
DR   SMR; O87838; -.
DR   STRING; 100226.SCO6583; -.
DR   GeneID; 1102022; -.
DR   KEGG; sco:SCO6583; -.
DR   PATRIC; fig|100226.15.peg.6688; -.
DR   eggNOG; COG1804; Bacteria.
DR   HOGENOM; CLU_033975_2_1_11; -.
DR   InParanoid; O87838; -.
DR   OMA; KFDIPCA; -.
DR   PhylomeDB; O87838; -.
DR   BRENDA; 2.8.3.16; 5998.
DR   UniPathway; UPA00540; UER00598.
DR   Proteomes; UP000001973; 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..410
FT                   /note="Formyl-CoA:oxalate CoA-transferase"
FT                   /id="PRO_0000194724"
FT   REGION          221..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        168
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00742"
FT   BINDING         18..19
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         72..75
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         96..98
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00742"
FT   BINDING         136..139
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         243..245
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   410 AA;  44664 MW;  3760A61D3D3DCAA4 CRC64;
     MTAKALEGIR VLDMTHVQSG PSATQLLAWL GADVVKLEAP HGDITRGQLR DLPDVDSLYF
     TMLNCNKRSI TLNTKSERGK EILTELIRRS DVMVENFGPG AVDRMGFTWD RVKEINPRIV
     YASIKGFGEG PYTAFKAYEV VAQAMGGSMS TTGFEDGPPL ATGAQIGDSG TGVHVVAGIL
     AALYQREHTG RGQRVNVAMQ HAVLNLCRVK LRDQQRLSHG PLAEYPNEDF GDEVPRSGNA
     SGGGQPGWAV KCAPGGPNDY VYVIVQPVGW QPLSELIGRP ELAEDPEWAT PRARLPKLNK
     MFQLIEEWSS TLPKWEVLER LNAHNIPCGP ILSTKEIIED DSLVANEMVV TVPHPERGEF
     VTVGSPLKLS DSPVEVTSSP LLGEHNEEVY VGELGLGDEE LRLLKSSGVI