FCTA_ECOLI
ID FCTA_ECOLI Reviewed; 416 AA.
AC P69902; P77407;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Formyl-CoA:oxalate CoA-transferase;
DE Short=FCOCT;
DE EC=2.8.3.16 {ECO:0000255|HAMAP-Rule:MF_00742, ECO:0000269|PubMed:18245280};
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}; Synonyms=yfdW;
GN OrderedLocusNames=b2374, JW2371;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP INDUCTION.
RX PubMed=12694615; DOI=10.1046/j.1365-2958.2003.03477.x;
RA Masuda N., Church G.M.;
RT "Regulatory network of acid resistance genes in Escherichia coli.";
RL Mol. Microbiol. 48:699-712(2003).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP SPECIFICITY.
RX PubMed=18245280; DOI=10.1128/jb.01823-07;
RA Toyota C.G., Berthold C.L., Gruez A., Jonsson S., Lindqvist Y.,
RA Cambillau C., Richards N.G.;
RT "Differential substrate specificity and kinetic behavior of Escherichia
RT coli YfdW and Oxalobacter formigenes formyl coenzyme A transferase.";
RL J. Bacteriol. 190:2556-2564(2008).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=23335415; DOI=10.1128/jb.01936-12;
RA Fontenot E.M., Ezelle K.E., Gabreski L.N., Giglio E.R., McAfee J.M.,
RA Mills A.C., Qureshi M.N., Salmon K.M., Toyota C.G.;
RT "YfdW and YfdU are required for oxalate-induced acid tolerance in
RT Escherichia coli K-12.";
RL J. Bacteriol. 195:1446-1455(2013).
RN [7] {ECO:0007744|PDB:1PT5, ECO:0007744|PDB:1PT7, ECO:0007744|PDB:1PT8}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS,
RP FUNCTION, ACTIVE SITE, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=12844490; DOI=10.1074/jbc.c300282200;
RA Gruez A., Roig-Zamboni V., Valencia C., Campanacci V., Cambillau C.;
RT "The crystal structure of the Escherichia coli YfdW gene product reveals a
RT new fold of two interlaced rings identifying a wide family of CoA
RT transferases.";
RL J. Biol. Chem. 278:34582-34586(2003).
RN [8] {ECO:0007744|PDB:1PQY, ECO:0007744|PDB:1Q6Y, ECO:0007744|PDB:1Q7E}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-416 IN COMPLEX WITH COENZYME A,
RP AND SUBUNIT.
RX PubMed=14993676; DOI=10.1107/s0907444904000034;
RA Gogos A., Gorman J., Shapiro L.;
RT "Structure of Escherichia coli YfdW, a type III CoA transferase.";
RL Acta Crystallogr. D 60:507-511(2004).
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. It can also use succinate as an acceptor.
CC {ECO:0000269|PubMed:12844490, ECO:0000269|PubMed:18245280,
CC ECO:0000269|PubMed:23335415}.
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 ECO:0000269|PubMed:18245280};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=formyl-CoA + succinate = formate + succinyl-CoA;
CC Xref=Rhea:RHEA:71735, ChEBI:CHEBI:15740, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:57292, ChEBI:CHEBI:57376;
CC Evidence={ECO:0000269|PubMed:18245280};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=180 uM for formyl-CoA (with succinate as acceptor at pH 6.7 and 30
CC degrees Celsius) {ECO:0000269|PubMed:18245280};
CC KM=352 uM for formyl-CoA (with oxalate as acceptor at pH 6.7 and 30
CC degrees Celsius) {ECO:0000269|PubMed:18245280};
CC KM=510 uM for oxalate (with formyl-CoA as donor at pH 6.7 and 30
CC degrees Celsius) {ECO:0000269|PubMed:18245280};
CC KM=80 mM for succinate (with formyl-CoA as donor at pH 6.7 and 30
CC degrees Celsius) {ECO:0000269|PubMed:18245280};
CC Note=kcat is 130 sec(-1) for CoA-transferase activity with formyl-CoA
CC as substrate (with oxalate as acceptor at pH 6.7 and 30 degrees
CC Celsius). kcat is 5.3 sec(-1) for CoA-transferase activity with
CC formyl-CoA as substrate (with succinate as acceptor at pH 6.7 and 30
CC degrees Celsius).;
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 ECO:0000269|PubMed:12844490, ECO:0000269|PubMed:14993676}.
CC -!- INDUCTION: By the acid response regulator EvgA.
CC {ECO:0000269|PubMed:12694615, ECO:0000269|PubMed:23335415}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a reduced acid
CC tolerance response (ATR) during the adaptation phase. However the
CC deletion of YfdW has no effect on survival in oxalate-containing
CC challenge medium. {ECO:0000269|PubMed:23335415}.
CC -!- SIMILARITY: Belongs to the CoA-transferase III family. Frc subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00742, ECO:0000305}.
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DR EMBL; U00096; AAC75433.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16247.1; -; Genomic_DNA.
DR PIR; C65011; C65011.
DR RefSeq; NP_416875.1; NC_000913.3.
DR RefSeq; WP_000106759.1; NZ_STEB01000008.1.
DR PDB; 1PQY; X-ray; 2.35 A; A=2-416.
DR PDB; 1PT5; X-ray; 2.00 A; A/B=1-416.
DR PDB; 1PT7; X-ray; 1.80 A; A/B=1-416.
DR PDB; 1PT8; X-ray; 2.20 A; A/B=1-416.
DR PDB; 1Q6Y; X-ray; 1.99 A; A=2-416.
DR PDB; 1Q7E; X-ray; 1.60 A; A=2-416.
DR PDBsum; 1PQY; -.
DR PDBsum; 1PT5; -.
DR PDBsum; 1PT7; -.
DR PDBsum; 1PT8; -.
DR PDBsum; 1Q6Y; -.
DR PDBsum; 1Q7E; -.
DR AlphaFoldDB; P69902; -.
DR SMR; P69902; -.
DR BioGRID; 4260863; 11.
DR BioGRID; 851183; 3.
DR IntAct; P69902; 4.
DR STRING; 511145.b2374; -.
DR PaxDb; P69902; -.
DR PRIDE; P69902; -.
DR DNASU; 946842; -.
DR EnsemblBacteria; AAC75433; AAC75433; b2374.
DR EnsemblBacteria; BAA16247; BAA16247; BAA16247.
DR GeneID; 66673756; -.
DR GeneID; 946842; -.
DR KEGG; ecj:JW2371; -.
DR KEGG; eco:b2374; -.
DR PATRIC; fig|1411691.4.peg.4355; -.
DR EchoBASE; EB3897; -.
DR eggNOG; COG1804; Bacteria.
DR HOGENOM; CLU_033975_2_1_6; -.
DR InParanoid; P69902; -.
DR OMA; KFDIPCA; -.
DR PhylomeDB; P69902; -.
DR BioCyc; EcoCyc:G7237-MON; -.
DR BioCyc; MetaCyc:G7237-MON; -.
DR BRENDA; 2.8.3.16; 2026.
DR UniPathway; UPA00540; UER00598.
DR EvolutionaryTrace; P69902; -.
DR PRO; PR:P69902; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0033608; F:formyl-CoA transferase activity; IDA:EcoCyc.
DR GO; GO:0071468; P:cellular response to acidic pH; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Transferase.
FT CHAIN 1..416
FT /note="Formyl-CoA:oxalate CoA-transferase"
FT /id="PRO_0000194716"
FT ACT_SITE 169
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:12844490"
FT BINDING 17..18
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT BINDING 38
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00742,
FT ECO:0000269|PubMed:14993676"
FT BINDING 72..75
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT BINDING 96..98
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT BINDING 104
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00742"
FT BINDING 137..140
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT BINDING 248..250
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 273..275
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT TURN 4..7
FT /evidence="ECO:0007829|PDB:1Q7E"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:1Q7E"
FT HELIX 18..28
FT /evidence="ECO:0007829|PDB:1Q7E"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:1Q7E"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:1Q7E"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:1Q7E"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:1Q7E"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:1Q7E"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:1Q7E"
FT HELIX 77..89
FT /evidence="ECO:0007829|PDB:1Q7E"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:1Q7E"
FT HELIX 101..104
FT /evidence="ECO:0007829|PDB:1PT7"
FT HELIX 109..115
FT /evidence="ECO:0007829|PDB:1Q7E"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:1Q7E"
FT TURN 132..135
FT /evidence="ECO:0007829|PDB:1Q7E"
FT HELIX 140..146
FT /evidence="ECO:0007829|PDB:1Q7E"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:1Q7E"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:1Q7E"
FT HELIX 170..190
FT /evidence="ECO:0007829|PDB:1Q7E"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:1Q7E"
FT HELIX 200..207
FT /evidence="ECO:0007829|PDB:1Q7E"
FT HELIX 209..221
FT /evidence="ECO:0007829|PDB:1Q7E"
FT TURN 228..232
FT /evidence="ECO:0007829|PDB:1Q7E"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:1Q7E"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:1Q7E"
FT TURN 258..262
FT /evidence="ECO:0007829|PDB:1Q7E"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:1Q7E"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:1Q7E"
FT HELIX 277..283
FT /evidence="ECO:0007829|PDB:1Q7E"
FT HELIX 287..290
FT /evidence="ECO:0007829|PDB:1Q7E"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:1Q7E"
FT HELIX 298..301
FT /evidence="ECO:0007829|PDB:1Q7E"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:1Q7E"
FT HELIX 305..316
FT /evidence="ECO:0007829|PDB:1Q7E"
FT HELIX 321..328
FT /evidence="ECO:0007829|PDB:1Q7E"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:1Q7E"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:1Q7E"
FT HELIX 341..346
FT /evidence="ECO:0007829|PDB:1Q7E"
FT HELIX 348..352
FT /evidence="ECO:0007829|PDB:1Q7E"
FT STRAND 355..361
FT /evidence="ECO:0007829|PDB:1Q7E"
FT TURN 362..364
FT /evidence="ECO:0007829|PDB:1Q7E"
FT STRAND 365..370
FT /evidence="ECO:0007829|PDB:1Q7E"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:1PT7"
FT TURN 389..392
FT /evidence="ECO:0007829|PDB:1Q7E"
FT HELIX 393..399
FT /evidence="ECO:0007829|PDB:1Q7E"
FT HELIX 404..416
FT /evidence="ECO:0007829|PDB:1Q7E"
SQ SEQUENCE 416 AA; 45828 MW; 97F7FA4001073301 CRC64;
MSTPLQGIKV LDFTGVQSGP SCTQMLAWFG ADVIKIERPG VGDVTRHQLR DIPDIDALYF
TMLNSNKRSI ELNTKTAEGK EVMEKLIREA DILVENFHPG AIDHMGFTWE HIQEINPRLI
FGSIKGFDEC SPYVNVKAYE NVAQAAGGAA STTGFWDGPP LVSAAALGDS NTGMHLLIGL
LAALLHREKT GRGQRVTMSM QDAVLNLCRV KLRDQQRLDK LGYLEEYPQY PNGTFGDAVP
RGGNAGGGGQ PGWILKCKGW ETDPNAYIYF TIQEQNWENT CKAIGKPEWI TDPAYSTAHA
RQPHIFDIFA EIEKYTVTID KHEAVAYLTQ FDIPCAPVLS MKEISLDPSL RQSGSVVEVE
QPLRGKYLTV GCPMKFSAFT PDIKAAPLLG EHTAAVLQEL GYSDDEIAAM KQNHAI
