FCTA_OXAFO
ID FCTA_OXAFO Reviewed; 428 AA.
AC O06644;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 130.
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:15213226, ECO:0000269|PubMed:18162462, ECO:0000269|PubMed:18245280, ECO:0000269|PubMed:2361939, ECO:0000269|PubMed:9150242};
DE AltName: Full=Formyl-coenzyme A transferase {ECO:0000255|HAMAP-Rule:MF_00742};
GN Name=frc {ECO:0000255|HAMAP-Rule:MF_00742};
OS Oxalobacter formigenes.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Oxalobacter.
OX NCBI_TaxID=847;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS,
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=OxB;
RX PubMed=9150242; DOI=10.1128/jb.179.10.3378-3381.1997;
RA Sidhu H., Ogden S.D., Lung H.-Y., Luttge B.G., Baetz A.L., Peck A.B.;
RT "DNA sequencing and expression of the formyl coenzyme A transferase gene,
RT frc, from Oxalobacter formigenes.";
RL J. Bacteriol. 179:3378-3381(1997).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, SUBCELLULAR LOCATION, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RC STRAIN=OxB;
RX PubMed=2361939; DOI=10.1128/jb.172.7.3537-3540.1990;
RA Baetz A.L., Allison M.J.;
RT "Purification and characterization of formyl-coenzyme A transferase from
RT Oxalobacter formigenes.";
RL J. Bacteriol. 172:3537-3540(1990).
RN [3] {ECO:0007744|PDB:1P5H, ECO:0007744|PDB:1P5R}
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH COENZYME A, AND
RP SUBUNIT.
RX PubMed=12839984; DOI=10.1093/emboj/cdg333;
RA Ricagno S., Jonsson S., Richards N., Lindqvist Y.;
RT "Formyl-CoA transferase encloses the CoA binding site at the interface of
RT an interlocked dimer.";
RL EMBO J. 22:3210-3219(2003).
RN [4] {ECO:0007744|PDB:1T3Z, ECO:0007744|PDB:1T4C, ECO:0007744|PDB:1VGQ, ECO:0007744|PDB:1VGR}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 2-428 OF MUTANTS ALA-169;
RP GLU-169; SER-169 IN COMPLEX WITH COENZYME A, FUNCTION, CATALYTIC ACTIVITY,
RP MUTAGENESIS OF ASP-169, ACTIVE SITE, BIOPHYSICOCHEMICAL PROPERTIES,
RP REACTION MECHANISM, AND SUBUNIT.
RX PubMed=15213226; DOI=10.1074/jbc.m404873200;
RA Jonsson S., Ricagno S., Lindqvist Y., Richards N.G.;
RT "Kinetic and mechanistic characterization of the formyl-CoA transferase
RT from Oxalobacter formigenes.";
RL J. Biol. Chem. 279:36003-36012(2004).
RN [5] {ECO:0007744|PDB:2VJP, ECO:0007744|PDB:2VJQ}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF MUTANTS PRO-48 AND PHE-48,
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF TRP-48, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, SUBSTRATE SPECIFICITY, AND SUBUNIT.
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] {ECO:0007744|PDB:2VJK, ECO:0007744|PDB:2VJL, ECO:0007744|PDB:2VJM, ECO:0007744|PDB:2VJN, ECO:0007744|PDB:2VJO}
RP X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF MUTANTS ALA-17 AND ALA-260 IN
RP COMPLEX WITH COENZYME A AND SUBSTRATE ANALOGS, FUNCTION, CATALYTIC
RP ACTIVITY, MUTAGENESIS OF GLN-17; GLY-259 AND GLY-260, BIOPHYSICOCHEMICAL
RP PROPERTIES, MASS SPECTROMETRY, ACTIVITY REGULATION, REACTION MECHANISM, AND
RP SUBUNIT.
RX PubMed=18162462; DOI=10.1074/jbc.m709353200;
RA Berthold C.L., Toyota C.G., Richards N.G., Lindqvist Y.;
RT "Reinvestigation of the catalytic mechanism of formyl-CoA transferase, a
RT class III CoA-transferase.";
RL J. Biol. Chem. 283:6519-6529(2008).
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). Essential enzyme for the bacterium survival, as it
CC relies on oxalic acid as its sole source of energy. Catalyzes the
CC transfer of the CoA moiety from formyl-CoA to oxalate (PubMed:15213226,
CC PubMed:18162462, PubMed:18245280, PubMed:2361939, PubMed:9150242). It
CC can also use succinate as acceptor (PubMed:18245280, PubMed:2361939).
CC {ECO:0000269|PubMed:15213226, ECO:0000269|PubMed:18162462,
CC ECO:0000269|PubMed:18245280, ECO:0000269|PubMed:2361939,
CC ECO:0000269|PubMed:9150242}.
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:15213226, ECO:0000269|PubMed:18162462,
CC ECO:0000269|PubMed:18245280, ECO:0000269|PubMed:2361939,
CC ECO:0000269|PubMed:9150242};
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, ECO:0000269|PubMed:2361939};
CC -!- ACTIVITY REGULATION: Inhibited by the sulfhydryl reagents N-
CC ethylmaleimide and p-chloromercuribenzoate, and by chloride.
CC Competitively inhibited by acetyl-CoA. {ECO:0000269|PubMed:18162462,
CC ECO:0000269|PubMed:18245280, ECO:0000269|PubMed:2361939}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2 uM for formyl-CoA (with oxalate as acceptor at pH 6.7 and 30
CC degrees Celsius) {ECO:0000269|PubMed:18162462,
CC ECO:0000269|PubMed:18245280};
CC KM=8 uM for formyl-CoA (with oxalate as acceptor at pH 6.7 and 30
CC degrees Celsius) {ECO:0000269|PubMed:15213226};
CC KM=16 uM for formyl-CoA (with succinate as acceptor at pH 6.7 and 30
CC degrees Celsius) {ECO:0000269|PubMed:18245280};
CC KM=0.32 mM for succinate (with formyl-CoA as donor at pH 6.7 and 30
CC degrees Celsius) {ECO:0000269|PubMed:18245280};
CC KM=2.3 mM for succinate (with formyl-CoA as donor at pH 6.8 and 25
CC degrees Celsius) {ECO:0000269|PubMed:2361939};
CC KM=3 mM for formyl-CoA (with oxalate as acceptor at pH 6.8 and 25
CC degrees Celsius) {ECO:0000269|PubMed:2361939};
CC KM=3.9 mM for oxalate (with formyl-CoA as donor at pH 6.7 and 30
CC degrees Celsius) {ECO:0000269|PubMed:15213226,
CC ECO:0000269|PubMed:18245280};
CC KM=5.1 mM for oxalate {ECO:0000269|PubMed:2361939};
CC Vmax=6.4 umol/min/mg enzyme with oxalate as substrate (with formyl-
CC CoA as donor at pH 6.8 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:2361939};
CC Vmax=19.2 umol/min/mg enzyme with succinate as substrate (with
CC formyl-CoA as donor at pH 6.8 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:2361939};
CC Vmax=29.6 umol/min/mg enzyme with formyl-CoA as substrate (with
CC oxalate as acceptor at pH 6.8 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:2361939};
CC Note=kcat is 5.3 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 149 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). {ECO:0000269|PubMed:18245280};
CC pH dependence:
CC Optimum pH is between 6.5 and 7.5. {ECO:0000269|PubMed:15213226,
CC ECO:0000269|PubMed:18162462, ECO:0000269|PubMed:18245280,
CC ECO:0000269|PubMed:2361939};
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:12839984, ECO:0000269|PubMed:15213226,
CC ECO:0000269|PubMed:18162462, ECO:0000269|PubMed:18245280,
CC ECO:0000269|PubMed:2361939}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:2361939}.
CC -!- MASS SPECTROMETRY: Mass=47196; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:18162462};
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; U82167; AAC45298.1; -; Genomic_DNA.
DR RefSeq; WP_005880857.1; NZ_CP042242.1.
DR PDB; 1P5H; X-ray; 2.20 A; A/B=1-428.
DR PDB; 1P5R; X-ray; 2.50 A; A/B=1-428.
DR PDB; 1T3Z; X-ray; 2.30 A; A/B=2-428.
DR PDB; 1T4C; X-ray; 2.61 A; A/B=2-428.
DR PDB; 1VGQ; X-ray; 2.13 A; A/B=2-428.
DR PDB; 1VGR; X-ray; 2.10 A; A/B=2-428.
DR PDB; 2VJK; X-ray; 1.97 A; A/B=1-428.
DR PDB; 2VJL; X-ray; 2.00 A; A/B=1-428.
DR PDB; 2VJM; X-ray; 1.89 A; A/B=1-428.
DR PDB; 2VJN; X-ray; 2.00 A; A/B=1-428.
DR PDB; 2VJO; X-ray; 2.20 A; A/B=1-428.
DR PDB; 2VJP; X-ray; 1.95 A; A/B=1-428.
DR PDB; 2VJQ; X-ray; 1.80 A; A/B/C/D=1-428.
DR PDBsum; 1P5H; -.
DR PDBsum; 1P5R; -.
DR PDBsum; 1T3Z; -.
DR PDBsum; 1T4C; -.
DR PDBsum; 1VGQ; -.
DR PDBsum; 1VGR; -.
DR PDBsum; 2VJK; -.
DR PDBsum; 2VJL; -.
DR PDBsum; 2VJM; -.
DR PDBsum; 2VJN; -.
DR PDBsum; 2VJO; -.
DR PDBsum; 2VJP; -.
DR PDBsum; 2VJQ; -.
DR AlphaFoldDB; O06644; -.
DR SMR; O06644; -.
DR DrugBank; DB01992; Coenzyme A.
DR DrugBank; DB01846; Oxidized coenzyme A.
DR KEGG; ag:AAC45298; -.
DR KEGG; ofo:BRW83_1110; -.
DR BioCyc; MetaCyc:MON-16179; -.
DR BRENDA; 2.8.3.16; 4478.
DR UniPathway; UPA00540; UER00598.
DR EvolutionaryTrace; O06644; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 2.
DR SUPFAM; SSF89796; SSF89796; 1.
DR TIGRFAMs; TIGR03253; oxalate_frc; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..428
FT /note="Formyl-CoA:oxalate CoA-transferase"
FT /id="PRO_0000194720"
FT ACT_SITE 169
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00742,
FT ECO:0000269|PubMed:15213226"
FT BINDING 15..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:12839984, ECO:0000269|PubMed:15213226,
FT ECO:0000269|PubMed:18162462"
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 ECO:0000269|PubMed:12839984, ECO:0000269|PubMed:15213226,
FT ECO:0000269|PubMed:18162462"
FT BINDING 137..140
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT BINDING 260..262
FT /ligand="substrate"
FT MUTAGEN 17
FT /note="Q->A: 45-fold decrease of the catalytic effiency."
FT /evidence="ECO:0000269|PubMed:18162462"
FT MUTAGEN 48
FT /note="W->F: Little change in the affinity binding and
FT catalytic efficiency, and it does not display major
FT structural changes."
FT /evidence="ECO:0000269|PubMed:18245280"
FT MUTAGEN 48
FT /note="W->P: Little change in the affinity binding and
FT catalytic efficiency. It exhibits substrate inhibition with
FT oxalate. It does not display major structural changes."
FT /evidence="ECO:0000269|PubMed:18245280"
FT MUTAGEN 169
FT /note="D->A: Loss of CoA-transferase activity."
FT /evidence="ECO:0000269|PubMed:15213226"
FT MUTAGEN 169
FT /note="D->E: Loss of CoA-transferase activity."
FT /evidence="ECO:0000269|PubMed:15213226"
FT MUTAGEN 169
FT /note="D->S: Loss of CoA-transferase activity."
FT /evidence="ECO:0000269|PubMed:15213226"
FT MUTAGEN 259
FT /note="G->A: 2.5-fold decrease of the catalytic effiency."
FT /evidence="ECO:0000269|PubMed:18162462"
FT MUTAGEN 260
FT /note="G->A: 25-fold decrease of the catalytic effiency.
FT Reduction of the affinity binding for both formyl-CoA and
FT oxalate."
FT /evidence="ECO:0000269|PubMed:18162462"
FT TURN 4..7
FT /evidence="ECO:0007829|PDB:2VJQ"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:2VJQ"
FT HELIX 18..28
FT /evidence="ECO:0007829|PDB:2VJQ"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:2VJQ"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:2VJQ"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:2VJQ"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:2VJQ"
FT TURN 62..66
FT /evidence="ECO:0007829|PDB:1T4C"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:2VJQ"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:2VJK"
FT HELIX 77..89
FT /evidence="ECO:0007829|PDB:2VJQ"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:2VJQ"
FT HELIX 101..104
FT /evidence="ECO:0007829|PDB:2VJQ"
FT HELIX 109..115
FT /evidence="ECO:0007829|PDB:2VJQ"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:2VJQ"
FT TURN 132..135
FT /evidence="ECO:0007829|PDB:2VJQ"
FT HELIX 140..146
FT /evidence="ECO:0007829|PDB:2VJQ"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:2VJQ"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:2VJQ"
FT HELIX 169..190
FT /evidence="ECO:0007829|PDB:2VJQ"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:2VJQ"
FT HELIX 200..207
FT /evidence="ECO:0007829|PDB:2VJQ"
FT HELIX 209..221
FT /evidence="ECO:0007829|PDB:2VJQ"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:2VJQ"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:2VJK"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:1T4C"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:2VJQ"
FT STRAND 261..268
FT /evidence="ECO:0007829|PDB:2VJQ"
FT TURN 270..274
FT /evidence="ECO:0007829|PDB:2VJQ"
FT STRAND 279..283
FT /evidence="ECO:0007829|PDB:2VJQ"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:2VJQ"
FT HELIX 289..295
FT /evidence="ECO:0007829|PDB:2VJQ"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:2VJQ"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:2VJQ"
FT HELIX 310..313
FT /evidence="ECO:0007829|PDB:2VJQ"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:2VJQ"
FT HELIX 317..326
FT /evidence="ECO:0007829|PDB:2VJQ"
FT TURN 327..330
FT /evidence="ECO:0007829|PDB:2VJQ"
FT HELIX 333..342
FT /evidence="ECO:0007829|PDB:2VJQ"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:2VJQ"
FT HELIX 353..357
FT /evidence="ECO:0007829|PDB:2VJQ"
FT HELIX 360..364
FT /evidence="ECO:0007829|PDB:2VJQ"
FT STRAND 367..371
FT /evidence="ECO:0007829|PDB:2VJQ"
FT TURN 374..376
FT /evidence="ECO:0007829|PDB:2VJQ"
FT STRAND 379..382
FT /evidence="ECO:0007829|PDB:2VJQ"
FT STRAND 385..390
FT /evidence="ECO:0007829|PDB:2VJQ"
FT TURN 401..404
FT /evidence="ECO:0007829|PDB:2VJQ"
FT HELIX 405..411
FT /evidence="ECO:0007829|PDB:2VJQ"
FT HELIX 416..424
FT /evidence="ECO:0007829|PDB:2VJQ"
SQ SEQUENCE 428 AA; 47327 MW; 386E87C19EA0C8AC CRC64;
MTKPLDGINV LDFTHVQAGP ACTQMMGFLG ANVIKIERRG SGDMTRGWLQ DKPNVDSLYF
TMFNCNKRSI ELDMKTPEGK ELLEQMIKKA DVMVENFGPG ALDRMGFTWE YIQELNPRVI
LASVKGYAEG HANEHLKVYE NVAQCSGGAA ATTGFWDGPP TVSGAALGDS NSGMHLMIGI
LAALEMRHKT GRGQKVAVAM QDAVLNLVRI KLRDQQRLER TGILAEYPQA QPNFAFDRDG
NPLSFDNITS VPRGGNAGGG GQPGWMLKCK GWETDADSYV YFTIAANMWP QICDMIDKPE
WKDDPAYNTF EGRVDKLMDI FSFIETKFAD KDKFEVTEWA AQYGIPCGPV MSMKELAHDP
SLQKVGTVVE VVDEIRGNHL TVGAPFKFSG FQPEITRAPL LGEHTDEVLK ELGLDDAKIK
ELHAKQVV
