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Protein

Formyl-CoA:oxalate CoA-transferase

Gene

frc

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the catabolism of oxalate and in the adapatation to low pH via the induction of the oxalate-dependent acid tolerance response (ATR). Catalyzes the transfer of the CoA moiety from formyl-CoA to oxalate. It can also use succinate as an acceptor.3 Publications

Catalytic activityi

Formyl-CoA + oxalate = formate + oxalyl-CoA.UniRule annotation1 Publication

Kineticsi

Kcat is 130 sec(-1) for CoA-transferase activity with formyl-CoA as substrate (with oxalate as acceptor at pH 6.7 and 30 degrees Celsius). Kcat is 5.3 sec(-1) for CoA-transferase activity with formyl-CoA as substrate (with succinate as acceptor at pH 6.7 and 30 degrees Celsius).

  1. KM=180 µM for formyl-CoA (with succinate as acceptor at pH 6.7 and 30 degrees Celsius)1 Publication
  2. KM=352 µM for formyl-CoA (with oxalate as acceptor at pH 6.7 and 30 degrees Celsius)1 Publication
  3. KM=510 µM for oxalate (with formyl-CoA as donor at pH 6.7 and 30 degrees Celsius)1 Publication
  4. KM=80 mM for succinate (with formyl-CoA as donor at pH 6.7 and 30 degrees Celsius)1 Publication

    Pathwayi: oxalate degradation

    This protein is involved in step 1 of the subpathway that synthesizes CO(2) and formate from oxalate.UniRule annotation
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Formyl-CoA:oxalate CoA-transferase (frc)
    2. Oxalyl-CoA decarboxylase (oxc)
    This subpathway is part of the pathway oxalate degradation, which is itself part of Metabolic intermediate degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes CO(2) and formate from oxalate, the pathway oxalate degradation and in Metabolic intermediate degradation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei38 – 381Coenzyme AUniRule annotation1 Publication
    Binding sitei104 – 1041Coenzyme AUniRule annotation
    Active sitei169 – 1691Nucleophile1 Publication

    GO - Molecular functioni

    • formyl-CoA transferase activity Source: EcoCyc

    GO - Biological processi

    • cellular response to acidic pH Source: EcoCyc
    • oxalate catabolic process Source: UniProtKB-UniPathway
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    BioCyciEcoCyc:G7237-MONOMER.
    ECOL316407:JW2371-MONOMER.
    MetaCyc:G7237-MONOMER.
    BRENDAi2.8.3.16. 2026.
    UniPathwayiUPA00540; UER00598.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Formyl-CoA:oxalate CoA-transferase (EC:2.8.3.16UniRule annotation)
    Short name:
    FCOCT
    Alternative name(s):
    Formyl-coenzyme A transferaseUniRule annotation
    Short name:
    Formyl-CoA transferaseUniRule annotation
    Gene namesi
    Name:frcUniRule annotation
    Synonyms:yfdW
    Ordered Locus Names:b2374, JW2371
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG14145. frc.

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene show a reduced acid tolerance response (ATR) during the adaptation phase. However the deletion of YfdW has no effect on survival in oxalate-containing challenge medium.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 416416Formyl-CoA:oxalate CoA-transferasePRO_0000194716Add
    BLAST

    Proteomic databases

    PaxDbiP69902.
    PRIDEiP69902.

    Expressioni

    Inductioni

    By the acid response regulator EvgA.2 Publications

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation2 Publications

    Protein-protein interaction databases

    BioGridi4260863. 11 interactions.
    IntActiP69902. 4 interactions.
    STRINGi511145.b2374.

    Structurei

    Secondary structure

    1
    416
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni4 – 74Combined sources
    Beta strandi9 – 124Combined sources
    Helixi18 – 2811Combined sources
    Beta strandi32 – 376Combined sources
    Turni39 – 413Combined sources
    Helixi44 – 463Combined sources
    Turni47 – 493Combined sources
    Helixi58 – 614Combined sources
    Beta strandi68 – 714Combined sources
    Helixi77 – 8913Combined sources
    Beta strandi91 – 955Combined sources
    Helixi101 – 1044Combined sources
    Helixi109 – 1157Combined sources
    Beta strandi120 – 1278Combined sources
    Turni132 – 1354Combined sources
    Helixi140 – 1467Combined sources
    Helixi149 – 1524Combined sources
    Turni167 – 1693Combined sources
    Helixi170 – 19021Combined sources
    Beta strandi195 – 1995Combined sources
    Helixi200 – 2078Combined sources
    Helixi209 – 22113Combined sources
    Turni228 – 2325Combined sources
    Beta strandi247 – 2504Combined sources
    Beta strandi252 – 2565Combined sources
    Turni258 – 2625Combined sources
    Beta strandi267 – 2715Combined sources
    Helixi274 – 2763Combined sources
    Helixi277 – 2837Combined sources
    Helixi287 – 2904Combined sources
    Turni293 – 2953Combined sources
    Helixi298 – 3014Combined sources
    Helixi302 – 3043Combined sources
    Helixi305 – 31612Combined sources
    Helixi321 – 3288Combined sources
    Helixi329 – 3313Combined sources
    Beta strandi335 – 3373Combined sources
    Helixi341 – 3466Combined sources
    Helixi348 – 3525Combined sources
    Beta strandi355 – 3617Combined sources
    Turni362 – 3643Combined sources
    Beta strandi365 – 3706Combined sources
    Beta strandi373 – 3764Combined sources
    Turni389 – 3924Combined sources
    Helixi393 – 3997Combined sources
    Helixi404 – 41613Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PQYX-ray2.35A2-416[»]
    1PT5X-ray2.00A/B1-416[»]
    1PT7X-ray1.80A/B1-416[»]
    1PT8X-ray2.20A/B1-416[»]
    1Q6YX-ray1.99A2-416[»]
    1Q7EX-ray1.60A2-416[»]
    ProteinModelPortaliP69902.
    SMRiP69902. Positions 2-416.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP69902.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni17 – 182Coenzyme A binding
    Regioni72 – 754Coenzyme A binding
    Regioni96 – 983Coenzyme A binding
    Regioni137 – 1404Coenzyme A binding
    Regioni248 – 2503Substrate bindingCurated
    Regioni273 – 2753Coenzyme A binding

    Sequence similaritiesi

    Belongs to the CaiB/BaiF CoA-transferase family.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4105C04. Bacteria.
    COG1804. LUCA.
    HOGENOMiHOG000219745.
    InParanoidiP69902.
    KOiK07749.
    OMAiKFDIPCA.
    PhylomeDBiP69902.

    Family and domain databases

    Gene3Di3.40.50.10540. 2 hits.
    HAMAPiMF_00742. Formyl_CoA_transfer. 1 hit.
    InterProiIPR003673. CoA-Trfase_fam_III.
    IPR023606. CoA-Trfase_III_dom.
    IPR017659. Formyl_CoA_transfer.
    [Graphical view]
    PfamiPF02515. CoA_transf_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF89796. SSF89796. 1 hit.
    TIGRFAMsiTIGR03253. oxalate_frc. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P69902-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSTPLQGIKV LDFTGVQSGP SCTQMLAWFG ADVIKIERPG VGDVTRHQLR
    60 70 80 90 100
    DIPDIDALYF TMLNSNKRSI ELNTKTAEGK EVMEKLIREA DILVENFHPG
    110 120 130 140 150
    AIDHMGFTWE HIQEINPRLI FGSIKGFDEC SPYVNVKAYE NVAQAAGGAA
    160 170 180 190 200
    STTGFWDGPP LVSAAALGDS NTGMHLLIGL LAALLHREKT GRGQRVTMSM
    210 220 230 240 250
    QDAVLNLCRV KLRDQQRLDK LGYLEEYPQY PNGTFGDAVP RGGNAGGGGQ
    260 270 280 290 300
    PGWILKCKGW ETDPNAYIYF TIQEQNWENT CKAIGKPEWI TDPAYSTAHA
    310 320 330 340 350
    RQPHIFDIFA EIEKYTVTID KHEAVAYLTQ FDIPCAPVLS MKEISLDPSL
    360 370 380 390 400
    RQSGSVVEVE QPLRGKYLTV GCPMKFSAFT PDIKAAPLLG EHTAAVLQEL
    410
    GYSDDEIAAM KQNHAI
    Length:416
    Mass (Da):45,828
    Last modified:January 4, 2005 - v1
    Checksum:i97F7FA4001073301
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAC75433.1.
    AP009048 Genomic DNA. Translation: BAA16247.1.
    PIRiC65011.
    RefSeqiNP_416875.1. NC_000913.3.
    WP_000106759.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75433; AAC75433; b2374.
    BAA16247; BAA16247; BAA16247.
    GeneIDi946842.
    KEGGiecj:JW2371.
    eco:b2374.
    PATRICi32120127. VBIEscCol129921_2472.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAC75433.1.
    AP009048 Genomic DNA. Translation: BAA16247.1.
    PIRiC65011.
    RefSeqiNP_416875.1. NC_000913.3.
    WP_000106759.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PQYX-ray2.35A2-416[»]
    1PT5X-ray2.00A/B1-416[»]
    1PT7X-ray1.80A/B1-416[»]
    1PT8X-ray2.20A/B1-416[»]
    1Q6YX-ray1.99A2-416[»]
    1Q7EX-ray1.60A2-416[»]
    ProteinModelPortaliP69902.
    SMRiP69902. Positions 2-416.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260863. 11 interactions.
    IntActiP69902. 4 interactions.
    STRINGi511145.b2374.

    Proteomic databases

    PaxDbiP69902.
    PRIDEiP69902.

    Protocols and materials databases

    DNASUi946842.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75433; AAC75433; b2374.
    BAA16247; BAA16247; BAA16247.
    GeneIDi946842.
    KEGGiecj:JW2371.
    eco:b2374.
    PATRICi32120127. VBIEscCol129921_2472.

    Organism-specific databases

    EchoBASEiEB3897.
    EcoGeneiEG14145. frc.

    Phylogenomic databases

    eggNOGiENOG4105C04. Bacteria.
    COG1804. LUCA.
    HOGENOMiHOG000219745.
    InParanoidiP69902.
    KOiK07749.
    OMAiKFDIPCA.
    PhylomeDBiP69902.

    Enzyme and pathway databases

    UniPathwayiUPA00540; UER00598.
    BioCyciEcoCyc:G7237-MONOMER.
    ECOL316407:JW2371-MONOMER.
    MetaCyc:G7237-MONOMER.
    BRENDAi2.8.3.16. 2026.

    Miscellaneous databases

    EvolutionaryTraceiP69902.
    PROiP69902.

    Family and domain databases

    Gene3Di3.40.50.10540. 2 hits.
    HAMAPiMF_00742. Formyl_CoA_transfer. 1 hit.
    InterProiIPR003673. CoA-Trfase_fam_III.
    IPR023606. CoA-Trfase_III_dom.
    IPR017659. Formyl_CoA_transfer.
    [Graphical view]
    PfamiPF02515. CoA_transf_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF89796. SSF89796. 1 hit.
    TIGRFAMsiTIGR03253. oxalate_frc. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiFCTA_ECOLI
    AccessioniPrimary (citable) accession number: P69902
    Secondary accession number(s): P77407
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 4, 2005
    Last sequence update: January 4, 2005
    Last modified: September 7, 2016
    This is version 102 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.