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Protein

Acetyl-CoA:oxalate CoA-transferase

Gene

yfdE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the catabolism of oxalate and in the adapatation to low pH. ACOCT serves to prime the oxalate-induced acid tolerance response (ATR) cycle by producing substrate for oxalyl-CoA decarboxylase (OXC) and formyl-coenzyme A transferase (FCOCT). Catalyzes the reversible conversion of acetyl-CoA and oxalate to oxalyl-CoA and acetate. It can also use formyl-CoA and oxalate to produce oxalyl-CoA and formate with significantly reduced specific activity.1 Publication

Catalytic activityi

Acetyl-CoA + oxalate = acetate + oxalyl-CoA.1 Publication

Kineticsi

Kcat is 11 sec(-1) for the CoA-transferase activity with acetyl-CoA as substrate (at pH 6.7 and 25 degrees Celsius). Kcat is 15 sec(-1) for the CoA-transferase activity with oxalate as substrate (at pH 6.7 and 25 degrees Celsius).

  1. KM=17 µM for acetyl-CoA (at pH 6.7 and 25 degrees Celsius)1 Publication
  2. KM=22 mM for oxalate (at pH 6.7 and 25 degrees Celsius)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei233 – 2331By similarity

    GO - Molecular functioni

    • acetyl-CoA:oxalate CoA-transferase Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    BioCyciEcoCyc:G7234-MONOMER.
    ECOL316407:JW2368-MONOMER.
    MetaCyc:G7234-MONOMER.
    BRENDAi2.8.3.19. 2026.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetyl-CoA:oxalate CoA-transferase (EC:2.8.3.19)
    Short name:
    ACOCT
    Alternative name(s):
    Acetyl-coenzyme A transferase
    CoA:oxalate CoA-transferase
    Gene namesi
    Name:yfdE
    Ordered Locus Names:b2371, JW2368
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG13284. yfdE.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 381381Acetyl-CoA:oxalate CoA-transferasePRO_0000194725Add
    BLAST

    Proteomic databases

    PaxDbiP76518.

    Expressioni

    Inductioni

    By the acid response regulator EvgA.2 Publications

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi4259190. 3 interactions.
    DIPiDIP-11994N.
    IntActiP76518. 7 interactions.
    MINTiMINT-1289026.
    STRINGi511145.b2371.

    Structurei

    Secondary structure

    1
    381
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni9 – 124Combined sources
    Beta strandi14 – 174Combined sources
    Helixi23 – 3311Combined sources
    Beta strandi37 – 426Combined sources
    Turni44 – 463Combined sources
    Helixi49 – 524Combined sources
    Helixi62 – 687Combined sources
    Beta strandi72 – 754Combined sources
    Helixi81 – 9313Combined sources
    Beta strandi95 – 995Combined sources
    Helixi105 – 1084Combined sources
    Helixi113 – 1197Combined sources
    Beta strandi124 – 1318Combined sources
    Beta strandi133 – 1353Combined sources
    Turni136 – 1394Combined sources
    Helixi144 – 1518Combined sources
    Helixi153 – 1564Combined sources
    Helixi171 – 19424Combined sources
    Beta strandi199 – 2035Combined sources
    Helixi204 – 2096Combined sources
    Helixi214 – 2229Combined sources
    Beta strandi239 – 2424Combined sources
    Beta strandi245 – 2473Combined sources
    Beta strandi249 – 2524Combined sources
    Helixi256 – 26611Combined sources
    Helixi269 – 2713Combined sources
    Turni275 – 2773Combined sources
    Helixi280 – 2856Combined sources
    Helixi287 – 29812Combined sources
    Helixi303 – 31210Combined sources
    Beta strandi317 – 3193Combined sources
    Helixi323 – 3264Combined sources
    Helixi330 – 3345Combined sources
    Beta strandi338 – 3414Combined sources
    Beta strandi344 – 3474Combined sources
    Beta strandi350 – 3534Combined sources
    Beta strandi360 – 3623Combined sources
    Turni368 – 3714Combined sources
    Helixi372 – 3798Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4HL6X-ray2.12A/B/C/D/E/F1-381[»]
    ProteinModelPortaliP76518.
    SMRiP76518. Positions 6-381.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the CaiB/BaiF CoA-transferase family.Curated

    Phylogenomic databases

    eggNOGiENOG4105C04. Bacteria.
    COG1804. LUCA.
    HOGENOMiHOG000219745.
    InParanoidiP76518.
    KOiK18702.
    OMAiHCAVSGF.
    PhylomeDBiP76518.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

    P76518-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTNNESKGPF EGLLVIDMTH VLNGPFGTQL LCNMGARVIK VEPPGHGDDT
    60 70 80 90 100
    RTFGPYVDGQ SLYYSFINHG KESVVLDLKN DHDKSIFINM LKQADVLAEN
    110 120 130 140 150
    FRPGTMEKLG FSWETLQEIN PRLIYASSSG FGHTGPLKDA PAYDTIIQAM
    160 170 180 190 200
    SGIMMETGYP DAPPVRVGTS LADLCGGVYL FSGIVSALYG REKSQRGAHV
    210 220 230 240 250
    DIAMFDATLS FLEHGLMAYI ATGKSPQRLG NRHPYMAPFD VFNTQDKPIT
    260 270 280 290 300
    ICCGNDKLFS ALCQALELTE LVNDPRFSSN ILRVQNQAIL KQYIERTLKT
    310 320 330 340 350
    QAAEVWLARI HEVGVPVAPL LSVAEAIKLP QTQARNMLIE AGGIMMPGNP
    360 370 380
    IKISGCADPH VMPGAATLDQ HGEQIRQEFS S
    Length:381
    Mass (Da):41,671
    Last modified:August 29, 2001 - v2
    Checksum:i9C6801BCACFA5AE8
    GO

    Sequence cautioni

    The sequence D14008 differs from that shown. Reason: Frameshift at positions 360 and 366. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti294 – 2941I → T in D14008 (PubMed:8125343).Curated
    Sequence conflicti333 – 3331Q → E in D14008 (PubMed:8125343).Curated
    Sequence conflicti357 – 3571A → T in D14008 (PubMed:8125343).Curated
    Sequence conflicti368 – 3681L → S in D14008 (PubMed:8125343).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAC75430.2.
    AP009048 Genomic DNA. Translation: BAA16242.1.
    D14008 Genomic DNA. No translation available.
    PIRiH65010.
    RefSeqiNP_416872.4. NC_000913.3.
    WP_001296867.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75430; AAC75430; b2371.
    BAA16242; BAA16242; BAA16242.
    GeneIDi946432.
    KEGGiecj:JW2368.
    eco:b2371.
    PATRICi32120121. VBIEscCol129921_2469.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAC75430.2.
    AP009048 Genomic DNA. Translation: BAA16242.1.
    D14008 Genomic DNA. No translation available.
    PIRiH65010.
    RefSeqiNP_416872.4. NC_000913.3.
    WP_001296867.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4HL6X-ray2.12A/B/C/D/E/F1-381[»]
    ProteinModelPortaliP76518.
    SMRiP76518. Positions 6-381.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4259190. 3 interactions.
    DIPiDIP-11994N.
    IntActiP76518. 7 interactions.
    MINTiMINT-1289026.
    STRINGi511145.b2371.

    Proteomic databases

    PaxDbiP76518.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75430; AAC75430; b2371.
    BAA16242; BAA16242; BAA16242.
    GeneIDi946432.
    KEGGiecj:JW2368.
    eco:b2371.
    PATRICi32120121. VBIEscCol129921_2469.

    Organism-specific databases

    EchoBASEiEB3069.
    EcoGeneiEG13284. yfdE.

    Phylogenomic databases

    eggNOGiENOG4105C04. Bacteria.
    COG1804. LUCA.
    HOGENOMiHOG000219745.
    InParanoidiP76518.
    KOiK18702.
    OMAiHCAVSGF.
    PhylomeDBiP76518.

    Enzyme and pathway databases

    BioCyciEcoCyc:G7234-MONOMER.
    ECOL316407:JW2368-MONOMER.
    MetaCyc:G7234-MONOMER.
    BRENDAi2.8.3.19. 2026.

    Miscellaneous databases

    PROiP76518.

    Family and domain databases

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

    Entry informationi

    Entry nameiACOCT_ECOLI
    AccessioniPrimary (citable) accession number: P76518
    Secondary accession number(s): P76946
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: August 29, 2001
    Last modified: September 7, 2016
    This is version 123 of the entry and version 2 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. 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.