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P37766

- YDIF_ECOLI

UniProt

P37766 - YDIF_ECOLI

Protein

Acetate CoA-transferase YdiF

Gene

ydiF

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 3 (01 Dec 2000)
      Previous versions | rss
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    Functioni

    CoA transferase having broad substrate specificity for short-chain acyl-CoA thioesters with the activity decreasing when the length of the carboxylic acid chain exceeds four carbons. May play a role in short-chain fatty acid metabolism in E.coli By similarity.By similarity

    Catalytic activityi

    Acyl-CoA + acetate = a fatty acid anion + acetyl-CoA.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei333 – 33315-glutamyl coenzyme A thioester intermediateBy similarity

    GO - Molecular functioni

    1. acetate CoA-transferase activity Source: UniProtKB

    GO - Biological processi

    1. ketone body catabolic process Source: InterPro
    2. protein homotetramerization Source: UniProtKB
    3. short-chain fatty acid metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    BioCyciEcoCyc:EG12432-MONOMER.
    ECOL316407:JW1684-MONOMER.
    RETL1328306-WGS:GSTH-1755-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetate CoA-transferase YdiF (EC:2.8.3.8)
    Alternative name(s):
    Short-chain acyl-CoA:acetate CoA-transferase
    Gene namesi
    Name:ydiF
    Ordered Locus Names:b1694, JW1684
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG12432. ydiF.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 531531Acetate CoA-transferase YdiFPRO_0000168990Add
    BLAST

    Proteomic databases

    PaxDbiP37766.
    PRIDEiP37766.

    Expressioni

    Gene expression databases

    GenevestigatoriP37766.

    Interactioni

    Subunit structurei

    Homotetramer; dimer of dimers.By similarity

    Protein-protein interaction databases

    IntActiP37766. 2 interactions.
    STRINGi511145.b1694.

    Structurei

    3D structure databases

    ProteinModelPortaliP37766.
    SMRiP37766. Positions 4-529.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the 3-oxoacid CoA-transferase family.Curated

    Phylogenomic databases

    eggNOGiCOG4670.
    HOGENOMiHOG000058376.
    OMAiASDLKVM.
    OrthoDBiEOG6Z3KMD.
    PhylomeDBiP37766.

    Family and domain databases

    InterProiIPR014388. 3-oxoacid_CoA-transferase.
    IPR004165. CoA_trans_fam_I.
    [Graphical view]
    PANTHERiPTHR13707. PTHR13707. 1 hit.
    PfamiPF01144. CoA_trans. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000858. SCOT-t. 1 hit.
    SMARTiSM00882. CoA_trans. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P37766-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKPVKPPRIN GRVPVLSAQE AVNYIPDEAT LCVLGAGGGI LEATTLITAL    50
    ADKYKQTQTP RNLSIISPTG LGDRADRGIS PLAQEGLVKW ALCGHWGQSP 100
    RISELAEQNK IIAYNYPQGV LTQTLRAAAA HQPGIISDIG IGTFVDPRQQ 150
    GGKLNEVTKE DLIKLVEFDN KEYLYYKAIA PDIAFIRATT CDSEGYATFE 200
    DEVMYLDALV IAQAVHNNGG IVMMQVQKMV KKATLHPKSV RIPGYLVDIV 250
    VVDPDQTQLY GGAPVNRFIS GDFTLDDSTK LSLPLNQRKL VARRALFEMR 300
    KGAVGNVGVG IADGIGLVAR EEGCADDFIL TVETGPIGGI TSQGIAFGAN 350
    VNTRAILDMT SQFDFYHGGG LDVCYLSFAE VDQHGNVGVH KFNGKIMGTG 400
    GFIDISATSK KIIFCGTLTA GSLKTEITDG KLNIVQEGRV KKFIRELPEI 450
    TFSGKIALER GLDVRYITER AVFTLKEDGL HLIEIAPGVD LQKDILDKMD 500
    FTPVISPELK LMDERLFIDA AMGFVLPEAA H 531
    Length:531
    Mass (Da):57,562
    Last modified:December 1, 2000 - v3
    Checksum:iE07A0D445015030D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00096 Genomic DNA. Translation: AAC74764.1.
    AP009048 Genomic DNA. Translation: BAA15447.2.
    X04306 Genomic DNA. No translation available.
    PIRiF64927.
    RefSeqiNP_416209.1. NC_000913.3.
    YP_489956.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74764; AAC74764; b1694.
    BAA15447; BAA15447; BAA15447.
    GeneIDi12931296.
    946211.
    KEGGiecj:Y75_p1669.
    eco:b1694.
    PATRICi32118694. VBIEscCol129921_1765.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00096 Genomic DNA. Translation: AAC74764.1 .
    AP009048 Genomic DNA. Translation: BAA15447.2 .
    X04306 Genomic DNA. No translation available.
    PIRi F64927.
    RefSeqi NP_416209.1. NC_000913.3.
    YP_489956.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P37766.
    SMRi P37766. Positions 4-529.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P37766. 2 interactions.
    STRINGi 511145.b1694.

    Proteomic databases

    PaxDbi P37766.
    PRIDEi P37766.

    Protocols and materials databases

    DNASUi 946211.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC74764 ; AAC74764 ; b1694 .
    BAA15447 ; BAA15447 ; BAA15447 .
    GeneIDi 12931296.
    946211.
    KEGGi ecj:Y75_p1669.
    eco:b1694.
    PATRICi 32118694. VBIEscCol129921_1765.

    Organism-specific databases

    EchoBASEi EB2328.
    EcoGenei EG12432. ydiF.

    Phylogenomic databases

    eggNOGi COG4670.
    HOGENOMi HOG000058376.
    OMAi ASDLKVM.
    OrthoDBi EOG6Z3KMD.
    PhylomeDBi P37766.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG12432-MONOMER.
    ECOL316407:JW1684-MONOMER.
    RETL1328306-WGS:GSTH-1755-MONOMER.

    Miscellaneous databases

    PROi P37766.

    Gene expression databases

    Genevestigatori P37766.

    Family and domain databases

    InterProi IPR014388. 3-oxoacid_CoA-transferase.
    IPR004165. CoA_trans_fam_I.
    [Graphical view ]
    PANTHERi PTHR13707. PTHR13707. 1 hit.
    Pfami PF01144. CoA_trans. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000858. SCOT-t. 1 hit.
    SMARTi SM00882. CoA_trans. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. "The overexpression and complete amino acid sequence of Escherichia coli 3-dehydroquinase."
      Duncan K., Chaudhuri S., Campbell M.S., Coggins J.R.
      Biochem. J. 238:475-483(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64.
    5. "Intrinsic and extrinsic approaches for detecting genes in a bacterial genome."
      Borodovsky M., Rudd K.E., Koonin E.V.
      Nucleic Acids Res. 22:4756-4767(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.

    Entry informationi

    Entry nameiYDIF_ECOLI
    AccessioniPrimary (citable) accession number: P37766
    Secondary accession number(s): P76199, P76898
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: December 1, 2000
    Last modified: October 1, 2014
    This is version 96 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Formation of the covalent enzyme-CoA thioester intermediate proceeds via an unstable anhydride species formed between the carboxylate group of the catalytic glutamate of the enzyme and the carbonyl carbon of the thioester linkage of the substrate.By similarity

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3