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Q8X5X6

- YDIF_ECO57

UniProt

Q8X5X6 - YDIF_ECO57

Protein

Acetate CoA-transferase YdiF

Gene

ydiF

Organism
Escherichia coli O157:H7
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      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. Exhibits high activity with acetoacetyl-CoA, propionyl-CoA, crotonoyl-CoA or butyryl-CoA as donors, with acetate as an acceptor. When acetyl-CoA is used as the donor, propionate, acetoacetate, butyrate, isobutyrate, and 4-hydroxybutyrate can be utilized as acceptors but not isovalerate. May play a role in short-chain fatty acid metabolism in E.coli.1 Publication

    Catalytic activityi

    Acyl-CoA + acetate = a fatty acid anion + acetyl-CoA.1 Publication

    Sites

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

    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

    BioCyciECOL386585:GJFA-2374-MONOMER.
    ECOO157:YDIF-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:ydiFImported
    Ordered Locus Names:Z2722, ECs2401
    OrganismiEscherichia coli O157:H7
    Taxonomic identifieri83334 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000558: Chromosome, UP000002519: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 531531Acetate CoA-transferase YdiFPRO_0000418373Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer; dimer of dimers.1 Publication

    Protein-protein interaction databases

    STRINGi155864.Z2722.

    Structurei

    Secondary structure

    1
    531
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi18 – 225
    Beta strandi30 – 334
    Turni38 – 414
    Helixi44 – 5714
    Beta strandi62 – 698
    Beta strandi72 – 776
    Helixi80 – 823
    Turni85 – 873
    Beta strandi88 – 958
    Helixi100 – 1078
    Beta strandi110 – 1145
    Helixi118 – 12912
    Beta strandi134 – 1374
    Turni139 – 1424
    Turni147 – 1526
    Beta strandi155 – 1573
    Beta strandi163 – 1686
    Beta strandi171 – 1777
    Beta strandi182 – 1876
    Beta strandi189 – 1924
    Helixi208 – 2169
    Turni217 – 2193
    Beta strandi221 – 23010
    Helixi237 – 2393
    Beta strandi240 – 2423
    Helixi244 – 2463
    Beta strandi248 – 2525
    Turni267 – 2715
    Helixi287 – 29610
    Beta strandi304 – 3074
    Turni311 – 3144
    Helixi315 – 3217
    Helixi325 – 3273
    Beta strandi328 – 3314
    Beta strandi335 – 3384
    Beta strandi354 – 3563
    Helixi359 – 3679
    Beta strandi372 – 3776
    Beta strandi379 – 3824
    Beta strandi390 – 3923
    Helixi402 – 4065
    Beta strandi410 – 4156
    Beta strandi418 – 4225
    Beta strandi424 – 4274
    Beta strandi432 – 4365
    Beta strandi439 – 4457
    Helixi454 – 4596
    Beta strandi463 – 4675
    Beta strandi469 – 4768
    Beta strandi479 – 4857
    Helixi491 – 4944
    Helixi496 – 4983
    Beta strandi499 – 5013
    Beta strandi504 – 5118
    Helixi514 – 5174
    Beta strandi518 – 5203

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2AHUX-ray1.90A/B/C/D1-531[»]
    2AHVX-ray2.00A/B/C/D1-531[»]
    2AHWX-ray2.15A/B/C/D1-531[»]
    ProteinModelPortaliQ8X5X6.
    SMRiQ8X5X6. Positions 4-529.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8X5X6.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the 3-oxoacid CoA-transferase family.Sequence Analysis

    Phylogenomic databases

    HOGENOMiHOG000058376.
    OMAiASDLKVM.
    OrthoDBiEOG6Z3KMD.

    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.

    Q8X5X6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKPVKPPRIN GRVPVLSAQE AVNYIPDEAT LCVLGAGGGI LEATTLITAL    50
    ADKYKQTQTP RNLSIISPTG LGDRADRGIS PLAQEGLVKW ALCGHWGQSP 100
    RISDLAEQNK IIAYNYPQGV LTQTLRAAAA HQPGIISDIG IGTFVDPRQQ 150
    GGKLNEVTKE DLIKLVEFDN KEYLYYKAIA PDIAFIRATT CDSEGYATFE 200
    DEVMYLDALV IAQAVHNNGG IVMMQVQKMV KKATLHPKSV RIPGYLVDIV 250
    VVDPDQSQLY GGAPVNRFIS GDFTLDDSTK LSLPLNQRKL VARRALFEMR 300
    KGAVGNVGVG IADGIGLVAR EEGCADDFIL TVETGPIGGI TSQGIAFGAN 350
    VNTRAILDMT SQFDFYHGGG LDVCYLSFAE VDQHGNVGVH KFNGKIMGTG 400
    GFIDISATSK KIIFCGTLTA GSLKTEIADG KLNIVQEGRV KKFIRELPEI 450
    TFSGKIALER GLDVRYITER AVFTLKEDGL HLIEIAPGVD LQKDILDKMD 500
    FTPVISPELK LMDERLFIDA AMGFVLPEAA H 531
    Length:531
    Mass (Da):57,504
    Last modified:March 1, 2002 - v1
    Checksum:iFC70D164D28A4E3E
    GO

    Mass spectrometryi

    Molecular mass is 59628 Da from positions 1 - 531. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005174 Genomic DNA. Translation: AAG56681.1.
    BA000007 Genomic DNA. Translation: BAB35824.1.
    PIRiA90929.
    E85777.
    RefSeqiNP_288128.1. NC_002655.2.
    NP_310428.1. NC_002695.1.

    Genome annotation databases

    EnsemblBacteriaiAAG56681; AAG56681; Z2722.
    BAB35824; BAB35824; BAB35824.
    GeneIDi912561.
    961665.
    KEGGiece:Z2722.
    ecs:ECs2401.
    PATRICi18354144. VBIEscCol44059_2283.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005174 Genomic DNA. Translation: AAG56681.1 .
    BA000007 Genomic DNA. Translation: BAB35824.1 .
    PIRi A90929.
    E85777.
    RefSeqi NP_288128.1. NC_002655.2.
    NP_310428.1. NC_002695.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2AHU X-ray 1.90 A/B/C/D 1-531 [» ]
    2AHV X-ray 2.00 A/B/C/D 1-531 [» ]
    2AHW X-ray 2.15 A/B/C/D 1-531 [» ]
    ProteinModelPortali Q8X5X6.
    SMRi Q8X5X6. Positions 4-529.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 155864.Z2722.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAG56681 ; AAG56681 ; Z2722 .
    BAB35824 ; BAB35824 ; BAB35824 .
    GeneIDi 912561.
    961665.
    KEGGi ece:Z2722.
    ecs:ECs2401.
    PATRICi 18354144. VBIEscCol44059_2283.

    Phylogenomic databases

    HOGENOMi HOG000058376.
    OMAi ASDLKVM.
    OrthoDBi EOG6Z3KMD.

    Enzyme and pathway databases

    BioCyci ECOL386585:GJFA-2374-MONOMER.
    ECOO157:YDIF-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q8X5X6.

    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: O157:H7 / EDL933 / ATCC 700927 / EHEC.
    2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
      Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
      , Kuhara S., Shiba T., Hattori M., Shinagawa H.
      DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.
    3. "Crystallographic trapping of the glutamyl-CoA thioester intermediate of family I CoA transferases."
      Rangarajan E.S., Li Y., Ajamian E., Iannuzzi P., Kernaghan S.D., Fraser M.E., Cygler M., Matte A.
      J. Biol. Chem. 280:42919-42928(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH COENZYME A VIA A GAMMA-GLUTAMYL-THIOESTER COVALENT LINKAGE, FUNCTION, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBUNIT, MASS SPECTROMETRY, REACTION MECHANISM.
      Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

    Entry informationi

    Entry nameiYDIF_ECO57
    AccessioniPrimary (citable) accession number: Q8X5X6
    Secondary accession number(s): Q7ADH3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2012
    Last sequence update: March 1, 2002
    Last modified: October 1, 2014
    This is version 76 of the entry and version 1 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.

    Keywords - Technical termi

    3D-structure, Complete proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3