Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q8X5X6 (YDIF_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetate CoA-transferase YdiF
EC=2.8.3.8
Alternative name(s):
Short-chain acyl-CoA:acetate CoA-transferase
Gene names
Name:ydiF
Ordered Locus Names:Z2722, ECs2401
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length531 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3

Catalytic activity

Acyl-CoA + acetate = a fatty acid anion + acetyl-CoA. Ref.3

Subunit structure

Homotetramer; dimer of dimers. Ref.3

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.

Sequence similarities

Belongs to the 3-oxoacid CoA-transferase family.

Mass spectrometry

Molecular mass is 59628 Da from positions 1 - 531. Determined by ESI. Ref.3

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 531531Acetate CoA-transferase YdiF
PRO_0000418373

Sites

Active site3331Acyl-thioester intermediate

Secondary structure

1 .......................................................................................................... 531
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8X5X6 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: FC70D164D28A4E3E

FASTA53157,504
        10         20         30         40         50         60 
MKPVKPPRIN GRVPVLSAQE AVNYIPDEAT LCVLGAGGGI LEATTLITAL ADKYKQTQTP 

        70         80         90        100        110        120 
RNLSIISPTG LGDRADRGIS PLAQEGLVKW ALCGHWGQSP RISDLAEQNK IIAYNYPQGV 

       130        140        150        160        170        180 
LTQTLRAAAA HQPGIISDIG IGTFVDPRQQ GGKLNEVTKE DLIKLVEFDN KEYLYYKAIA 

       190        200        210        220        230        240 
PDIAFIRATT CDSEGYATFE DEVMYLDALV IAQAVHNNGG IVMMQVQKMV KKATLHPKSV 

       250        260        270        280        290        300 
RIPGYLVDIV VVDPDQSQLY GGAPVNRFIS GDFTLDDSTK LSLPLNQRKL VARRALFEMR 

       310        320        330        340        350        360 
KGAVGNVGVG IADGIGLVAR EEGCADDFIL TVETGPIGGI TSQGIAFGAN VNTRAILDMT 

       370        380        390        400        410        420 
SQFDFYHGGG LDVCYLSFAE VDQHGNVGVH KFNGKIMGTG GFIDISATSK KIIFCGTLTA 

       430        440        450        460        470        480 
GSLKTEIADG KLNIVQEGRV KKFIRELPEI TFSGKIALER GLDVRYITER AVFTLKEDGL 

       490        500        510        520        530 
HLIEIAPGVD LQKDILDKMD FTPVISPELK LMDERLFIDA AMGFVLPEAA H

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE005174 Genomic DNA. Translation: AAG56681.1.
BA000007 Genomic DNA. Translation: BAB35824.1.
PIRA90929.
E85777.
RefSeqNP_288128.1. NC_002655.2.
NP_310428.1. NC_002695.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2AHUX-ray1.90A/B/C/D1-531[»]
2AHVX-ray2.00A/B/C/D1-531[»]
2AHWX-ray2.15A/B/C/D1-531[»]
ProteinModelPortalQ8X5X6.
SMRQ8X5X6. Positions 4-529.
ModBaseSearch...

Protein-protein interaction databases

STRING155864.Z2722.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG56681; AAG56681; Z2722.
BAB35824; BAB35824; BAB35824.
GeneID912561.
961665.
KEGGece:Z2722.
ecs:ECs2401.
PATRIC18354144. VBIEscCol44059_2283.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000058376.
OMAASDLKVM.
ProtClustDBCLSK880166.

Enzyme and pathway databases

BioCycECOL386585:GJFA-2374-MONOMER.

Family and domain databases

InterProIPR014388. 3-oxoacid_CoA-transferase.
IPR004165. CoA_trans_fam_I.
[Graphical view]
PANTHERPTHR13707. PTHR13707. 1 hit.
PfamPF01144. CoA_trans. 1 hit.
[Graphical view]
PIRSFPIRSF000858. SCOT-t. 1 hit.
SMARTSM00882. CoA_trans. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8X5X6.

Entry information

Entry nameYDIF_ECO57
AccessionPrimary (citable) accession number: Q8X5X6
Secondary accession number(s): Q7ADH3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2012
Last sequence update: March 1, 2002
Last modified: May 1, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents