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P37766

- YDIF_ECOLI

UniProt

P37766 - YDIF_ECOLI

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Protein

Acetate CoA-transferase YdiF

Gene

ydiF

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

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
Complete GO annotation...

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.
InParanoidiP37766.
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

        10         20         30         40         50
MKPVKPPRIN GRVPVLSAQE AVNYIPDEAT LCVLGAGGGI LEATTLITAL
60 70 80 90 100
ADKYKQTQTP RNLSIISPTG LGDRADRGIS PLAQEGLVKW ALCGHWGQSP
110 120 130 140 150
RISELAEQNK IIAYNYPQGV LTQTLRAAAA HQPGIISDIG IGTFVDPRQQ
160 170 180 190 200
GGKLNEVTKE DLIKLVEFDN KEYLYYKAIA PDIAFIRATT CDSEGYATFE
210 220 230 240 250
DEVMYLDALV IAQAVHNNGG IVMMQVQKMV KKATLHPKSV RIPGYLVDIV
260 270 280 290 300
VVDPDQTQLY GGAPVNRFIS GDFTLDDSTK LSLPLNQRKL VARRALFEMR
310 320 330 340 350
KGAVGNVGVG IADGIGLVAR EEGCADDFIL TVETGPIGGI TSQGIAFGAN
360 370 380 390 400
VNTRAILDMT SQFDFYHGGG LDVCYLSFAE VDQHGNVGVH KFNGKIMGTG
410 420 430 440 450
GFIDISATSK KIIFCGTLTA GSLKTEITDG KLNIVQEGRV KKFIRELPEI
460 470 480 490 500
TFSGKIALER GLDVRYITER AVFTLKEDGL HLIEIAPGVD LQKDILDKMD
510 520 530
FTPVISPELK LMDERLFIDA AMGFVLPEAA H
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.
InParanoidi P37766.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 97 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