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Protein

Acetate CoA-transferase YdiF

Gene

ydiF

Organism
Escherichia coli O157:H7
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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)DescriptionActionsGraphical viewLength
Active sitei3335-glutamyl coenzyme A thioester intermediate1

GO - Molecular functioni

  • acetate CoA-transferase activity Source: UniProtKB

GO - Biological processi

  • ketone body catabolic process Source: InterPro
  • protein homotetramerization Source: UniProtKB
  • short-chain fatty acid metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciECOO157: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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000558 Componenti: Chromosome
  • UP000002519 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004183731 – 531Acetate CoA-transferase YdiFAdd BLAST531

Interactioni

Subunit structurei

Homotetramer; dimer of dimers.1 Publication

Protein-protein interaction databases

STRINGi155864.Z2722.

Structurei

Secondary structure

1531
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi18 – 22Combined sources5
Beta strandi30 – 33Combined sources4
Turni38 – 41Combined sources4
Helixi44 – 57Combined sources14
Beta strandi62 – 69Combined sources8
Beta strandi72 – 77Combined sources6
Helixi80 – 82Combined sources3
Turni85 – 87Combined sources3
Beta strandi88 – 95Combined sources8
Helixi100 – 107Combined sources8
Beta strandi110 – 114Combined sources5
Helixi118 – 129Combined sources12
Beta strandi134 – 137Combined sources4
Turni139 – 142Combined sources4
Turni147 – 152Combined sources6
Beta strandi155 – 157Combined sources3
Beta strandi163 – 168Combined sources6
Beta strandi171 – 177Combined sources7
Beta strandi182 – 187Combined sources6
Beta strandi189 – 192Combined sources4
Helixi208 – 216Combined sources9
Turni217 – 219Combined sources3
Beta strandi221 – 230Combined sources10
Helixi237 – 239Combined sources3
Beta strandi240 – 242Combined sources3
Helixi244 – 246Combined sources3
Beta strandi248 – 252Combined sources5
Turni267 – 271Combined sources5
Helixi287 – 296Combined sources10
Beta strandi304 – 307Combined sources4
Turni311 – 314Combined sources4
Helixi315 – 321Combined sources7
Helixi325 – 327Combined sources3
Beta strandi328 – 331Combined sources4
Beta strandi335 – 338Combined sources4
Beta strandi354 – 356Combined sources3
Helixi359 – 367Combined sources9
Beta strandi372 – 377Combined sources6
Beta strandi379 – 382Combined sources4
Beta strandi390 – 392Combined sources3
Helixi402 – 406Combined sources5
Beta strandi410 – 415Combined sources6
Beta strandi418 – 422Combined sources5
Beta strandi424 – 427Combined sources4
Beta strandi432 – 436Combined sources5
Beta strandi439 – 445Combined sources7
Helixi454 – 459Combined sources6
Beta strandi463 – 467Combined sources5
Beta strandi469 – 476Combined sources8
Beta strandi479 – 485Combined sources7
Helixi491 – 494Combined sources4
Helixi496 – 498Combined sources3
Beta strandi499 – 501Combined sources3
Beta strandi504 – 511Combined sources8
Helixi514 – 517Combined sources4
Beta strandi518 – 520Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8X5X6.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4108IIG. Bacteria.
COG4670. LUCA.
HOGENOMiHOG000058376.
KOiK19709.
OMAiASDLKVM.

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

        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
RISDLAEQNK 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
VVDPDQSQLY 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 GSLKTEIADG KLNIVQEGRV KKFIRELPEI
460 470 480 490 500
TFSGKIALER GLDVRYITER AVFTLKEDGL HLIEIAPGVD LQKDILDKMD
510 520 530
FTPVISPELK LMDERLFIDA AMGFVLPEAA H
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:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG56681.1.
BA000007 Genomic DNA. Translation: BAB35824.1.
PIRiA90929.
E85777.
RefSeqiNP_310428.1. NC_002695.1.
WP_000805650.1. NZ_LPWC02000002.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG56681.1.
BA000007 Genomic DNA. Translation: BAB35824.1.
PIRiA90929.
E85777.
RefSeqiNP_310428.1. NC_002695.1.
WP_000805650.1. NZ_LPWC02000002.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi155864.Z2722.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiENOG4108IIG. Bacteria.
COG4670. LUCA.
HOGENOMiHOG000058376.
KOiK19709.
OMAiASDLKVM.

Enzyme and pathway databases

BioCyciECOO157:YDIF-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ8X5X6.

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]
ProtoNetiSearch...

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: November 2, 2016
This is version 90 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

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.