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Q8X5X6

- YDIF_ECO57

UniProt

Q8X5X6 - YDIF_ECO57

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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

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
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        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_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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 77 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