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Protein

Acetyl-CoA acetyltransferase

Gene

thlA

Organism
Peptoclostridium difficile (strain 630) (Clostridium difficile)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

2 acetyl-CoA = CoA + acetoacetyl-CoA.

Pathwayi: (R)-mevalonate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes (R)-mevalonate from acetyl-CoA.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Acetyl-CoA acetyltransferase (thlA)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
This subpathway is part of the pathway (R)-mevalonate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (R)-mevalonate from acetyl-CoA, the pathway (R)-mevalonate biosynthesis and in Metabolic intermediate biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei88 – 881Acyl-thioester intermediateBy similarity
Active sitei348 – 3481Proton acceptorBy similarity
Active sitei378 – 3781Proton acceptorBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BioCyciCDIF272563:GJFE-1210-MONOMER.
UniPathwayiUPA00058; UER00101.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-CoA acetyltransferase (EC:2.3.1.9)
Alternative name(s):
Acetoacetyl-CoA thiolase
Gene namesi
Name:thlA
Ordered Locus Names:CD630_10590
OrganismiPeptoclostridium difficile (strain 630) (Clostridium difficile)
Taxonomic identifieri272563 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesPeptostreptococcaceaePeptoclostridium
Proteomesi
  • UP000001978 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 391391Acetyl-CoA acetyltransferasePRO_5000077784Add
BLAST

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi272563.CD1059.

Structurei

Secondary structure

1
391
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 118Combined sources
Turni20 – 234Combined sources
Helixi26 – 4015Combined sources
Helixi45 – 473Combined sources
Beta strandi50 – 545Combined sources
Helixi65 – 728Combined sources
Beta strandi81 – 844Combined sources
Helixi87 – 893Combined sources
Helixi90 – 10314Combined sources
Beta strandi108 – 11811Combined sources
Turni126 – 1305Combined sources
Helixi142 – 1465Combined sources
Beta strandi148 – 1503Combined sources
Turni151 – 1544Combined sources
Helixi157 – 16812Combined sources
Helixi172 – 19120Combined sources
Turni192 – 1987Combined sources
Beta strandi202 – 2043Combined sources
Beta strandi211 – 2133Combined sources
Helixi225 – 2306Combined sources
Beta strandi234 – 2363Combined sources
Turni243 – 2453Combined sources
Beta strandi250 – 26011Combined sources
Helixi261 – 2677Combined sources
Beta strandi272 – 28211Combined sources
Helixi285 – 2906Combined sources
Helixi292 – 30312Combined sources
Helixi307 – 3093Combined sources
Beta strandi311 – 3155Combined sources
Helixi320 – 33011Combined sources
Beta strandi336 – 3383Combined sources
Helixi343 – 3464Combined sources
Turni350 – 3523Combined sources
Helixi353 – 36816Combined sources
Beta strandi371 – 3799Combined sources
Turni380 – 3823Combined sources
Beta strandi383 – 3908Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DD5X-ray1.25A1-391[»]
ProteinModelPortaliQ18AR0.
SMRiQ18AR0. Positions 4-390.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.Curated

Phylogenomic databases

eggNOGiENOG4105CHU. Bacteria.
COG0183. LUCA.
HOGENOMiHOG000012238.
KOiK00626.
OMAiMRMGARM.
OrthoDBiEOG68M4GV.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PfamiPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMiSSF53901. SSF53901. 2 hits.
TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEiPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q18AR0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREVVIASAA RTAVGSFGGA FKSVSAVELG VTAAKEAIKR ANITPDMIDE
60 70 80 90 100
SLLGGVLTAG LGQNIARQIA LGAGIPVEKP AMTINIVCGS GLRSVSMASQ
110 120 130 140 150
LIALGDADIM LVGGAENMSM SPYLVPSARY GARMGDAAFV DSMIKDGLSD
160 170 180 190 200
IFNNYHMGIT AENIAEQWNI TREEQDELAL ASQNKAEKAQ AEGKFDEEIV
210 220 230 240 250
PVVIKGRKGD TVVDKDEYIK PGTTMEKLAK LRPAFKKDGT VTAGNASGIN
260 270 280 290 300
DGAAMLVVMA KEKAEELGIE PLATIVSYGT AGVDPKIMGY GPVPATKKAL
310 320 330 340 350
EAANMTIEDI DLVEANEAFA AQSVAVIRDL NIDMNKVNVN GGAIAIGHPI
360 370 380 390
GCSGARILTT LLYEMKRRDA KTGLATLCIG GGMGTTLIVK R
Length:391
Mass (Da):40,860
Last modified:July 25, 2006 - v1
Checksum:i7B6713CCC8F70899
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM180355 Genomic DNA. Translation: CAJ67900.1.
RefSeqiWP_009888868.1. NZ_CP010905.1.
YP_001087540.1. NC_009089.1.

Genome annotation databases

EnsemblBacteriaiCAJ67900; CAJ67900; CD630_10590.
GeneIDi4915191.
KEGGicdf:CD630_10590.
pdc:CDIF630_01199.
PATRICi19440445. VBICloDif38397_1111.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM180355 Genomic DNA. Translation: CAJ67900.1.
RefSeqiWP_009888868.1. NZ_CP010905.1.
YP_001087540.1. NC_009089.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DD5X-ray1.25A1-391[»]
ProteinModelPortaliQ18AR0.
SMRiQ18AR0. Positions 4-390.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272563.CD1059.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAJ67900; CAJ67900; CD630_10590.
GeneIDi4915191.
KEGGicdf:CD630_10590.
pdc:CDIF630_01199.
PATRICi19440445. VBICloDif38397_1111.

Phylogenomic databases

eggNOGiENOG4105CHU. Bacteria.
COG0183. LUCA.
HOGENOMiHOG000012238.
KOiK00626.
OMAiMRMGARM.
OrthoDBiEOG68M4GV.

Enzyme and pathway databases

UniPathwayiUPA00058; UER00101.
BioCyciCDIF272563:GJFE-1210-MONOMER.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PfamiPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMiSSF53901. SSF53901. 2 hits.
TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEiPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 630.

Entry informationi

Entry nameiTHLA_PEPD6
AccessioniPrimary (citable) accession number: Q18AR0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: July 25, 2006
Last modified: July 6, 2016
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.