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Protein

Acetyl-CoA acetyltransferase

Gene

thlA

Organism
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

2 acetyl-CoA = CoA + acetoacetyl-CoA.PROSITE-ProRule annotation

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)DescriptionActionsGraphical viewLength
Active sitei88Acyl-thioester intermediateBy similarity1
Active sitei348Proton acceptorPROSITE-ProRule annotation1
Active sitei378Proton acceptorPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BioCyciMetaCyc:THLCLOS-MONOMER.
SABIO-RKP45359.
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
Synonyms:thl
Ordered Locus Names:CA_C2873
OrganismiClostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Taxonomic identifieri272562 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
Proteomesi
  • UP000000814 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002064031 – 392Acetyl-CoA acetyltransferaseAdd BLAST392

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi272562.CA_C2873.

Structurei

Secondary structure

1392
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 11Combined sources8
Turni20 – 23Combined sources4
Helixi26 – 41Combined sources16
Helixi45 – 47Combined sources3
Beta strandi50 – 54Combined sources5
Helixi65 – 72Combined sources8
Beta strandi81 – 85Combined sources5
Helixi87 – 89Combined sources3
Helixi90 – 103Combined sources14
Beta strandi108 – 118Combined sources11
Beta strandi123 – 125Combined sources3
Turni126 – 130Combined sources5
Helixi142 – 147Combined sources6
Turni151 – 154Combined sources4
Helixi157 – 168Combined sources12
Helixi172 – 191Combined sources20
Turni192 – 198Combined sources7
Beta strandi202 – 205Combined sources4
Beta strandi210 – 213Combined sources4
Helixi225 – 229Combined sources5
Beta strandi233 – 236Combined sources4
Beta strandi242 – 246Combined sources5
Beta strandi250 – 260Combined sources11
Helixi261 – 266Combined sources6
Beta strandi272 – 279Combined sources8
Helixi285 – 290Combined sources6
Helixi294 – 302Combined sources9
Helixi307 – 309Combined sources3
Beta strandi311 – 315Combined sources5
Helixi320 – 330Combined sources11
Helixi334 – 336Combined sources3
Helixi343 – 346Combined sources4
Helixi350 – 368Combined sources19
Beta strandi372 – 377Combined sources6
Turni381 – 383Combined sources3
Beta strandi385 – 391Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4WYRX-ray2.30A/B1-392[»]
4XL2X-ray1.77A/B1-392[»]
ProteinModelPortaliP45359.
SMRiP45359.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.Curated

Phylogenomic databases

eggNOGiENOG4105CHU. Bacteria.
COG0183. LUCA.
HOGENOMiHOG000012238.
KOiK00626.
OMAiESTEKHN.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020610. Thiolase_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.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P45359-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKEVVIASAV RTAIGSYGKS LKDVPAVDLG ATAIKEAVKK AGIKPEDVNE
60 70 80 90 100
VILGNVLQAG LGQNPARQAS FKAGLPVEIP AMTINKVCGS GLRTVSLAAQ
110 120 130 140 150
IIKAGDADVI IAGGMENMSR APYLANNARW GYRMGNAKFV DEMITDGLWD
160 170 180 190 200
AFNDYHMGIT AENIAERWNI SREEQDEFAL ASQKKAEEAI KSGQFKDEIV
210 220 230 240 250
PVVIKGRKGE TVVDTDEHPR FGSTIEGLAK LKPAFKKDGT VTAGNASGLN
260 270 280 290 300
DCAAVLVIMS AEKAKELGVK PLAKIVSYGS AGVDPAIMGY GPFYATKAAI
310 320 330 340 350
EKAGWTVDEL DLIESNEAFA AQSLAVAKDL KFDMNKVNVN GGAIALGHPI
360 370 380 390
GASGARILVT LVHAMQKRDA KKGLATLCIG GGQGTAILLE KC
Length:392
Mass (Da):41,241
Last modified:November 1, 1995 - v1
Checksum:i024D9B21D200856D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U08465 Genomic DNA. Translation: AAA82724.1.
AF072734 Genomic DNA. Translation: AAC26023.1.
AE001437 Genomic DNA. Translation: AAK80816.1.
PIRiE97253.
JC4032.
RefSeqiNP_349476.1. NC_003030.1.
WP_010966157.1. NC_003030.1.

Genome annotation databases

EnsemblBacteriaiAAK80816; AAK80816; CA_C2873.
GeneIDi1119056.
KEGGicac:CA_C2873.
PATRICi32040157. VBICloAce74127_3057.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U08465 Genomic DNA. Translation: AAA82724.1.
AF072734 Genomic DNA. Translation: AAC26023.1.
AE001437 Genomic DNA. Translation: AAK80816.1.
PIRiE97253.
JC4032.
RefSeqiNP_349476.1. NC_003030.1.
WP_010966157.1. NC_003030.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4WYRX-ray2.30A/B1-392[»]
4XL2X-ray1.77A/B1-392[»]
ProteinModelPortaliP45359.
SMRiP45359.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272562.CA_C2873.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK80816; AAK80816; CA_C2873.
GeneIDi1119056.
KEGGicac:CA_C2873.
PATRICi32040157. VBICloAce74127_3057.

Phylogenomic databases

eggNOGiENOG4105CHU. Bacteria.
COG0183. LUCA.
HOGENOMiHOG000012238.
KOiK00626.
OMAiESTEKHN.

Enzyme and pathway databases

UniPathwayiUPA00058; UER00101.
BioCyciMetaCyc:THLCLOS-MONOMER.
SABIO-RKP45359.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020610. Thiolase_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.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTHLA_CLOAB
AccessioniPrimary (citable) accession number: P45359
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 2, 2016
This is version 115 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, Direct protein sequencing, 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.