Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei88 – 881Acyl-thioester intermediateBy similarity
Active sitei348 – 3481Proton acceptorPROSITE-ProRule annotation
Active sitei378 – 3781Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BioCyciCACE272562:GJIH-2956-MONOMER.
MetaCyc:THLCLOS-MONOMER.
RETL1328306-WGS:GSTH-5125-MONOMER.
RETL1328306-WGS:GSTH-6664-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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 392392Acetyl-CoA acetyltransferasePRO_0000206403Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi272562.CA_C2873.

Structurei

Secondary structure

1
392
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 118Combined sources
Turni20 – 234Combined sources
Helixi26 – 4116Combined sources
Helixi45 – 473Combined sources
Beta strandi50 – 545Combined sources
Helixi65 – 728Combined sources
Beta strandi81 – 855Combined sources
Helixi87 – 893Combined sources
Helixi90 – 10314Combined sources
Beta strandi108 – 11811Combined sources
Beta strandi123 – 1253Combined sources
Turni126 – 1305Combined sources
Helixi142 – 1476Combined sources
Turni151 – 1544Combined sources
Helixi157 – 16812Combined sources
Helixi172 – 19120Combined sources
Turni192 – 1987Combined sources
Beta strandi202 – 2054Combined sources
Beta strandi210 – 2134Combined sources
Helixi225 – 2295Combined sources
Beta strandi233 – 2364Combined sources
Beta strandi242 – 2465Combined sources
Beta strandi250 – 26011Combined sources
Helixi261 – 2666Combined sources
Beta strandi272 – 2798Combined sources
Helixi285 – 2906Combined sources
Helixi294 – 3029Combined sources
Helixi307 – 3093Combined sources
Beta strandi311 – 3155Combined sources
Helixi320 – 33011Combined sources
Helixi334 – 3363Combined sources
Helixi343 – 3464Combined sources
Helixi350 – 36819Combined sources
Beta strandi372 – 3776Combined sources
Turni381 – 3833Combined sources
Beta strandi385 – 3917Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4WYRX-ray2.30A/B1-392[»]
4XL2X-ray1.77A/B1-392[»]
ProteinModelPortaliP45359.
SMRiP45359. Positions 3-391.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.Curated

Phylogenomic databases

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

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
EntryMethodResolution (Å)ChainPositionsPDBsum
4WYRX-ray2.30A/B1-392[»]
4XL2X-ray1.77A/B1-392[»]
ProteinModelPortaliP45359.
SMRiP45359. Positions 3-391.
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.
OrthoDBiEOG68M4GV.

Enzyme and pathway databases

UniPathwayiUPA00058; UER00101.
BioCyciCACE272562:GJIH-2956-MONOMER.
MetaCyc:THLCLOS-MONOMER.
RETL1328306-WGS:GSTH-5125-MONOMER.
RETL1328306-WGS:GSTH-6664-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...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of an acetyl-CoA C-acetyltransferase (thiolase) gene from Clostridium acetobutylicum ATCC 824."
    Stim-Herndon K.P., Petersen D.J., Bennett G.N.
    Gene 154:81-85(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.
  2. "Differential regulation of two thiolase genes from Clostridium acetobutylicum DSM 792."
    Winzer K., Lorenz K., Zickner B., Duerre P.
    J. Mol. Microbiol. Biotechnol. 2:531-541(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.
  4. "Cloning of the Clostridium acetobutylicum ATCC 824 acetyl coenzyme A acetyltransferase (thiolase; EC 2.3.1.9) gene."
    Petersen D.J., Bennett G.N.
    Appl. Environ. Microbiol. 57:2735-2741(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-30.
    Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.

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: January 20, 2016
This is version 111 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.