Reviewed, UniProtKB/Swiss-Prot P45359 (THLA_CLOAB)

Names and origin

Protein names

Recommended name:
    Acetyl-CoA acetyltransferase
    EC=2.3.1.9
Alternative name(s):
    Acetoacetyl-CoA thiolase

Gene names

Name:	thlA
Synonyms:	thl
Ordered Locus Names:	CA_C2873

Organism

Clostridium acetobutylicum [Complete proteome] [HAMAP]

Taxonomic identifier

1488 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	392 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	2 acetyl-CoA = CoA + acetoacetyl-CoA.
Pathway	Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3.
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the thiolase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acetyl-CoA C-acetyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 392	392	Acetyl-CoA acetyltransferase		PRO_0000206403
Sites
	Active site	88	1	Acyl-thioester intermediate By similarity
	Active site	348	1	Proton acceptor By similarity
	Active site	378	1	Proton acceptor By similarity

Sequences

	Sequence		Length	Mass (Da)
	P45359-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 024D9B21D200856D	FASTA	392	41,241
	10 20 30 40 50 60 MKEVVIASAV RTAIGSYGKS LKDVPAVDLG ATAIKEAVKK AGIKPEDVNE VILGNVLQAG 70 80 90 100 110 120 LGQNPARQAS FKAGLPVEIP AMTINKVCGS GLRTVSLAAQ IIKAGDADVI IAGGMENMSR 130 140 150 160 170 180 APYLANNARW GYRMGNAKFV DEMITDGLWD AFNDYHMGIT AENIAERWNI SREEQDEFAL 190 200 210 220 230 240 ASQKKAEEAI KSGQFKDEIV PVVIKGRKGE TVVDTDEHPR FGSTIEGLAK LKPAFKKDGT 250 260 270 280 290 300 VTAGNASGLN DCAAVLVIMS AEKAKELGVK PLAKIVSYGS AGVDPAIMGY GPFYATKAAI 310 320 330 340 350 360 EKAGWTVDEL DLIESNEAFA AQSLAVAKDL KFDMNKVNVN GGAIALGHPI GASGARILVT 370 380 390 LVHAMQKRDA KKGLATLCIG GGQGTAILLE KC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 7867955] [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: 11075929] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.
[3]	"Genome sequence and comparative analysis of the solvent-producing bacterium Clostridium acetobutylicum." Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V., Smith D.R. J. Bacteriol. 183:4823-4838(2001) [PubMed: 11466286] [Abstract] 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: 1685080] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-30. Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U08465 Genomic DNA. Translation: AAA82724.1. AF072734 Genomic DNA. Translation: AAC26023.1. AE001437 Genomic DNA. Translation: AAK80816.1.
PIR	E97253. JC4032.
RefSeq	NP_349476.1.
3D structure databases
HSSP	HSSP built from PDB template 1M3K based on UniProtKB P07097.
ModBase	Search...
Genome annotation databases
GeneID	1119056.
GenomeReviews	Gene locus CA_C2873 in contig AE001437_GR.
KEGG	cac:CAC2873.
NMPDR	fig|272562.1.peg.3005.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P45359.
OMA	EIVPVMV.
Enzyme and pathway databases
BioCyc	CACE272562:CAC2873-MON. MetaCyc:THLCLOS-MON.
BRENDA	2.3.1.9. 2866.
Family and domain databases
InterPro	IPR002155. Thiolase. IPR016038. Thiolase-like_subgr. [Graphical view]
Gene3D	G3DSA:3.40.47.10. Thiolase-like_subgr. 1 hit.
PANTHER	PTHR18919. Thiolase. 1 hit.
Pfam	PF02803. Thiolase_C. 1 hit. PF00108. Thiolase_N. 1 hit. [Graphical view]
PIRSF	PIRSF000429. Ac-CoA_Ac_transf. 1 hit.
TIGRFAMs	TIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITE	PS00098. THIOLASE_1. 1 hit. PS00737. THIOLASE_2. 1 hit. PS00099. THIOLASE_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

THLA_CLOAB

Accession

Primary (citable) accession number: P45359

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	November 3, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)