Reviewed, UniProtKB/Swiss-Prot P14611 (THIL_RALEH)

Names and origin

Protein names

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

Gene names

Name:	phbA
Ordered Locus Names:	H16_A1438

Organism

Ralstonia eutropha (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)) [Complete proteome] [HAMAP]

Taxonomic identifier

381666 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

Protein attributes

Sequence length	393 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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
Biological process	PHB biosynthesis
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	poly-hydroxybutyrate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
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 – 393	393	Acetyl-CoA acetyltransferase		PRO_0000206418
Sites
	Active site	88	1	Acyl-thioester intermediate By similarity
	Active site	349	1	Proton acceptor By similarity
	Active site	379	1	Proton acceptor By similarity

Sequences

	Sequence		Length	Mass (Da)
	P14611-1 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 232C1127E20B3961	FASTA	393	40,549
	10 20 30 40 50 60 MTDVVIVSAA RTAVGKFGGS LAKIPAPELG AVVIKAALER AGVKPEQVSE VIMGQVLTAG 70 80 90 100 110 120 SGQNPARQAA IKAGLPAMVP AMTINKVCGS GLKAVMLAAN AIMAGDAEIV VAGGQENMSA 130 140 150 160 170 180 APHVLPGSRD GFRMGDAKLV DTMIVDGLWD VYNQYHMGIT AENVAKEYGI TREAQDEFAV 190 200 210 220 230 240 GSQNKAEAAQ KAGKFDEEIV PVLIPQRKGD PVAFKTDEFV RQGATLDSMS GLKPAFDKAG 250 260 270 280 290 300 TVTAANASGL NDGAAAVVVM SAAKAKELGL TPLATIKSYA NAGVDPKVMG MGPVPASKRA 310 320 330 340 350 360 LSRAEWTPQD LDLMEINEAF AAQALAVHQQ MGWDTSKVNV NGGAIAIGHP IGASGCRILV 370 380 390 TLLHEMKRRD AKKGLASLCI GGGMGVALAV ERK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Poly-beta-hydroxybutyrate biosynthesis in Alcaligenes eutrophus H16. Characterization of the genes encoding beta-ketothiolase and acetoacetyl-CoA reductase." Peoples O.P., Sinskey A.J. J. Biol. Chem. 264:15293-15297(1989) [PubMed: 2670935] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia eutropha H16." Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I., Gottschalk G., Steinbuechel A., Friedrich B., Bowien B. Nat. Biotechnol. 24:1257-1262(2006) [PubMed: 16964242] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Poly-beta-hydroxybutyrate (PHB) biosynthesis in Alcaligenes eutrophus H16. Identification and characterization of the PHB polymerase gene (phbC)." Peoples O.P., Sinskey A.J. J. Biol. Chem. 264:15298-15303(1989) [PubMed: 2670936] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.

Cross-references

Sequence databases
EMBLGenBankDDBJ	J04987 Genomic DNA. Translation: AAA21972.1. AM260479 Genomic DNA. Translation: CAJ92573.1. J05003 Genomic DNA. Translation: AAA21976.1.
PIR	XXALAE. A34340.
RefSeq	YP_725941.1.
3D structure databases
HSSP	HSSP built from PDB template 1M3K based on UniProtKB P07097.
ModBase	Search...
Protein-protein interaction databases
STRING	P14611.
Genome annotation databases
GeneID	4249783.
GenomeReviews	Gene locus H16_A1438 in contig AM260479_GR.
KEGG	reh:H16_A1438.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P14611.
OMA	DANTHDG.
Enzyme and pathway databases
BioCyc	MetaCyc:MON-13086.
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

THIL_RALEH

Accession

Primary (citable) accession number: P14611
Secondary accession number(s): Q0KBP8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	November 3, 2009
This is version 75 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)