Reviewed, UniProtKB/Swiss-Prot P50174 (THIL_RHIME)

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:	R03262
ORF Names:	SMc03879

Organism

Rhizobium meliloti (Sinorhizobium meliloti) [Complete proteome] [HAMAP]

Taxonomic identifier

382 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium

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 By similarity.
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_0000206461
Sites
	Active site	90	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)
	P50174-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: B3162E72A9DB2A0D	FASTA	393	40,851
	10 20 30 40 50 60 MSNPSIVIAS AARTAVGSFN GAFGNTLAHE LGAAAIKAVL ERAGVEAGEV DEVILGQVLP 70 80 90 100 110 120 AGEGQNPARQ AAMKAGLPQE KTAWGMNQLC GSGLRAVALG MQQIATGDAK VIVAGGMESM 130 140 150 160 170 180 SMAPHCAHLR GGVKMGDYKM IDTMIKDGLT DAFYGYHMGI TAENVARKWQ LTREEQDEFA 190 200 210 220 230 240 LASQNKAEAA QKAGRFADEI VPFVVKTRKG DVNVDQDEYI RHGATLDSIA KLRPAFDKEG 250 260 270 280 290 300 TVTAGNASGL NDGAAAALLM TEAEAARRGI QPLARIVSWA TAGVDPQIMG TGPIPASRKA 310 320 330 340 350 360 LEKAGWSVAD IELVEANEAF AAQACAVNKD LGWDPSIVNV NGGAIAIGHP IGASGARVLN 370 380 390 TLLFEMKRRG VSKGLATLCI GGGMGVAMCV ERL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Poly-beta-hydroxybutyrate (PHB) biosynthetic genes in Rhizobium meliloti 41." Tombolini R., Povolo S., Buson A., Squartini A., Nuti M.P. Microbiology 141:2553-2559(1995) [PubMed: 7582015] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 41.
[2]	"Analysis of the chromosome sequence of the legume symbiont Sinorhizobium meliloti strain 1021." Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D. , Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F. Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001) [PubMed: 11481430] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U17226 Genomic DNA. Translation: AAA90982.1. AL591688 Genomic DNA. Translation: CAC47841.1.
RefSeq	NP_387368.1.
3D structure databases
HSSP	HSSP built from PDB template 1DLU based on UniProtKB P07097.
SMR	P50174. Positions 2-393.
ModBase	Search...
Genome annotation databases
GeneID	1234956.
GenomeReviews	Gene locus R03262 in contig AL591688_GR.
KEGG	sme:SMc03879.
NMPDR	fig|266834.1.peg.4556.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P50174.
OMA	GMESMSM.
Enzyme and pathway databases
BioCyc	SMEL266834:SMC03879-MON.
BRENDA	2.3.1.9. 142.
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_RHIME

Accession

Primary (citable) accession number: P50174

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	November 3, 2009
This is version 62 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)