P45369 (THIL_ALLVD) Reviewed, UniProtKB/Swiss-Prot

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:	Alvin_0063

Organism

Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / D) (Chromatium vinosum) [Complete proteome] [HAMAP]

Taxonomic identifier

572477 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Chromatiales › Chromatiaceae › Allochromatium › Chromatium vinosum

Protein attributes

Sequence length	394 AA.
Sequence status	Complete.
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 – 394	394	Acetyl-CoA acetyltransferase		PRO_0000206419
Sites
	Active site	89	1	Acyl-thioester intermediate By similarity
	Active site	350	1	Proton acceptor By similarity
	Active site	380	1	Proton acceptor By similarity
Experimental info
	Sequence conflict	2	1	N → S in AAA23322. Ref.1
	Sequence conflict	19	1	S → G in AAA23322. Ref.1
	Sequence conflict	73	1	K → H in AAA23322. Ref.1
	Sequence conflict	239	1	R → K in AAA23322. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P45369 [UniParc]. Last modified June 15, 2010. Version 2. Checksum: 8AECC7EB26B29344	FASTA	394	41,129
	10 20 30 40 50 60 MNENIVIVDA GRSAIGTFSG SLSSLSATEI GTAVLKGLLA RTGLAPEQID EVILGQVLTA 70 80 90 100 110 120 GVGQNPARQT TLKAGLPHSV PAMTINKVCG SGLKAVHLAM QAIACGDADI VIAGGQESMS 130 140 150 160 170 180 QSSHVLPRSR DGQRMGDWSM KDTMIVDGLW DAFNNYHMGT TAENIAQKYG FTREQQDAFA 190 200 210 220 230 240 AASQQKTEAA QKAGRFQDEI IPIEIPQRKG DPKVFDADEF PRHGTTAESL GKLRPAFSRD 250 260 270 280 290 300 GSVTAGNASG INDGAAMVVV MKESKAKELG LKPMARLVAF ASAGVDPAIM GTGPIPASTK 310 320 330 340 350 360 CLEKAGWTPA DLDLIEANEA FAAQAMSVNQ DMGWDLSKVN VNGGAIAIGH PIGASGARVL 370 380 390 VTLLYEMQKR DAKKGLATLC IGGGQGVALA VERM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and nucleotide sequences of genes relevant for biosynthesis of poly(3-hydroxybutyric acid) in Chromatium vinosum strain D." Liebergesell M., Steinbuechel A. Eur. J. Biochem. 209:135-150(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete sequence of chromosome of Allochromatium vinosum DSM 180." US DOE Joint Genome Institute Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Zigann R., Dahl C., Woyke T. Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 17899 / DSM 180 / NBRC 103801 / D.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L01112 Genomic DNA. Translation: AAA23322.1. CP001896 Genomic DNA. Translation: ADC61035.1.
PIR	S29276.
RefSeq	YP_003442067.1. NC_013851.1.
3D structure databases
ProteinModelPortal	P45369.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ADC61035; ADC61035; Alvin_0063.
GeneID	8785390.
KEGG	alv:Alvin_0063.
PATRIC	31919867. VBIAllVin64954_0065.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HOG000012238.
KO	K00626.
ProtClustDB	CLSK2782295.
Enzyme and pathway databases
BioCyc	AVIN572477:GCJK-63-MONOMER.
UniPathway	UPA00058; UER00101.
Family and domain databases
Gene3D	3.40.47.10. 4 hits.
InterPro	IPR002155. Thiolase. IPR016039. Thiolase-like. IPR016038. Thiolase-like_subgr. IPR020615. Thiolase_acyl_enz_int_AS. IPR020610. Thiolase_AS. IPR020617. Thiolase_C. IPR020613. Thiolase_CS. IPR020616. Thiolase_N. [Graphical view]
PANTHER	PTHR18919. PTHR18919. 1 hit.
Pfam	PF02803. Thiolase_C. 1 hit. PF00108. Thiolase_N. 1 hit. [Graphical view]
PIRSF	PIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAM	SSF53901. Thiolase-like. 2 hits.
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_ALLVD

Accession

Primary (citable) accession number: P45369
Secondary accession number(s): D3RUY6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	June 15, 2010
Last modified:	May 29, 2013
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program