Q6L8K7 (THIL_YARLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetyl-CoA acetyltransferase
EC=2.3.1.9

Alternative name(s):
Peroxisomal acetoacetyl-CoA thiolase
Short name=Thiolase

Gene names

Name:	PAT1
Ordered Locus Names:	YALI0E11099g

Organism

Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)

Taxonomic identifier

284591 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Dipodascaceae › Yarrowia

Protein attributes

Sequence length	397 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Essential for n-decane utilization.
Catalytic activity	2 acetyl-CoA = CoA + acetoacetyl-CoA.
Subcellular location	Peroxisome.
Sequence similarities	Belongs to the thiolase family.

Ontologies

Keywords
Cellular component	Peroxisome
Ligand	Metal-binding Potassium
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acetyl-CoA C-acetyltransferase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 397	397	Acetyl-CoA acetyltransferase		PRO_0000206415
Sites
	Active site	95	1	Acyl-thioester intermediate By similarity
	Active site	351	1	Proton acceptor By similarity
	Active site	379	1	Proton acceptor By similarity
	Metal binding	187	1	Potassium By similarity
	Metal binding	246	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	247	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	249	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	347	1	Potassium; via carbonyl oxygen By similarity
	Binding site	187	1	Coenzyme A By similarity
	Binding site	230	1	Coenzyme A By similarity
	Binding site	250	1	Coenzyme A By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6L8K7 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 84CFBCE9D5A29EE0	FASTA	397	41,357
	10 20 30 40 50 60 MRLTLPRLNA AYIVGAARTP VGKFNGALKS VSAIDLGITA AKAAVQRSKV PADQIDEFLF 70 80 90 100 110 120 GQVLTANSGQ APARQVVIKG GFPESVEATT INKVCSSGLK TVALAAQAIK AGDRNVIVAG 130 140 150 160 170 180 GMESMSNTPY YSGRGLVFGN QKLEDSIVKD GLWDPYNNIH MGNCCENTNK RDGITREQQD 190 200 210 220 230 240 EYAIESYRRA NESIKNGAFK DEIVPVEIKT RKGTVTVSED EEPKGANAEK LKGLKPVFDK 250 260 270 280 290 300 QGSVTAGNAS PINDGASAVV VASGTKAKEL GTPVLAKIVS YADAATAPID FTIAPSLAIP 310 320 330 340 350 360 AALKKAGLTK DDIALWEINE AFSGVALANL MRLGIDKSKV NVKGGAVALG HPIGASGNRI 370 380 390 FVTLVNALKE GEYGVAAICN GGGASTAIVI KKVSSVE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of acetoacetyl-CoA thiolase gene essential for n-decane assimilation in yeast Yarrowia lipolytica." Yamagami S., Iida T., Nagata Y., Ohta A., Takagi M. Biochem. Biophys. Res. Commun. 282:832-838(2001) [PubMed: 11401539] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: CXAU1.
[2]	"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CLIB 122 / E 150.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB120846 Genomic DNA. Translation: BAD20191.1. CR382131 Genomic DNA. Translation: CAG79399.1.
PIR	JC7675.
RefSeq	XP_503808.1. XM_503808.1.
3D structure databases
ProteinModelPortal	Q6L8K7.
SMR	Q6L8K7. Positions 6-393.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6L8K7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2911520.
GenomeReviews	Gene locus YALI0E11099g in contig CR382131_GR.
KEGG	yli:YALI0E11099g.
Phylogenomic databases
eggNOG	fuNOG05493.
HOGENOM	HBG370930.
OMA	AYAVPKV.
OrthoDB	EOG4FXVH3.
Family and domain databases
InterPro	IPR002155. Thiolase. IPR016039. Thiolase-like. IPR016038. Thiolase-like_subgr. IPR020615. Thiolase_acyl_enz_int_AS. IPR020617. Thiolase_C. IPR020613. Thiolase_CS. IPR020616. Thiolase_N. [Graphical view]
Gene3D	G3DSA:3.40.47.10. Thiolase-like_subgr. 4 hits.
KO	K00626.
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.
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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

THIL_YARLI

Accession

Primary (citable) accession number: Q6L8K7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	July 5, 2004
Last modified:	December 14, 2011
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program