Reviewed, UniProtKB/Swiss-Prot Q04677 (THIB_CANTR)

Names and origin

Protein names

Recommended name:
    Acetyl-CoA acetyltransferase IB
    EC=2.3.1.9
Alternative name(s):
    Peroxisomal acetoacetyl-CoA thiolase
    Thiolase IB

Gene names

Name:

PACTB

Organism

Candida tropicalis (Yeast)

Taxonomic identifier

5482 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	403 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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	Multimeric By similarity.
Subcellular location	Peroxisome.
Sequence similarities	Belongs to the thiolase family.

Ontologies

Keywords
Cellular component	Peroxisome
Molecular function	Acyltransferase Transferase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	peroxisome 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
	Initiator methionine	1	1	Removed Ref.1
	Chain	2 – 403	402	Acetyl-CoA acetyltransferase IB		PRO_0000206414
Regions
	Motif	401 – 403	3	Microbody targeting signal Potential
Sites
	Active site	91	1	Acyl-thioester intermediate By similarity
	Active site	353	1	Proton acceptor By similarity
	Active site	383	1	Proton acceptor By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q04677-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 42647747B663D47F	FASTA	403	41,930
	10 20 30 40 50 60 MTLPPVYIVS TARTPIGSFQ GSLSSLTYSD LGAHAVKAAL AKVPQIKPQD VDEIVFGGVL 70 80 90 100 110 120 QANVGQAPAR QVALKAGLPD SIIASTINKV CASGMKAVII GAQNIICGTS DIVVVGGAES 130 140 150 160 170 180 MSNTPYYLPS ARSGARYGDA VMVDGVQKDG LLDVYEEKLM GVAAEKCAKD HGFSREDQDN 190 200 210 220 230 240 FAINSYKKAG KALSEGKFKS EIAPVTIKGF RGKPDTVIEN DEEIGKFNED RLKSARTVFQ 250 260 270 280 290 300 KENGTVTAPN ASKLNDGGAA LVLVSEAKLK QLGLKPLAKI SGWGEAARTP FDFTIAPALA 310 320 330 340 350 360 VPKAVKHAGL TVDRVDFFEL NEAFSVVGLA NAELVKIPLE KLNVYGGAVA MGHPLGCSGA 370 380 390 400 RIIVTLLSVL TQEGGRFGAA GVCNGGGGAS AIVIEKIDSD AKL

References

[1]

"Peroxisomal acetoacetyl-CoA thiolase of an n-alkane-utilizing yeast, Candida tropicalis." Kurihara T., Ueda M., Kanayama N., Kondo J., Teranishi Y., Tanaka A. Eur. J. Biochem. 210:999-1005(1992) [PubMed: 1362382] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-17; 209-233 AND 280-290. Strain: ATCC 20336 / pK233 / NCYC 997.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D13471 Genomic DNA. Translation: BAA02716.1.
3D structure databases
SMR	Q04677. Positions 5-397.
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.3.1.9. 1242.
Family and domain databases
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]
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

THIB_CANTR

Accession

Primary (citable) accession number: Q04677

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 63 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)