DB code: D00090

CATH domain 3.40.47.10 : Peroxisomal Thiolase; Chain A, domain 1 Catalytic domain
3.40.47.20 : Peroxisomal Thiolase; Chain A, domain 1 Catalytic domain
E.C. 2.3.1.16
CSA 1afw
M-CSA 1afw
MACiE M0077

CATH domain Related DB codes (homologues)
3.40.47.10 : Peroxisomal Thiolase; Chain A, domain 1 D00411 D00509 D00825 D00826 D00867 D00871

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P27796 3-ketoacyl-CoA thiolase, peroxisomal
EC 2.3.1.16
Beta-ketothiolase
Acetyl-CoA acyltransferase
Peroxisomal 3-oxoacyl-CoA thiolase
NP_012106.1 (Protein)
NM_001179508.1 (DNA/RNA sequence)
PF02803 (Thiolase_C)
PF00108 (Thiolase_N)
[Graphical View]

KEGG enzyme name
acetyl-CoA C-acyltransferase
beta-ketothiolase
3-ketoacyl-CoA thiolase
KAT
beta-ketoacyl coenzyme A thiolase
beta-ketoacyl-CoA thiolase
beta-ketoadipyl coenzyme A thiolase
beta-ketoadipyl-CoA thiolase
3-ketoacyl CoA thiolase
3-ketoacyl coenzyme A thiolase
3-ketoacyl thiolase
3-ketothiolase
3-oxoacyl-CoA thiolase
3-oxoacyl-coenzyme A thiolase
6-oxoacyl-CoA thiolase
acetoacetyl-CoA beta-ketothiolase
acetyl-CoA acyltransferase
ketoacyl-CoA acyltransferase
ketoacyl-coenzyme A thiolase
long-chain 3-oxoacyl-CoA thiolase
oxoacyl-coenzyme A thiolase
pro-3-ketoacyl-CoA thiolase
thiolase I
2-methylacetoacetyl-CoA thiolase [misleading]

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P27796 THIK_YEAST Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA. Homodimer. Peroxisome.

KEGG Pathways
Map code Pathways E.C.
MAP00062 Fatty acid elongation in mitochondria
MAP00071 Fatty acid metabolism
MAP00120 Bile acid biosynthesis
MAP00280 Valine, leucine and isoleucine degradation
MAP00281 Geraniol degradation
MAP00362 Benzoate degradation via hydroxylation
MAP00592 alpha-Linolenic acid metabolism
MAP00642 Ethylbenzene degradation
MAP01040 Biosynthesis of unsaturated fatty acids

Compound table
Substrates Products Intermediates
KEGG-id C00040 C00024 C00010 C00264
E.C.
Compound Acyl-CoA Acetyl-CoA CoA 3-Oxoacyl-CoA
Type amine group,carbohydrate,nucleotide ,peptide/protein,sulfide group amine group,carbohydrate,nucleotide ,peptide/protein,sulfide group amine group,carbohydrate,nucleotide ,peptide/protein,sulfhydryl group amine group,carbohydrate,nucleotide ,peptide/protein,phosphate group/phosphate ion,sulfide group
ChEBI 15351
15346
PubChem 444493
6302
6816
87642
1afwA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1afwB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1pxtA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1pxtB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1afwA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1afwB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1pxtA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1pxtB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
PDB;1Swiss-prot;P27796

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1afwA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 125
1afwB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 125
1pxtA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 125
1pxtB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 125
1afwA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 375;CYS 403
1afwB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 375;CYS 403
1pxtA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 375;CYS 403
1pxtB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 375;CYS 403

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[3]
p.800-801, p.804, Fig.13
[5]
p.723, Fig.9 4

References
[1]
Resource
Comments
Medline ID
PubMed ID 2859988
Journal Eur J Biochem
Year 1985
Volume 149
Pages 181-6
Authors Mori M, Matsue H, Miura S, Tatibana M, Hashimoto T
Title Transport of proteins into mitochondrial matrix. Evidence suggesting a common pathway for 3-ketoacyl-CoA thiolase and enzymes having presequences.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 2213879
Journal J Mol Biol
Year 1990
Volume 215
Pages 211-3
Authors Zeelen JP, Wierenga RK, Erdmann R, Kunau WH
Title Crystallographic studies of 3-ketoacylCoA thiolase from yeast Saccharomyces cerevisiae.
Related PDB
Related UniProtKB
[3]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS)
Medline ID 95111951
PubMed ID 7812714
Journal Structure
Year 1994
Volume 2
Pages 797-808
Authors Mathieu M, Zeelen JP, Pauptit RA, Erdmann R, Kunau WH, Wierenga RK
Title The 2.8 A crystal structure of peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: a five-layered alpha beta alpha beta alpha structure constructed from two core domains of identical topology.
Related PDB 1pxt
Related UniProtKB P27796
[4]
Resource
Comments
Medline ID
PubMed ID 7756275
Journal Biochemistry
Year 1995
Volume 34
Pages 6441-7
Authors Yang SY, He XY, Schulz H
Title Glutamate 139 of the large alpha-subunit is the catalytic base in the dehydration of both D- and L-3-hydroxyacyl-coenzyme A but not in the isomerization of delta 3, delta 2-enoyl-coenzyme A catalyzed by the multienzyme complex of fatty acid oxidation from Escherichia coli.
Related PDB
Related UniProtKB
[5]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS)
Medline ID 98022915
PubMed ID 9402066
Journal J Mol Biol
Year 1997
Volume 273
Pages 714-28
Authors Mathieu M, Modis Y, Zeelen JP, Engel CK, Abagyan RA, Ahlberg A, Rasmussen B, Lamzin VS, Kunau WH, Wierenga RK
Title The 1.8 A crystal structure of the dimeric peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: implications for substrate binding and reaction mechanism.
Related PDB 1afw 1afy
Related UniProtKB P27796
[6]
Resource
Comments
Medline ID
PubMed ID 9215574
Journal Protein Eng
Year 1997
Volume 10
Pages 561-6
Authors Rangan VS, Serre L, Witkowska HE, Bari A, Smith S
Title Characterization of the malonyl-/acetyltransacylase domain of the multifunctional animal fatty acid synthase by expression in Escherichia coli and refolding in vitro.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 9744475
Journal Hum Mutat
Year 1998
Volume 12
Pages 245-54
Authors Fukao T, Nakamura H, Song XQ, Nakamura K, Orii KE, Kohno Y, Kano M, Yamaguchi S, Hashimoto T, Orii T, Kondo N
Title Characterization of N93S, I312T, and A333P missense mutations in two Japanese families with mitochondrial acetoacetyl-CoA thiolase deficiency.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 10098837
Journal J Neurochem
Year 1999
Volume 72
Pages 1362-71
Authors Ballestero RP, Dybowski JA, Levy G, Agranoff BW, Uhler MD
Title Cloning and characterization of zRICH, a 2',3'-cyclic-nucleotide 3'-phosphodiesterase induced during zebrafish optic nerve regeneration.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 10727229
Journal Biochemistry
Year 2000
Volume 39
Pages 3360-8
Authors Vinarov DA, Miziorko HM
Title 3-hydroxy-3-methylglutaryl-coenzyme A synthase reaction intermediates: detection of a covalent tetrahedral adduct by differential isotope shift 13C nuclear magnetic resonance spectroscopy.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 11915938
Journal Cell Mol Life Sci
Year 2002
Volume 59
Pages 193-212
Authors Stolowich NJ, Petrescu AD, Huang H, Martin GG, Scott AI, Schroeder F
Title Sterol carrier protein-2: structure reveals function.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 11914035
Journal Mol Genet Metab
Year 2002
Volume 75
Pages 235-43
Authors Fukao T, Nakamura H, Nakamura K, Perez-Cerda C, Baldellou A, Barrionuevo CR, Castello FG, Kohno Y, Ugarte M, Kondo N
Title Characterization of six mutations in five Spanish patients with mitochondrial acetoacetyl-CoA thiolase deficiency: effects of amino acid substitutions on tertiary structure.
Related PDB
Related UniProtKB

Comments

Created Updated
2004-03-17 2009-02-26