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InterPro: IPR016038 Thiolase-like, subgroup
Protein matches
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UniProtKB Matches: 22396 proteins |
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Accession
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IPR016038 Thiolase-like_subgr |
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Type
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Domain |
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Signatures
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InterPro Relationships
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Parent
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IPR016039 Thiolase-like
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Found in
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IPR000794 Beta-ketoacyl synthase
IPR002155 Thiolase
IPR004432 Polyketide-type polyunsaturated fatty acid synthase, PfaA
IPR004655 Beta-ketoacyl-acyl carrier protein synthase III (FabH)
IPR004656 Putative condensing enzyme FabH-related
IPR011141 Polyketide synthase, type III
IPR011554 Hydroxymethylglutaryl-CoA synthase, prokaryotic
IPR012392 Very-long-chain 3-ketoacyl-CoA synthase
IPR012793 Beta-ketoadipyl CoA thiolase
IPR012805 Acetyl-CoA C-acyltransferase FadA
IPR012806 Acetyl-CoA C-acyltransferase FadI
IPR013528 Hydroxymethylglutaryl-coenzyme A synthase, N-terminal
IPR017568 3-oxoacyl-[acyl-carrier-protein] synthase 2
IPR020841 Polyketide synthase, beta-ketoacyl synthase region
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Contains
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IPR001099 Chalcone/stilbene synthase, N-terminal
IPR012328 Chalcone/stilbene synthase, C-terminal
IPR013601 FAE1/Type III polyketide synthase-like protein
IPR013747 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C-terminal
IPR013751 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III
IPR014030 Beta-ketoacyl synthase, N-terminal
IPR014031 Beta-ketoacyl synthase, C-terminal
IPR018088 Chalcone/stilbene synthase, active site
IPR018201 Beta-ketoacyl synthase, active site
IPR020615 Thiolase, acyl-enzyme intermediate active site
IPR020616 Thiolase, N-terminal
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GO Term annotation
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Process
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GO:0008152 metabolic process
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Function
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GO:0003824 catalytic activity
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InterPro annotation
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 Entry Details in BioMart
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Abstract
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This entry represents a subgroup of thiolase-like domains (missing a few subfamilies). These domains have a 3-layer structure with an alpha/beta/alpha topology. This domain usually occurs in two similar copies that are related by a pseudo-dyad, and which arose through duplication. The proteins in this entry can be split into two groups: those related to thiolase, and those related to chalcone synthase. The thiolase-like enzymes include:
- Thiolase, where the topology of each domain is similar to the first domain of phosphoglucomutase [1]
- Beta-ketoacyl-ACP synthases types I (EC:2.3.1.41) and II (EC:2.3.1.179) [2, 3]
- Actinorhodin polyketide beta-ketoacyl synthases 1 and 2 [4]
The chalcone synthase-like enzymes include:
- Chalcone synthase (EC:2.3.1.74) [5]
- Polyketide synthases [6]
- Dihydropinosylvin synthase [7]
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Structural links
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Database links
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Example proteins
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P09110 3-ketoacyl-CoA thiolase, peroxisomal
P19096 Fatty acid synthase
P19097 Fatty acid synthase subunit alpha
P34255 Uncharacterized protein B0303.3
Q56WD9 3-ketoacyl-CoA thiolase 2, peroxisomal
More proteins
Example Proteins Key
| InterPro entry accession number/name and structure databases |
Colour code |
| IPR001227 |
Acyl transferase domain |
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| IPR013149 |
Alcohol dehydrogenase, zinc-binding |
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| IPR020843 |
Polyketide synthase, enoylreductase |
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| IPR016039 |
Thiolase-like |
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| IPR014030 |
Beta-ketoacyl synthase, N-terminal |
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| IPR016038 |
Thiolase-like, subgroup |
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| IPR018201 |
Beta-ketoacyl synthase, active site |
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| IPR020842 |
Polyketide synthase/Fatty acid synthase, KR |
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| IPR016036 |
Malonyl-CoA ACP transacylase, ACP-binding |
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| IPR002198 |
Short-chain dehydrogenase/reductase SDR |
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| IPR008278 |
4'-phosphopantetheinyl transferase |
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| IPR014031 |
Beta-ketoacyl synthase, C-terminal |
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| IPR016035 |
Acyl transferase/acyl hydrolase/lysophospholipase |
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| IPR020610 |
Thiolase, active site |
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| IPR011032 |
GroES-like |
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| IPR016040 |
NAD(P)-binding domain |
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| IPR020613 |
Thiolase, conserved site |
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| IPR002155 |
Thiolase |
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| IPR020615 |
Thiolase, acyl-enzyme intermediate active site |
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| IPR020616 |
Thiolase, N-terminal |
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| IPR020617 |
Thiolase, C-terminal |
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| IPR006162 |
Phosphopantetheine attachment site |
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| IPR009081 |
Acyl carrier protein-like |
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| IPR006163 |
Phosphopantetheine-binding |
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| IPR000794 |
Beta-ketoacyl synthase |
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| IPR014043 |
Acyl transferase |
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| IPR004568 |
Phosphopantethiene-protein transferase |
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| IPR001031 |
Thioesterase |
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| IPR013217 |
Methyltransferase type 12 |
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ModBase |
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SWISS-MODEL |
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PDB Chain |
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Publications
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1.
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Mathieu M, Modis Y, Zeelen JP, Engel CK, Abagyan RA, Ahlberg A, Rasmussen B, Lamzin VS, Kunau WH, Wierenga RK.
The 1.8 A crystal structure of the dimeric peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: implications for substrate binding and reaction mechanism.
J. Mol. Biol. 273 714-28 1997
[PubMed: 9402066]
http://dx.doi.org/10.1006/jmbi.1997.1331
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2.
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von Wettstein-Knowles P, Olsen JG, McGuire KA, Henriksen A.
Fatty acid synthesis. Role of active site histidines and lysine in Cys-His-His-type beta-ketoacyl-acyl carrier protein synthases.
FEBS J. 273 695-710 2006
[PubMed: 16441657]
http://dx.doi.org/10.1111/j.1742-4658.2005.05101.x
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3.
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Huang W, Jia J, Edwards P, Dehesh K, Schneider G, Lindqvist Y.
Crystal structure of beta-ketoacyl-acyl carrier protein synthase II from E.coli reveals the molecular architecture of condensing enzymes.
EMBO J. 17 1183-91 1998
[PubMed: 9482715]
http://dx.doi.org/10.1093/emboj/17.5.1183
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4.
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Keatinge-Clay AT, Maltby DA, Medzihradszky KF, Khosla C, Stroud RM.
An antibiotic factory caught in action.
Nat. Struct. Mol. Biol. 11 888-93 2004
[PubMed: 15286722]
http://dx.doi.org/10.1038/nsmb808
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5.
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Jez JM, Bowman ME, Noel JP.
Structure-guided programming of polyketide chain-length determination in chalcone synthase.
Biochemistry 40 14829-38 2001
[PubMed: 11732902]
http://dx.doi.org/10.1021/bi015621z
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6.
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Sankaranarayanan R, Saxena P, Marathe UB, Gokhale RS, Shanmugam VM, Rukmini R.
A novel tunnel in mycobacterial type III polyketide synthase reveals the structural basis for generating diverse metabolites.
Nat. Struct. Mol. Biol. 11 894-900 2004
[PubMed: 15286723]
http://dx.doi.org/10.1038/nsmb809
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7.
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Austin MB, Bowman ME, Ferrer JL, Schroder J, Noel JP.
An aldol switch discovered in stilbene synthases mediates cyclization specificity of type III polyketide synthases.
Chem. Biol. 11 1179-94 2004
[PubMed: 15380179]
http://dx.doi.org/10.1016/j.chembiol.2004.05.024
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Additional Reading
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Bagautdinov B, Ukita Y, Miyano M, Kunishima N.
Structure of 3-oxoacyl-(acyl-carrier protein) synthase II from Thermus thermophilus HB8.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64 2008 358-66
[PubMed: 18453702]
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Alhamadsheh MM, Musayev F, Komissarov AA, Sachdeva S, Wright HT, Scarsdale N, Florova G, Reynolds KA.
Alkyl-CoA disulfides as inhibitors and mechanistic probes for FabH enzymes.
Chem. Biol. 14 2007 513-24
[PubMed: 17524982]
http://dx.doi.org/10.1016/j.chembiol.2007.03.013
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Sachdeva S, Musayev F, Alhamadsheh MM, Neel Scarsdale J, Tonie Wright H, Reynolds KA.
Probing reactivity and substrate specificity of both subunits of the dimeric Mycobacterium tuberculosis FabH using alkyl-CoA disulfide inhibitors and acyl-CoA substrates.
Bioorg. Chem. 36 2008 85-90
[PubMed: 18096200]
http://dx.doi.org/10.1016/j.bioorg.2007.11.001
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Sachdeva S, Musayev FN, Alhamadsheh MM, Scarsdale JN, Wright HT, Reynolds KA.
Separate entrance and exit portals for ligand traffic in Mycobacterium tuberculosis FabH.
Chem. Biol. 15 2008 402-12
[PubMed: 18420147]
http://dx.doi.org/10.1016/j.chembiol.2008.03.007
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Pappenberger G, Schulz-Gasch T, Kusznir E, Muller F, Hennig M.
Structure-assisted discovery of an aminothiazole derivative as a lead molecule for inhibition of bacterial fatty-acid synthesis.
Acta Crystallogr. D Biol. Crystallogr. 63 2007 1208-16
[PubMed: 18084068]
http://dx.doi.org/10.1107/S0907444907049852
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