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190  structures 5851  species 2  interactions 23531  sequences 1627  architectures

Family: Ketoacyl-synt_C (PF02801)

Summary: Beta-ketoacyl synthase, C-terminal domain

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This is the Wikipedia entry entitled "Beta-ketoacyl-ACP synthase". More...

Beta-ketoacyl-ACP synthase Edit Wikipedia article

3-oxoacyl-ACP synthase, mitochondrial
Identifiers
Symbol OXSM
Entrez 54995
HUGO 26063
OMIM 610324
RefSeq NM_017897
UniProt Q9NWU1
Other data
Locus Chr. 3 p24.2
Beta-ketoacyl synthase, N-terminal domain
PDB 1oxh EBI.jpg
the crystal structure of beta-ketoacyl-[acyl carrier protein] synthase ii from streptococcus pneumoniae, triclinic form
Identifiers
Symbol ketoacyl-synt
Pfam PF00109
Pfam clan CL0046
InterPro IPR014030
PROSITE PDOC00529
SCOP 1kas
SUPERFAMILY 1kas
Beta-ketoacyl synthase, C-terminal domain
PDB 2ix4 EBI.jpg
arabidopsis thaliana mitochondrial beta-ketoacyl acp synthase hexanoic acid complex
Identifiers
Symbol Ketoacyl-synt_C
Pfam PF02801
Pfam clan CL0046
InterPro IPR014031
PROSITE PDOC00529
SCOP 1kas
SUPERFAMILY 1kas

In molecular biology, Beta-ketoacyl-ACP synthase EC 2.3.1.41, is an enzyme involved in fatty acid synthesis. It results in the formation of acetoacetyl ACP. FattyAcid-MB-Condensation.png

It is the enzyme that catalyses the condensation of malonyl-ACP with the growing fatty acid chain.[1] It is found as a component of a number of enzymatic systems, including fatty acid synthetase (FAS), which catalyses the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH; the multi-functional 6-methysalicylic acid synthase (MSAS) from Penicillium patulum,[2] which is involved in the biosynthesis of a polyketide antibiotic; polyketide antibiotic synthase enzyme systems; Emericella nidulans multifunctional protein Wa, which is involved in the biosynthesis of conidial green pigment; Rhizobium nodulation protein nodE, which probably acts as a beta-ketoacyl synthase in the synthesis of the nodulation Nod factor fatty acyl chain; and yeast mitochondrial protein CEM1. The condensation reaction is a two step process, first the acyl component of an activated acyl primer is transferred to a cysteine residue of the enzyme and is then condensed with an activated malonyl donor with the concomitant release of carbon dioxide.

Beta-ketoacyl synthase contains two protein domains. The active site is located between the N- and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine. Residues from both domains contribute to substrate binding and catalysis[3]

See also[edit]

External links[edit]

References[edit]

  1. ^ Kauppinen S, Siggaard-Andersen M, von Wettstein-Knowles P (1988). "beta-Ketoacyl-ACP synthase I of Escherichia coli: nucleotide sequence of the fabB gene and identification of the cerulenin binding residue". Carlsberg Res. Commun. 53 (6): 357–70. PMID 3076376. 
  2. ^ Beck J, Ripka S, Siegner A, Schiltz E, Schweizer E (September 1990). "The multifunctional 6-methylsalicylic acid synthase gene of Penicillium patulum. Its gene structure relative to that of other polyketide synthases". Eur. J. Biochem. 192 (2): 487–98. doi:10.1111/j.1432-1033.1990.tb19252.x. PMID 2209605. 
  3. ^ Huang W, Jia J, Edwards P, Dehesh K, Schneider G, Lindqvist Y (1998). "Crystal structure of beta-ketoacyl-acyl carrier protein synthase II from E.coli reveals the molecular architecture of condensing enzymes.". EMBO J 17 (5): 1183–91. doi:10.1093/emboj/17.5.1183. PMC 1170466. PMID 9482715. 

This article incorporates text from the public domain Pfam and InterPro IPR014030

This article incorporates text from the public domain Pfam and InterPro IPR014031

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Beta-ketoacyl synthase, C-terminal domain Provide feedback

The structure of beta-ketoacyl synthase is similar to that of the thiolase family (PF00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.

Literature references

  1. Huang W, Jia J, Edwards P, Dehesh K, Schneider G, Lindqvist Y; , EMBO J 1998;17:1183-1191.: Crystal structure of beta-ketoacyl-acyl carrier protein synthase II from E.coli reveals the molecular architecture of condensing enzymes. PUBMED:9482715 EPMC:9482715


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR014031

Beta-ketoacyl-ACP synthase EC (KAS) [PUBMED:3076376] is the enzyme that catalyzes the condensation of malonyl-ACP with the growing fatty acid chain. It is found as a component of a number of enzymatic systems, including fatty acid synthetase (FAS), which catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH; the multi-functional 6-methysalicylic acid synthase (MSAS) from Penicillium patulum [PUBMED:2209605], which is involved in the biosynthesis of a polyketide antibiotic; polyketide antibiotic synthase enzyme systems; Emericella nidulans multifunctional protein Wa, which is involved in the biosynthesis of conidial green pigment; Rhizobium nodulation protein nodE, which probably acts as a beta-ketoacyl synthase in the synthesis of the nodulation Nod factor fatty acyl chain; and yeast mitochondrial protein CEM1. The condensation reaction is a two step process, first the acyl component of an activated acyl primer is transferred to a cysteine residue of the enzyme and is then condensed with an activated malonyl donor with the concomitant release of carbon dioxide.

This entry represents the C-terminal domain of beta-ketoacyl-ACP synthases. The active site is contained in a cleft betweeen N- and C-terminal domains, with residues from both domains contributing to substrate binding and catalysis [PUBMED:11152607].

Domain organisation

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Alignments

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(165)
Full
(23531)
Representative proteomes NCBI
(21515)
Meta
(3921)
RP15
(1709)
RP35
(3766)
RP55
(5251)
RP75
(6174)
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  Seed
(165)
Full
(23531)
Representative proteomes NCBI
(21515)
Meta
(3921)
RP15
(1709)
RP35
(3766)
RP55
(5251)
RP75
(6174)
Alignment:
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  Seed
(165)
Full
(23531)
Representative proteomes NCBI
(21515)
Meta
(3921)
RP15
(1709)
RP35
(3766)
RP55
(5251)
RP75
(6174)
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Pfam alignments:

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Curation and family details

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Seed source: Dotter
Previous IDs: ketoacyl-synt_C;
Type: Domain
Author: Sonnhammer ELL, Griffiths-Jones SR
Number in seed: 165
Number in full: 23531
Average length of the domain: 108.60 aa
Average identity of full alignment: 35 %
Average coverage of the sequence by the domain: 10.85 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.7 20.7
Trusted cut-off 20.7 20.7
Noise cut-off 20.6 20.6
Model length: 119
Family (HMM) version: 17
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Interactions

There are 2 interactions for this family. More...

Ketoacyl-synt_C ketoacyl-synt

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Ketoacyl-synt_C domain has been found. There are 190 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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