Summary: Serine acetyltransferase, N-terminal
This is the Wikipedia entry entitled "Serine O-acetyltransferase". More...
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Serine O-acetyltransferase Edit Wikipedia article
|PDB structures||RCSB PDB PDBe PDBsum|
|Gene Ontology||AmiGO / EGO|
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:L-serine O-acetyltransferase. Other names in common use include SATase, L-serine acetyltransferase, serine acetyltransferase, and serine transacetylase. This enzyme participates in cysteine metabolism and sulfur metabolism.
N terminal protein domain
|SATase N terminal domain|
The structure of the enzyme serine acetyltransferase- apoenzyme (truncated)
In molecular biology, the protein domain SATase is short for Serine acetyltransferase and refers to an enzyme that catalyses the conversion of L-serine to L-cysteine in E. coli. More specifically, its role is to catalyse the activation of L-serine by acetyl-CoA.This entry refers to the N-terminus of the protein which has a sequence that is conserved in plants and bacteria.
Importance of function
The N-terminal domain of the protein Serine acetyltransferase helps catalyse acetyl transfer. This particular enzyme catalyses serine into cysteine which is eventually converted to the essential amino acid methionine. Of particular interest to scientists, is the ability to harness the natural ability of the enzyme, Serine acetyltransferase, to create nutritionally essential amino acids and to exploit this ability through transgenic plants. These transgenic plants would contain more essential sulphur amino acids meaning a healthier diet for humans and animals.
The amino-terminal alpha-helical domain particularly the amino acid residues His158 (histidine in position 158) and Asp143 (aspartic acid in position 143) form a catalytic triad with the substrate for acetyl transfer. There are eight alpha helices that form the N-terminal domain.
- Denk D, Böck A (March 1987). "L-cysteine biosynthesis in Escherichia coli: nucleotide sequence and expression of the serine acetyltransferase (cysE) gene from the wild-type and a cysteine-excreting mutant". J. Gen. Microbiol. 133 (3): 515–25. PMID 3309158.
- Saito K, Yokoyama H, Noji M, Murakoshi I (July 1995). "Molecular cloning and characterization of a plant serine acetyltransferase playing a regulatory role in cysteine biosynthesis from watermelon". J. Biol. Chem. 270 (27): 16321–6. PMID 7608200.
- Tabe L, Wirtz M, Molvig L, Droux M, Hell R (March 2010). "Overexpression of serine acetlytransferase produced large increases in O-acetylserine and free cysteine in developing seeds of a grain legume". J. Exp. Bot. 61 (3): 721–33. doi:10.1093/jxb/erp338. PMC 2814105. PMID 19939888.
- Pye VE, Tingey AP, Robson RL, Moody PC (September 2004). "The structure and mechanism of serine acetyltransferase from Escherichia coli". J. Biol. Chem. 279 (39): 40729–36. doi:10.1074/jbc.M403751200. PMID 15231846.
- Kredich NM, Tomkins GM (1966). "The enzymic synthesis of L-cysteine in Escherichia coli and Salmonella typhimurium". J. Biol. Chem. 241 (21): 4955–65. PMID 5332668.
- Smith IK, Thompson JF (1971). "Purification and characterization of L-serine transacetylase and O-acetyl-L-serine sulfhydrylase from kidney bean seedlings (Phaseolus vulgaris)". Biochim. Biophys. Acta. 227 (2): 288–95. PMID 5550822.
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Serine acetyltransferase, N-terminal Provide feedback
Denk D, Bock A; , J Gen Microbiol 1987;133:515-525.: L-cysteine biosynthesis in Escherichia coli: nucleotide sequence and expression of the serine acetyltransferase (cysE) gene from the wild-type and a cysteine-excreting mutant. PUBMED:3309158 EPMC:3309158
Saito K, Yokoyama H, Noji M, Murakoshi I; , J Biol Chem 1995;270:16321-16326.: Molecular cloning and characterization of a plant serine acetyltransferase playing a regulatory role in cysteine biosynthesis from watermelon. PUBMED:7608200 EPMC:7608200
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR010493
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||cytoplasm (GO:0005737)|
|Molecular function||serine O-acetyltransferase activity (GO:0009001)|
|Biological process||cysteine biosynthetic process from serine (GO:0006535)|
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Curation and family details
|Seed source:||Pfam-B_1192 (release 8.0)|
|Author:||Wilbrey A, Studholme DJ|
|Number in seed:||111|
|Number in full:||1759|
|Average length of the domain:||92.10 aa|
|Average identity of full alignment:||42 %|
|Average coverage of the sequence by the domain:||34.01 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||9|
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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 SATase_N domain has been found. There are 37 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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