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61  structures 6534  species 2  interactions 7534  sequences 15  architectures

Family: SATase_N (PF06426)

Summary: Serine acetyltransferase, N-terminal

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This is the Wikipedia entry entitled "Serine O-acetyltransferase". More...

Serine O-acetyltransferase Edit Wikipedia article

serine O-acetyltransferase
EC number
CAS number 9023-16-9
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO

In enzymology, a serine O-acetyltransferase (EC is an enzyme that catalyzes the chemical reaction

acetyl-CoA + L-serine \rightleftharpoons CoA + O-acetyl-L-serine

Thus, the two substrates of this enzyme are acetyl-CoA and L-serine, whereas its two products are CoA and O-acetyl-L-serine.

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.

Structural studies

As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1S80, 1SSM, 1SSQ, 1SST, 1T3D, 1Y7L, and 2ISQ.

N terminal protein domain

SATase N terminal domain
PDB 1ssm EBI.jpg
The structure of the enzyme serine acetyltransferase- apoenzyme (truncated)
Symbol SATase_N
Pfam PF06426
InterPro IPR010493

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.[1] 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.[2]

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.[3]


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.[4] There are eight alpha helices that form the N-terminal domain.[4]


  1. ^ 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. doi:10.1099/00221287-133-3-515. PMID 3309158. 
  2. ^ 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. doi:10.1074/jbc.270.27.16321. PMID 7608200. 
  3. ^ 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. 
  4. ^ a b 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. doi:10.1016/0005-2744(71)90061-1. PMID 5550822. 

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.

Serine acetyltransferase, N-terminal Provide feedback

The N-terminal domain of serine acetyltransferase has a sequence that is conserved in plants [2] and bacteria [1].

Literature references

  1. 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

  2. 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 N-terminal domain of serine acetyltransferase has a sequence that is conserved in plants [PUBMED:7608200] and bacteria [PUBMED:7608200].

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

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Curation View help on the curation process

Seed source: Pfam-B_1192 (release 8.0)
Previous IDs: none
Type: Domain
Author: Wilbrey A, Studholme DJ
Number in seed: 165
Number in full: 7534
Average length of the domain: 88.80 aa
Average identity of full alignment: 46 %
Average coverage of the sequence by the domain: 32.61 %

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HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.9 20.9
Trusted cut-off 20.9 20.9
Noise cut-off 20.8 20.8
Model length: 105
Family (HMM) version: 10
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Species distribution

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

SATase_N Hexapep


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 61 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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