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 | |||||||||
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Serine acetyltransferase hexamer, Haemophilus influenzae
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| Identifiers | |||||||||
| EC number | 2.3.1.30 | ||||||||
| CAS number | 9023-16-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a serine O-acetyltransferase (EC 2.3.1.30) is an enzyme that catalyzes the chemical reaction
- acetyl-CoA + L-serine 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.
Contents
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 | |||||||||
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The structure of the enzyme serine acetyltransferase- apoenzyme (truncated)
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| Identifiers | |||||||||
| Symbol | SATase_N | ||||||||
| Pfam | PF06426 | ||||||||
| InterPro | IPR010493 | ||||||||
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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]
Structure
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]
References
- ^ 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.
- ^ 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.
- ^ 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. - ^ 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.
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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
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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
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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
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.
| Cellular component | cytoplasm (GO:0005737) |
| Molecular function | serine O-acetyltransferase activity (GO:0009001) |
| Biological process | cysteine biosynthetic process from serine (GO:0006535) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...
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| Seed (157) |
Full (2991) |
Representative proteomes | UniProt (8294) |
NCBI (9090) |
Meta (492) |
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| RP15 (659) |
RP35 (1879) |
RP55 (2899) |
RP75 (4239) |
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| Jalview | |||||||||
| HTML | |||||||||
| PP/heatmap | 1 | ||||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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| Seed (157) |
Full (2991) |
Representative proteomes | UniProt (8294) |
NCBI (9090) |
Meta (492) |
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|---|---|---|---|---|---|---|---|---|---|
| RP15 (659) |
RP35 (1879) |
RP55 (2899) |
RP75 (4239) |
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| Raw Stockholm | |||||||||
| Gzipped | |||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | Pfam-B_1192 (release 8.0) |
| Previous IDs: | none |
| Type: | Domain |
| Sequence Ontology: | SO:0000417 |
| Author: |
Wilbrey A  , Studholme DJ
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| Number in seed: | 157 |
| Number in full: | 2991 |
| Average length of the domain: | 84.00 aa |
| Average identity of full alignment: | 34 % |
| Average coverage of the sequence by the domain: | 30.37 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 105 | ||||||||||||
| Family (HMM) version: | 14 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Eukaryota
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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 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 sequence.
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