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76  structures 2141  species 0  interactions 3273  sequences 39  architectures

Family: SATase_N (PF06426)

Summary: Serine acetyltransferase, N-terminal

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

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

Serine O-acetyltransferase Edit Wikipedia article

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.

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.

References

Template:Enzyme references

  • Kredich NM, Tomkins GM (1966). "The enzymic synthesis of L-cysteine in Escherichia coli and Salmonella typhimurium". J. Biol. Chem. 241: 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: 288–95. PMID 5550822.

External links

The CAS registry number for this enzyme class is Template:CAS registry.

Template:Enzyme links

Gene Ontology (GO) codes

Template:GO code links

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


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

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 and the UniProtKB sequence database. More...

View options

We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(130)
Full
(3273)
Representative proteomes UniProt
(12405)
RP15
(512)
RP35
(1669)
RP55
(3238)
RP75
(5379)
Jalview View  View  View  View  View  View  View 
HTML View  View           
PP/heatmap 1 View           

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(130)
Full
(3273)
Representative proteomes UniProt
(12405)
RP15
(512)
RP35
(1669)
RP55
(3238)
RP75
(5379)
Alignment:
Format:
Order:
Sequence:
Gaps:
Download/view:

Download options

We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(130)
Full
(3273)
Representative proteomes UniProt
(12405)
RP15
(512)
RP35
(1669)
RP55
(3238)
RP75
(5379)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download  

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 View help on the curation process

Seed source: Pfam-B_1192 (release 8.0)
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Wilbrey A , Studholme DJ
Number in seed: 130
Number in full: 3273
Average length of the domain: 90.9 aa
Average identity of full alignment: 34 %
Average coverage of the sequence by the domain: 31.5 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.0 21.0
Trusted cut-off 21.0 21.0
Noise cut-off 20.9 20.9
Model length: 105
Family (HMM) version: 17
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence

Selections

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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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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 76 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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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A096QL71 View 3D Structure Click here
A0A0H3H4G5 View 3D Structure Click here
A0A0R4J5I5 View 3D Structure Click here
A0A1D6MA66 View 3D Structure Click here
A0A368UIQ7 View 3D Structure Click here
A8F961 View 3D Structure Click here
B4FLW0 View 3D Structure Click here
B4FRV1 View 3D Structure Click here
I1JJI6 View 3D Structure Click here
I1KHY6 View 3D Structure Click here
I1KYI0 View 3D Structure Click here
I1M6H4 View 3D Structure Click here
I1N0C4 View 3D Structure Click here
K7K6E3 View 3D Structure Click here
K7LNN3 View 3D Structure Click here
K7MGT5 View 3D Structure Click here
P0A9D4 View 3D Structure Click here
P0A9D6 View 3D Structure Click here
P0A9D7 View 3D Structure Click here
P29847 View 3D Structure Click here
P43886 View 3D Structure Click here
P57162 View 3D Structure Click here
Q0DGG8 View 3D Structure Click here
Q0DUI1 View 3D Structure Click here
Q10QH1 View 3D Structure Click here
Q10S58 View 3D Structure Click here
Q329P7 View 3D Structure Click here
Q39218 View 3D Structure Click here
Q42538 View 3D Structure Click here
Q42588 View 3D Structure Click here
Q5F6X0 View 3D Structure Click here
Q89B11 View 3D Structure Click here
Q8S895 View 3D Structure Click here
Q8W0E4 View 3D Structure Click here
Q8W2B8 View 3D Structure Click here
Q9US33 View 3D Structure Click here