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InterPro: IPR005881 Serine O-acetyltransferase

Protein matchesHelp
UniProtKB
Matches:
1342 proteins
AccessionHelp IPR005881 Ser_O-AcTrfase
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Contains IPR001451 Bacterial transferase hexapeptide repeat
IPR011004 Trimeric LpxA-like
IPR018357 Hexapeptide transferase, conserved site
GO Term annotationHelp
Process GO:0006535 cysteine biosynthetic process from serine
Function GO:0009001 serine O-acetyltransferase activity
Component GO:0005737 cytoplasm
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

The biosynthesis of L-cysteine is the predominant way by which inorganic sulphur is incorporated into organic compounds. In this process, the most abundant utilizable source of sulphur, inorganic sulphate, is taken up and reduced to sulphide. Sulphide is used to produce L-cysteine, which serves for protein synthesis or the production of other sulphur-containing organic compounds. Two routes for cysteine biosynthesis in nature have been documented. Serine transacetylase (EC:2.3.1.30) catalyzes steps in pathway I, the activation of L-serine by acetyl-coenzyme A, yielding O-acetyl-L-serine.

Structural linksHelp
SCOP: b.81.1.6
Database linksHelp
Enzyme: EC:2.3.1.30

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR005881 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P0A9D4 Serine acetyltransferase

P74089 Serine acetyltransferase

Q0DGG8 Probable serine acetyltransferase 5

Q39218 Serine acetyltransferase 3, mitochondrial

Q56002 Serine acetyltransferase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR010493 Serine acetyltransferase, N-terminal
IPR018357 Hexapeptide transferase, conserved site
IPR005881 Serine O-acetyltransferase
IPR001451 Bacterial transferase hexapeptide repeat
IPR011004 Trimeric LpxA-like
SWISS-MODEL
PDB Chain
ModBase
CATH Domain
SCOP Domain

PublicationsHelp

Additional ReadingHelp
Olsen LR, Huang B, Vetting MW, Roderick SL.
Structure of serine acetyltransferase in complexes with CoA and its cysteine feedback inhibitor.
Biochemistry 43 2004 6013-9 [PubMed: 15147185]
http://dx.doi.org/10.1021/bi0358521
Pye VE, Tingey AP, Robson RL, Moody PC.
The structure and mechanism of serine acetyltransferase from Escherichia coli.
J. Biol. Chem. 279 2004 40729-36 [PubMed: 15231846]
http://dx.doi.org/10.1074/jbc.M403751200
Gorman J, Shapiro L.
Structure of serine acetyltransferase from Haemophilus influenzae Rd.
Acta Crystallogr. D Biol. Crystallogr. 60 2004 1600-5 [PubMed: 15333931]
http://dx.doi.org/10.1107/S0907444904015240
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InterPro 23.1