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InterPro: IPR010493 Serine acetyltransferase, N-terminal

Protein matches Help

UniProtKB

Matches:

542 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR010493 Ser_AcTrfase_N

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF06426	SATase_N	542
Signatures in BioMart

InterPro Relationships Help

Found in

IPR011004 Trimeric LpxA-like

GO Term annotation Help

Process

GO:0006535 cysteine biosynthetic process from serine

Function

GO:0009001 serine O-acetyltransferase activity

Component

GO:0005737 cytoplasm

InterPro annotation

Entry Details in BioMart

Abstract

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

Structural links Help

PDB - click here

SCOP: b.81.1.6

CATH: 1.10.3130.10

Database links Help

Enzyme: EC:2.3.1.30

PANDIT: PF06426

Blocks: IPB010493

CluSTr: ALLvsALL:41630:47

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR010493

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P0A9D4 Serine acetyltransferase

Q0DGG8 Probable serine acetyltransferase 5

Q39218 Serine acetyltransferase 3, mitochondrial

Q9US33 Putative 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

Publications Open in usermanual
1.	Saito K, Yokoyama H, Noji M, Murakoshi I. Molecular cloning and characterization of a plant serine acetyltransferase playing a regulatory role in cysteine biosynthesis from watermelon. J. Biol. Chem. 270 16321-6 1995 [PubMed: 7608200] http://dx.doi.org/10.1074/jbc.270.27.16321

Additional Reading Open in usermanual
	Denk D, Bock A. 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 1987 515-25 [PubMed: 3309158]
	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

InterPro 23.1