Reviewed, UniProtKB/Swiss-Prot P0A9D4 (CYSE_ECOLI)

Names and origin

Protein names

Recommended name:
    Serine acetyltransferase
      Short name=SAT
    EC=2.3.1.30

Gene names

Name:	cysE
Ordered Locus Names:	b3607, JW3582

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	273 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Acetyl-CoA + L-serine = CoA + O-acetyl-L-serine.
Enzyme regulation	Sensitive to feedback inhibition by L-cysteine.
Pathway	Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 1/2.
Subunit structure	Homohexamer. Dimer of a homotrimer. Ref.7
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the transferase hexapeptide repeat family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Cysteine biosynthesis
Cellular component	Cytoplasm
Domain	Repeat
Molecular function	Acyltransferase Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cysteine biosynthetic process from serine Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Inferred from physical interaction. Source: IntAct serine O-acetyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
nadE	P18843	1	EBI-1133237,EBI-548960

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 273

273

Serine acetyltransferase

PRO_0000068669

Secondary structure

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273

Helix Strand Turn

Details...

Helix

3 – 23

21

Helix

25 – 27

3

Helix

28 – 34

7

Turn

35 – 37

3

Helix

41 – 53

13

Beta strand

56 – 58

3

Helix

60 – 73

14

Helix

76 – 91

16

Helix

99 – 104

6

Helix

106 – 123

18

Helix

126 – 140

15

Beta strand

181 – 183

3

Beta strand

186 – 188

3

Beta strand

207 – 211

5

Beta strand

235 – 237

3

Turn

238 – 241

4

Beta strand

242 – 245

4

Beta strand

248 – 250

3

Helix

252 – 255

4

Sequences

	Sequence		Length	Mass (Da)
	P0A9D4-1 [UniParc]. Last modified July 19, 2005. Version 1. Checksum: 466EB898750EF709	FASTA	273	29,317
	10 20 30 40 50 60 MSCEELEIVW NNIKAEARTL ADCEPMLASF YHATLLKHEN LGSALSYMLA NKLSSPIMPA 70 80 90 100 110 120 IAIREVVEEA YAADPEMIAS AACDIQAVRT RDPAVDKYST PLLYLKGFHA LQAYRIGHWL 130 140 150 160 170 180 WNQGRRALAI FLQNQVSVTF QVDIHPAAKI GRGIMLDHAT GIVVGETAVI ENDVSILQSV 190 200 210 220 230 240 TLGGTGKSGG DRHPKIREGV MIGAGAKILG NIEVGRGAKI GAGSVVLQPV PPHTTAAGVP 250 260 270 ARIVGKPDSD KPSMDMDQHF NGINHTFEYG DGI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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." Denk D., Boeck A. J. Gen. Microbiol. 133:515-525(1987) [PubMed: 3309158] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Structure and expression of cysX, the second gene in the Escherichia coli K-12 cysE locus." Tei H., Murata K., Kimura A. Biochem. Biophys. Res. Commun. 167:948-955(1990) [PubMed: 2108679] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[3]	"Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes." Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R. Nucleic Acids Res. 22:2576-2586(1994) [PubMed: 8041620] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"The serine acetyltransferase from Escherichia coli. Over-expression, purification and preliminary crystallographic analysis." Wigley D.B., Derrick J.P., Shaw W.V. FEBS Lett. 277:267-271(1990) [PubMed: 2125278] [Abstract] Cited for: CHARACTERIZATION.
[7]	"Serine acetyltransferase from Escherichia coli is a dimer of trimers." Hindson V.J., Moody P.C., Rowe A.J., Shaw W.V. J. Biol. Chem. 275:461-466(2000) [PubMed: 10617639] [Abstract] Cited for: SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M15745 Genomic DNA. Translation: AAA23648.1.
M34333 Genomic DNA. Translation: AAA23659.1.
U00039 Genomic DNA. Translation: AAB18584.1.
U00096 Genomic DNA. Translation: AAC76631.1.
AP009048 Genomic DNA. Translation: BAE77685.1.

PIR

XYECSA. A27896.

RefSeq

AP_004184.1.
NP_418064.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1T3D	X-ray	2.20	A/B/C	1-273	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A9D4. 2 interactions.

2-D gel databases

ECO2DBASE

H029.3. 6TH EDITION.

Genome annotation databases

GeneID

948126.

GenomeReviews

Gene locus JW3582 in contig AP009048_GR.
Gene locus b3607 in contig U00096_GR.

KEGG

ecj:JW3582.
eco:b3607.

Organism-specific databases

EchoBASE

EB0184.

EcoGene

EG10187. cysE.

CMR

Search...

Phylogenomic databases

HOGENOM

P0A9D4.

OMA

P0A9D4. DLIRQTF.

Enzyme and pathway databases

BioCyc

EcoCyc:SERINE-O-ACETTRAN-MON.
MetaCyc:SERINE-O-ACETTRAN-MON.

BRENDA

2.3.1.30. 246.

Family and domain databases

InterPro

IPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR010493. Ser_AcTrfase_N.
IPR005881. Ser_O-AcTrfase.
[Graphical view]

Pfam

PF00132. Hexapep. 3 hits.
PF06426. SATase_N. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01172. cysE. 1 hit.

PROSITE

PS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

CYSE_ECOLI

Accession

Primary (citable) accession number: P0A9D4
Secondary accession number(s): P05796, Q2M7S1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	July 19, 2005
Last modified:	June 16, 2009
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)