Serine acetyltransferase - Escherichia coli (strain K12)

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P0A9D4 (CYSE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 73. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	273 AA.
Sequence status	Complete.
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.8
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 Reference proteome
Gene Ontology (GO)
Biological_process	cysteine biosynthetic process from serine Inferred from direct assay PubMed 5332668. Source: EcoCyc
Cellular_component	cysteine synthase complex Inferred from direct assay PubMed 10993149. Source: EcoCyc
Molecular_function	serine O-acetyltransferase activity Inferred from direct assay PubMed 5332668. Source: EcoCyc
Complete GO annotation...

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

273

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A9D4 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: 466EB898750EF709
Show »

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

« Hide

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[7]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[8]	"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] [Europe PMC] [Abstract] Cited for: SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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

NP_418064.1. NC_000913.2.
YP_491826.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

P0A9D4.

SMR

P0A9D4. Positions 1-262.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A9D4. 2 interactions.

STRING

511145.b3607.

Proteomic databases

PaxDb

P0A9D4.

PRIDE

P0A9D4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76631; AAC76631; b3607.
BAE77685; BAE77685; BAE77685.

GeneID

12930499.
948126.

KEGG

ecj:Y75_p3567.
eco:b3607.

PATRIC

32122699. VBIEscCol129921_3726.

Organism-specific databases

EchoBASE

EB0184.

EcoGene

EG10187. cysE.

Phylogenomic databases

eggNOG

COG1045.

HOGENOM

HOG000049437.

K00640.

OMA

RDIQAVC.

ProtClustDB

PRK11132.

Enzyme and pathway databases

BioCyc

EcoCyc:SERINE-O-ACETTRAN-MONOMER.
ECOL316407:JW3582-MONOMER.
MetaCyc:SERINE-O-ACETTRAN-MONOMER.

BRENDA

2.3.1.30. 2026.

SABIO-RK

P0A9D4.

UniPathway

UPA00136; UER00199.

Gene expression databases

Genevestigator

P0A9D4.

Family and domain databases

InterPro

IPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR010493. Ser_AcTrfase_N.
IPR005881. Ser_O-AcTrfase.
IPR011004. Trimer_LpxA-like.
[Graphical view]

Pfam

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

SMART

SM00971. SATase_N. 1 hit.
[Graphical view]

SUPFAM

SSF51161. Trimer_LpxA_like. 1 hit.

TIGRFAMs

TIGR01172. cysE. 1 hit.

PROSITE

PS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A9D4.

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:	May 1, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents