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P0A9D4 (CYSE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine acetyltransferase

Short name=SAT
EC=2.3.1.30
Gene names
Name:cysE
Ordered Locus Names:b3607, JW3582
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length273 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processAmino-acid biosynthesis
Cysteine biosynthesis
   Cellular componentCytoplasm
   DomainRepeat
   Molecular functionAcyltransferase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcysteine biosynthetic process from serine

Inferred from direct assay PubMed 5332668. Source: EcoCyc

   Cellular_componentcysteine synthase complex

Inferred from direct assay PubMed 10993149. Source: EcoCyc

   Molecular_functionserine O-acetyltransferase activity

Inferred from direct assay PubMed 5332668. Source: EcoCyc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 273273Serine acetyltransferase
PRO_0000068669

Secondary structure

................................... 273
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A9D4 [UniParc].

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

FASTA27329,317
        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' 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 277:1453-1462(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.
PIRXYECSA. A27896.
RefSeqNP_418064.1. NC_000913.3.
YP_491826.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1T3DX-ray2.20A/B/C1-273[»]
ProteinModelPortalP0A9D4.
SMRP0A9D4. Positions 1-262.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9377N.
IntActP0A9D4. 2 interactions.
STRING511145.b3607.

Proteomic databases

PaxDbP0A9D4.
PRIDEP0A9D4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76631; AAC76631; b3607.
BAE77685; BAE77685; BAE77685.
GeneID12930499.
948126.
KEGGecj:Y75_p3567.
eco:b3607.
PATRIC32122699. VBIEscCol129921_3726.

Organism-specific databases

EchoBASEEB0184.
EcoGeneEG10187. cysE.

Phylogenomic databases

eggNOGCOG1045.
HOGENOMHOG000049437.
KOK00640.
OMADRDPACH.
OrthoDBEOG6HMXK6.
PhylomeDBP0A9D4.
ProtClustDBPRK11132.

Enzyme and pathway databases

BioCycEcoCyc:SERINE-O-ACETTRAN-MONOMER.
ECOL316407:JW3582-MONOMER.
MetaCyc:SERINE-O-ACETTRAN-MONOMER.
BRENDA2.3.1.30. 2026.
SABIO-RKP0A9D4.
UniPathwayUPA00136; UER00199.

Gene expression databases

GenevestigatorP0A9D4.

Family and domain databases

InterProIPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR010493. Ser_AcTrfase_N.
IPR005881. Ser_O-AcTrfase.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamPF00132. Hexapep. 1 hit.
PF06426. SATase_N. 1 hit.
[Graphical view]
SMARTSM00971. SATase_N. 1 hit.
[Graphical view]
SUPFAMSSF51161. SSF51161. 1 hit.
TIGRFAMsTIGR01172. cysE. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A9D4.
PROP0A9D4.

Entry information

Entry nameCYSE_ECOLI
AccessionPrimary (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: April 16, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

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