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Protein

Serine acetyltransferase

Gene

cysE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Acetyl-CoA + L-serine = CoA + O-acetyl-L-serine.

Enzyme regulationi

Sensitive to feedback inhibition by L-cysteine.

Pathwayi

GO - Molecular functioni

  1. serine O-acetyltransferase activity Source: EcoCyc

GO - Biological processi

  1. cysteine biosynthetic process from serine Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Cysteine biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:SERINE-O-ACETTRAN-MONOMER.
ECOL316407:JW3582-MONOMER.
MetaCyc:SERINE-O-ACETTRAN-MONOMER.
RETL1328306-WGS:GSTH-1960-MONOMER.
RETL1328306-WGS:GSTH-3700-MONOMER.
BRENDAi2.3.1.30. 2026.
SABIO-RKP0A9D4.
UniPathwayiUPA00136; UER00199.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine acetyltransferase (EC:2.3.1.30)
Short name:
SAT
Gene namesi
Name:cysE
Ordered Locus Names:b3607, JW3582
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10187. cysE.

Subcellular locationi

GO - Cellular componenti

  1. cysteine synthase complex Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 273273Serine acetyltransferasePRO_0000068669Add
BLAST

Proteomic databases

PaxDbiP0A9D4.
PRIDEiP0A9D4.

Expressioni

Gene expression databases

GenevestigatoriP0A9D4.

Interactioni

Subunit structurei

Homohexamer; dimer of a homotrimer (PubMed:10617639). Forms a cysteine synthase complex with 2 copies of CysK (By similarity).By similarity1 Publication

Protein-protein interaction databases

DIPiDIP-9377N.
IntActiP0A9D4. 2 interactions.
STRINGi511145.b3607.

Structurei

Secondary structure

1
273
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 2321Combined sources
Helixi25 – 273Combined sources
Helixi28 – 347Combined sources
Turni35 – 373Combined sources
Helixi41 – 5313Combined sources
Beta strandi56 – 583Combined sources
Helixi60 – 7314Combined sources
Helixi76 – 9116Combined sources
Helixi99 – 1046Combined sources
Helixi106 – 12318Combined sources
Helixi126 – 14015Combined sources
Beta strandi181 – 1833Combined sources
Beta strandi186 – 1883Combined sources
Beta strandi207 – 2115Combined sources
Beta strandi235 – 2373Combined sources
Turni238 – 2414Combined sources
Beta strandi242 – 2454Combined sources
Beta strandi248 – 2503Combined sources
Helixi252 – 2554Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T3DX-ray2.20A/B/C1-273[»]
ProteinModelPortaliP0A9D4.
SMRiP0A9D4. Positions 1-262.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A9D4.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1045.
HOGENOMiHOG000049437.
InParanoidiP0A9D4.
KOiK00640.
OMAiRGFEDGD.
OrthoDBiEOG6HMXK6.
PhylomeDBiP0A9D4.

Family and domain databases

InterProiIPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR010493. Ser_AcTrfase_N.
IPR005881. Ser_O-AcTrfase.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamiPF00132. Hexapep. 1 hit.
PF06426. SATase_N. 1 hit.
[Graphical view]
SMARTiSM00971. SATase_N. 1 hit.
[Graphical view]
SUPFAMiSSF51161. SSF51161. 1 hit.
TIGRFAMsiTIGR01172. cysE. 1 hit.
PROSITEiPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A9D4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSCEELEIVW NNIKAEARTL ADCEPMLASF YHATLLKHEN LGSALSYMLA
60 70 80 90 100
NKLSSPIMPA IAIREVVEEA YAADPEMIAS AACDIQAVRT RDPAVDKYST
110 120 130 140 150
PLLYLKGFHA LQAYRIGHWL WNQGRRALAI FLQNQVSVTF QVDIHPAAKI
160 170 180 190 200
GRGIMLDHAT GIVVGETAVI ENDVSILQSV TLGGTGKSGG DRHPKIREGV
210 220 230 240 250
MIGAGAKILG NIEVGRGAKI GAGSVVLQPV PPHTTAAGVP ARIVGKPDSD
260 270
KPSMDMDQHF NGINHTFEYG DGI
Length:273
Mass (Da):29,317
Last modified:July 19, 2005 - v1
Checksum:i466EB898750EF709
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA27896. XYECSA.
RefSeqiNP_418064.1. NC_000913.3.
YP_491826.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76631; AAC76631; b3607.
BAE77685; BAE77685; BAE77685.
GeneIDi12930499.
948126.
KEGGiecj:Y75_p3567.
eco:b3607.
PATRICi32122699. VBIEscCol129921_3726.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA27896. XYECSA.
RefSeqiNP_418064.1. NC_000913.3.
YP_491826.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T3DX-ray2.20A/B/C1-273[»]
ProteinModelPortaliP0A9D4.
SMRiP0A9D4. Positions 1-262.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-9377N.
IntActiP0A9D4. 2 interactions.
STRINGi511145.b3607.

Proteomic databases

PaxDbiP0A9D4.
PRIDEiP0A9D4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76631; AAC76631; b3607.
BAE77685; BAE77685; BAE77685.
GeneIDi12930499.
948126.
KEGGiecj:Y75_p3567.
eco:b3607.
PATRICi32122699. VBIEscCol129921_3726.

Organism-specific databases

EchoBASEiEB0184.
EcoGeneiEG10187. cysE.

Phylogenomic databases

eggNOGiCOG1045.
HOGENOMiHOG000049437.
InParanoidiP0A9D4.
KOiK00640.
OMAiRGFEDGD.
OrthoDBiEOG6HMXK6.
PhylomeDBiP0A9D4.

Enzyme and pathway databases

UniPathwayiUPA00136; UER00199.
BioCyciEcoCyc:SERINE-O-ACETTRAN-MONOMER.
ECOL316407:JW3582-MONOMER.
MetaCyc:SERINE-O-ACETTRAN-MONOMER.
RETL1328306-WGS:GSTH-1960-MONOMER.
RETL1328306-WGS:GSTH-3700-MONOMER.
BRENDAi2.3.1.30. 2026.
SABIO-RKP0A9D4.

Miscellaneous databases

EvolutionaryTraceiP0A9D4.
PROiP0A9D4.

Gene expression databases

GenevestigatoriP0A9D4.

Family and domain databases

InterProiIPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR010493. Ser_AcTrfase_N.
IPR005881. Ser_O-AcTrfase.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamiPF00132. Hexapep. 1 hit.
PF06426. SATase_N. 1 hit.
[Graphical view]
SMARTiSM00971. SATase_N. 1 hit.
[Graphical view]
SUPFAMiSSF51161. SSF51161. 1 hit.
TIGRFAMsiTIGR01172. cysE. 1 hit.
PROSITEiPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiCYSE_ECOLI
AccessioniPrimary (citable) accession number: P0A9D4
Secondary accession number(s): P05796, Q2M7S1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: March 4, 2015
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.