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P0A9D4

- CYSE_ECOLI

UniProt

P0A9D4 - CYSE_ECOLI

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Protein

Serine acetyltransferase

Gene
cysE, b3607, JW3582
Organism
Escherichia coli (strain K12)
Status
Reviewed - 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: Chromosome, UP000000625: 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.1 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 – 2321
Helixi25 – 273
Helixi28 – 347
Turni35 – 373
Helixi41 – 5313
Beta strandi56 – 583
Helixi60 – 7314
Helixi76 – 9116
Helixi99 – 1046
Helixi106 – 12318
Helixi126 – 14015
Beta strandi181 – 1833
Beta strandi186 – 1883
Beta strandi207 – 2115
Beta strandi235 – 2373
Turni238 – 2414
Beta strandi242 – 2454
Beta strandi248 – 2503
Helixi252 – 2554

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T3DX-ray2.20A/B/C1-273[»]
ProteinModelPortaliP0A9D4.
SMRiP0A9D4. Positions 1-262.

Miscellaneous databases

EvolutionaryTraceiP0A9D4.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1045.
HOGENOMiHOG000049437.
KOiK00640.
OMAiRDIQAVC.
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

MSCEELEIVW NNIKAEARTL ADCEPMLASF YHATLLKHEN LGSALSYMLA    50
NKLSSPIMPA IAIREVVEEA YAADPEMIAS AACDIQAVRT RDPAVDKYST 100
PLLYLKGFHA LQAYRIGHWL WNQGRRALAI FLQNQVSVTF QVDIHPAAKI 150
GRGIMLDHAT GIVVGETAVI ENDVSILQSV TLGGTGKSGG DRHPKIREGV 200
MIGAGAKILG NIEVGRGAKI GAGSVVLQPV PPHTTAAGVP ARIVGKPDSD 250
KPSMDMDQHF NGINHTFEYG DGI 273
Length:273
Mass (Da):29,317
Last modified:July 19, 2005 - v1
Checksum:i466EB898750EF709
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi A27896. XYECSA.
RefSeqi NP_418064.1. NC_000913.3.
YP_491826.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1T3D X-ray 2.20 A/B/C 1-273 [» ]
ProteinModelPortali P0A9D4.
SMRi P0A9D4. Positions 1-262.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-9377N.
IntActi P0A9D4. 2 interactions.
STRINGi 511145.b3607.

Proteomic databases

PaxDbi P0A9D4.
PRIDEi P0A9D4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76631 ; AAC76631 ; b3607 .
BAE77685 ; BAE77685 ; BAE77685 .
GeneIDi 12930499.
948126.
KEGGi ecj:Y75_p3567.
eco:b3607.
PATRICi 32122699. VBIEscCol129921_3726.

Organism-specific databases

EchoBASEi EB0184.
EcoGenei EG10187. cysE.

Phylogenomic databases

eggNOGi COG1045.
HOGENOMi HOG000049437.
KOi K00640.
OMAi RDIQAVC.
OrthoDBi EOG6HMXK6.
PhylomeDBi P0A9D4.

Enzyme and pathway databases

UniPathwayi UPA00136 ; UER00199 .
BioCyci EcoCyc:SERINE-O-ACETTRAN-MONOMER.
ECOL316407:JW3582-MONOMER.
MetaCyc:SERINE-O-ACETTRAN-MONOMER.
RETL1328306-WGS:GSTH-1960-MONOMER.
RETL1328306-WGS:GSTH-3700-MONOMER.
BRENDAi 2.3.1.30. 2026.
SABIO-RK P0A9D4.

Miscellaneous databases

EvolutionaryTracei P0A9D4.
PROi P0A9D4.

Gene expression databases

Genevestigatori P0A9D4.

Family and domain databases

InterProi IPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR010493. Ser_AcTrfase_N.
IPR005881. Ser_O-AcTrfase.
IPR011004. Trimer_LpxA-like.
[Graphical view ]
Pfami PF00132. Hexapep. 1 hit.
PF06426. SATase_N. 1 hit.
[Graphical view ]
SMARTi SM00971. SATase_N. 1 hit.
[Graphical view ]
SUPFAMi SSF51161. SSF51161. 1 hit.
TIGRFAMsi TIGR01172. cysE. 1 hit.
PROSITEi PS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 80 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

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