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UniProtKB/Swiss-Prot entry P0A9D4


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CYSE_ECOLI
Primary accession number P0A9D4
Secondary accession numbers P05796 Q2M7S1
Integrated into Swiss-Prot on July 19, 2005
Sequence was last modified on July 19, 2005 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 35)
Name and origin of the protein
Protein name Serine acetyltransferase
Synonyms SAT
EC 2.3.1.30
Gene name
Name: cysE
OrderedLocusNames: b3607, JW3582
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3309158 [NCBI, ExPASy, EBI, Israel, Japan]
Denk D., Boeck A.;
"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.";
J. Gen. Microbiol. 133:515-525(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
DOI=10.1016/0006-291X(90)90615-T; PubMed=2108679 [NCBI, ExPASy, EBI, Israel, Japan]
Tei H., Murata K., Kimura A.;
"Structure and expression of cysX, the second gene in the Escherichia coli K-12 cysE locus.";
Biochem. Biophys. Res. Commun. 167:948-955(1990).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1093/nar/22.13.2576; PubMed=8041620 [NCBI, ExPASy, EBI, Israel, Japan]
Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
"Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes.";
Nucleic Acids Res. 22:2576-2586(1994).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
CHARACTERIZATION.
DOI=10.1016/0014-5793(90)80862-D; PubMed=2125278 [NCBI, ExPASy, EBI, Israel, Japan]
Wigley D.B., Derrick J.P., Shaw W.V.;
"The serine acetyltransferase from Escherichia coli. Over-expression, purification and preliminary crystallographic analysis.";
FEBS Lett. 277:267-271(1990).
[7]
SUBUNIT.
DOI=10.1074/jbc.275.1.461; PubMed=10617639 [NCBI, ExPASy, EBI, Israel, Japan]
Hindson V.J., Moody P.C., Rowe A.J., Shaw W.V.;
"Serine acetyltransferase from Escherichia coli is a dimer of trimers.";
J. Biol. Chem. 275:461-466(2000).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M15745; AAA23648.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M34333; AAA23659.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00039; AAB18584.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC76631.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE77685.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A27896; XYECSA.
RefSeq AP_004184.1; -.
NP_418064.1; -.
3D structure databases
PDB
1T3D; X-ray; 2.20 A; A/B/C=1-273.[ExPASy / RCSB / EBI]
PDBsum 1T3D; -.
ModBase P0A9D4.
Protein-protein interaction databases
IntAct P0A9D4; -.
Enzyme and pathway databases
BioCyc EcoCyc:SERINE-O-ACETTRAN-MON; -.
MetaCyc:SERINE-O-ACETTRAN-MON; -.
2D gel databases
ECO2DBASE H029.3; 6TH EDITION.
Organism-specific databases
EchoBASE EB0184; -.
EcoGene EG10187; cysE.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR001451; Hexapep_transf.
IPR010493; Ser_AcTrfase_N.
IPR005881; Ser_O-AcTrfase.
Graphical view of domain structure.
Pfam PF00132; Hexapep; 3.
PF06426; SATase_N; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR01172; cysE; 1.
PROSITE PS00101; HEXAPEP_TRANSFERASES; 1.
BLOCKS P0A9D4.
Genome annotation databases
GeneID 948126; -.
GenomeReviews U00096_GR; b3607.
AP009048_GR; JW3582.
KEGG ecj:JW3582; -.
eco:b3607; -.
Phylogenomic databases
HOGENOM P0A9D4; -.
Genome annotation databases
CMR P0A9D4; b3607.
Other
ProtoNet P0A9D4.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acyltransferase; Amino-acid biosynthesis; Complete proteome; Cysteine biosynthesis; Cytoplasm; Repeat; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   273  273     Serine acetyltransferase. PRO_0000068669
HELIX   3    23  21      
HELIX   25    27  3      
HELIX   28    34  7      
TURN   35    37  3      
HELIX   41    53  13      
STRAND   56    58  3      
HELIX   60    73  14      
HELIX   76    91  16      
HELIX   99   104  6      
HELIX   106   123  18      
HELIX   126   140  15      
STRAND   181   183  3      
STRAND   186   188  3      
STRAND   207   211  5      
STRAND   235   237  3      
TURN   238   241  4      
STRAND   242   245  4      
STRAND   248   250  3      
HELIX   252   255  4      
Sequence information
Length: 273 AA [This is the length of the unprocessed precursor] Molecular weight: 29317 Da [This is the MW of the unprocessed precursor] CRC64: 466EB898750EF709 [This is a checksum on the sequence]
        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 

P0A9D4 in FASTA format

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