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UniProtKB/Swiss-Prot entry P00963


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

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Entry information
Entry name ASNA_ECOLI
Primary accession number P00963
Secondary accession number Q2M862
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on July 21, 1986 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 87)
Name and origin of the protein
Protein name Aspartate--ammonia ligase
Synonyms EC 6.3.1.1
Asparagine synthetase A
Gene name
Name: asnA
OrderedLocusNames: b3744, JW3722
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].
STRAIN=K12;
DOI=10.1093/nar/9.18.4669; PubMed=6117826 [NCBI, ExPASy, EBI, Israel, Japan]
Nakamura M., Yamada M., Hirota Y., Sugimoto K., Oka A., Takanami M.;
"Nucleotide sequence of the asnA gene coding for asparagine synthetase of E. coli K-12.";
Nucleic Acids Res. 9:4669-4676(1981).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0378-1119(83)90087-2; PubMed=6357950 [NCBI, ExPASy, EBI, Israel, Japan]
Buhk H.-J., Messer W.;
"The replication origin region of Escherichia coli: nucleotide sequence and functional units.";
Gene 24:265-279(1983).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1006/geno.1993.1230; PubMed=7686882 [NCBI, ExPASy, EBI, Israel, Japan]
Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
"DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication.";
Genomics 16:551-561(1993).
[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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-252.
PubMed=383377 [NCBI, ExPASy, EBI, Israel, Japan]
Hirota Y., Yasuda S., Yamada M., Nishimura A., Sugimoto K., Sugisaki H., Oka A., Takanami M.;
"Structural and functional properties of the Escherichia coli origin of DNA replication.";
Cold Spring Harb. Symp. Quant. Biol. 43:129-138(1979).
[7]
PROTEIN SEQUENCE OF 1-5.
STRAIN=K12;
PubMed=1369484 [NCBI, ExPASy, EBI, Israel, Japan]
Sugiyama A., Kato H., Nishioka T., Oda J.;
"Overexpression and purification of asparagine synthetase from Escherichia coli.";
Biosci. Biotechnol. Biochem. 56:376-379(1992).
[8]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
STRAIN=K12;
DOI=10.1038/nsb0198-15; PubMed=9437423 [NCBI, ExPASy, EBI, Israel, Japan]
Nakatsu T., Kato H., Oda J.;
"Crystal structure of asparagine synthetase reveals a close evolutionary relationship to class II aminoacyl-tRNA synthetase.";
Nat. Struct. Biol. 5:15-19(1998).
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
V00263; CAA23512.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K00826; AAA24253.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J01657; AAA24248.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L10328; AAA62096.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC76767.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE77544.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M10679; AAA24249.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A01191; AJECNA.
RefSeq AP_004043.1; -.
NP_418200.1; -.
3D structure databases
PDB
11AS; X-ray; 2.50 A; A/B=1-330.[ExPASy / RCSB / EBI]
12AS; X-ray; 2.20 A; A/B=1-330.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 11AS; -.
12AS; -.
ModBase P00963.
Protein-protein interaction databases
DIP DIP:9176N; -.
IntAct P00963; 4.
Enzyme and pathway databases
BioCyc EcoCyc:ASNSYNA-MON; -.
MetaCyc:ASNSYNA-MON; -.
2D gel databases
SWISS-2DPAGE P00963; -.
Organism-specific databases
EchoBASE EB0089; -.
EcoGene EG10091; asnA.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004812; Molecular function: aminoacyl-tRNA ligase activity (inferred from electronic annotation from InterPro).
GO:0004071; Molecular function: aspartate-ammonia ligase activity (inferred from electronic annotation from HAMAP).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006529; Biological process: asparagine biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0006418; Biological process: tRNA aminoacylation for protein translation (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
HAMAP MF_00555; -; 1.
PBIL [Tree]
InterPro IPR006195; aa-tRNA-synth_II.
IPR004618; AsnA.
Graphical view of domain structure.
Pfam PF03590; AsnA; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001555; Asp_ammon_ligase; 1.
ProDom PD024629; AsnA; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00669; asnA; 1.
PROSITE PS50862; AA_TRNA_LIGASE_II; 1.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
GeneID 948258; -.
GenomeReviews AP009048_GR; JW3722.
U00096_GR; b3744.
KEGG ecj:JW3722; -.
eco:b3744; -.
Phylogenomic databases
HOGENOM P00963; -.
Other
DrugBank DB00131; Adenosine monophosphate.
Genome annotation databases
CMR P00963; b3744.
Other
ProtoNet P00963.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Amino-acid biosynthesis; Asparagine biosynthesis; Complete proteome; Cytoplasm; Direct protein sequencing; Ligase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   330  330     Aspartate--ammonia ligase. PRO_0000195873
HELIX   5    27  23      
STRAND   29    31  3      
STRAND   36    39  4      
TURN   48    51  4      
STRAND   60    62  3      
STRAND   67    69  3      
HELIX   76    83  8      
STRAND   91    99  9      
STRAND   112   122  11      
HELIX   130   154  25      
STRAND   166   169  4      
HELIX   170   176  7      
STRAND   177   180  4      
HELIX   182   193  12      
STRAND   194   199  6      
STRAND   206   208  3      
TURN   216   218  3      
STRAND   222   224  3      
STRAND   228   230  3      
STRAND   232   240  9      
TURN   241   244  4      
STRAND   245   255  11      
HELIX   258   268  11      
HELIX   273   275  3      
HELIX   277   283  7      
STRAND   290   296  7      
HELIX   297   305  9      
HELIX   310   312  3      
HELIX   320   325  6      
Sequence information
Length: 330 AA [This is the length of the unprocessed precursor] Molecular weight: 36651 Da [This is the MW of the unprocessed precursor] CRC64: 2A8D2E3ECE523FDD [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKTAYIAKQR QISFVKSHFS RQLEERLGLI EVQAPILSRV GDGTQDNLSG CEKAVQVKVK 

        70         80         90        100        110        120 
ALPDAQFEVV HSLAKWKRQT LGQHDFSAGE GLYTHMKALR PDEDRLSPLH SVYVDQWDWE 

       130        140        150        160        170        180 
RVMGDGERQF STLKSTVEAI WAGIKATEAA VSEEFGLAPF LPDQIHFVHS QELLSRYPDL 

       190        200        210        220        230        240 
DAKGRERAIA KDLGAVFLVG IGGKLSDGHR HDVRAPDYDD WSTPSELGHA GLNGDILVWN 

       250        260        270        280        290        300 
PVLEDAFELS SMGIRVDADT LKHQLALTGD EDRLELEWHQ ALLRGEMPQT IGGGIGQSRL 

       310        320        330 
TMLLLQLPHI GQVQCGVWPA AVRESVPSLL 

P00963 in FASTA format

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