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Protein

Aspartate--ammonia ligase

Gene

asnA

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

Functioni

May amidate Asp of the extracellular death factor precursor Asn-Asn-Trp-Asp-Asn to generate Asn-Asn-Trp-Asn-Asn.1 Publication

Catalytic activityi

ATP + L-aspartate + NH3 = AMP + diphosphate + L-asparagine.

Pathwayi: L-asparagine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-asparagine from L-aspartate (ammonia route).
Proteins known to be involved in this subpathway in this organism are:
  1. Aspartate--ammonia ligase (asnA)
This subpathway is part of the pathway L-asparagine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-asparagine from L-aspartate (ammonia route), the pathway L-asparagine biosynthesis and in Amino-acid biosynthesis.

GO - Molecular functioni

  • aminoacyl-tRNA ligase activity Source: InterPro
  • aspartate-ammonia ligase activity Source: EcoCyc
  • ATP binding Source: UniProtKB-HAMAP

GO - Biological processi

  • asparagine biosynthetic process Source: EcoCyc
  • cellular response to DNA damage stimulus Source: EcoliWiki
  • L-asparagine biosynthetic process Source: UniProtKB-UniPathway
  • tRNA aminoacylation for protein translation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Amino-acid biosynthesis, Asparagine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:ASNSYNA-MONOMER.
ECOL316407:JW3722-MONOMER.
MetaCyc:ASNSYNA-MONOMER.
UniPathwayiUPA00134; UER00194.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartate--ammonia ligase (EC:6.3.1.1)
Alternative name(s):
Asparagine synthetase A
Gene namesi
Name:asnA
Ordered Locus Names:b3744, JW3722
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10091. asnA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Loss of production of extracellular death factor.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 330330Aspartate--ammonia ligasePRO_0000195873Add
BLAST

Proteomic databases

EPDiP00963.
PaxDbiP00963.
PRIDEiP00963.

2D gel databases

SWISS-2DPAGEP00963.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi4263263. 101 interactions.
DIPiDIP-9176N.
IntActiP00963. 5 interactions.
STRINGi511145.b3744.

Structurei

Secondary structure

1
330
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 2723Combined sources
Beta strandi29 – 313Combined sources
Beta strandi36 – 394Combined sources
Turni48 – 514Combined sources
Beta strandi60 – 623Combined sources
Beta strandi67 – 693Combined sources
Helixi76 – 838Combined sources
Beta strandi91 – 999Combined sources
Beta strandi112 – 12211Combined sources
Helixi130 – 15425Combined sources
Beta strandi166 – 1694Combined sources
Helixi170 – 1767Combined sources
Beta strandi177 – 1804Combined sources
Helixi182 – 19312Combined sources
Beta strandi194 – 1996Combined sources
Beta strandi202 – 2043Combined sources
Beta strandi206 – 2083Combined sources
Beta strandi210 – 2123Combined sources
Turni216 – 2183Combined sources
Beta strandi222 – 2243Combined sources
Beta strandi228 – 2303Combined sources
Beta strandi232 – 2409Combined sources
Turni241 – 2444Combined sources
Beta strandi245 – 25511Combined sources
Helixi258 – 26811Combined sources
Helixi273 – 2753Combined sources
Helixi277 – 2837Combined sources
Beta strandi290 – 2967Combined sources
Helixi297 – 3059Combined sources
Helixi310 – 3123Combined sources
Helixi320 – 3256Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
11ASX-ray2.50A/B1-330[»]
12ASX-ray2.20A/B1-330[»]
ProteinModelPortaliP00963.
SMRiP00963. Positions 4-330.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00963.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CU9. Bacteria.
COG2502. LUCA.
HOGENOMiHOG000284502.
InParanoidiP00963.
KOiK01914.
OMAiQSRICMF.
OrthoDBiEOG64V2FB.
PhylomeDBiP00963.

Family and domain databases

HAMAPiMF_00555. AsnA.
InterProiIPR006195. aa-tRNA-synth_II.
IPR004618. AsnA.
[Graphical view]
PfamiPF03590. AsnA. 1 hit.
[Graphical view]
PIRSFiPIRSF001555. Asp_ammon_ligase. 1 hit.
TIGRFAMsiTIGR00669. asnA. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00963-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTAYIAKQR QISFVKSHFS RQLEERLGLI EVQAPILSRV GDGTQDNLSG
60 70 80 90 100
CEKAVQVKVK ALPDAQFEVV HSLAKWKRQT LGQHDFSAGE GLYTHMKALR
110 120 130 140 150
PDEDRLSPLH SVYVDQWDWE RVMGDGERQF STLKSTVEAI WAGIKATEAA
160 170 180 190 200
VSEEFGLAPF LPDQIHFVHS QELLSRYPDL DAKGRERAIA KDLGAVFLVG
210 220 230 240 250
IGGKLSDGHR HDVRAPDYDD WSTPSELGHA GLNGDILVWN PVLEDAFELS
260 270 280 290 300
SMGIRVDADT LKHQLALTGD EDRLELEWHQ ALLRGEMPQT IGGGIGQSRL
310 320 330
TMLLLQLPHI GQVQCGVWPA AVRESVPSLL
Length:330
Mass (Da):36,651
Last modified:July 21, 1986 - v1
Checksum:i2A8D2E3ECE523FDD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00263 Genomic DNA. Translation: CAA23512.1. Sequence problems.
K00826 Genomic DNA. Translation: AAA24253.1.
J01657 Genomic DNA. Translation: AAA24248.1.
L10328 Genomic DNA. Translation: AAA62096.1.
U00096 Genomic DNA. Translation: AAC76767.1.
AP009048 Genomic DNA. Translation: BAE77544.1.
M10679 Genomic DNA. Translation: AAA24249.1.
PIRiA01191. AJECNA.
RefSeqiNP_418200.1. NC_000913.3.
WP_000845104.1. NZ_LN832404.1.
YP_006952153.1. NC_019049.1.

Genome annotation databases

EnsemblBacteriaiAAC76767; AAC76767; b3744.
BAE77544; BAE77544; BAE77544.
GeneIDi13905103.
948258.
KEGGiecj:JW3722.
eco:b3744.
pg:13905103.
PATRICi32122987. VBIEscCol129921_3869.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00263 Genomic DNA. Translation: CAA23512.1. Sequence problems.
K00826 Genomic DNA. Translation: AAA24253.1.
J01657 Genomic DNA. Translation: AAA24248.1.
L10328 Genomic DNA. Translation: AAA62096.1.
U00096 Genomic DNA. Translation: AAC76767.1.
AP009048 Genomic DNA. Translation: BAE77544.1.
M10679 Genomic DNA. Translation: AAA24249.1.
PIRiA01191. AJECNA.
RefSeqiNP_418200.1. NC_000913.3.
WP_000845104.1. NZ_LN832404.1.
YP_006952153.1. NC_019049.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
11ASX-ray2.50A/B1-330[»]
12ASX-ray2.20A/B1-330[»]
ProteinModelPortaliP00963.
SMRiP00963. Positions 4-330.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263263. 101 interactions.
DIPiDIP-9176N.
IntActiP00963. 5 interactions.
STRINGi511145.b3744.

2D gel databases

SWISS-2DPAGEP00963.

Proteomic databases

EPDiP00963.
PaxDbiP00963.
PRIDEiP00963.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76767; AAC76767; b3744.
BAE77544; BAE77544; BAE77544.
GeneIDi13905103.
948258.
KEGGiecj:JW3722.
eco:b3744.
pg:13905103.
PATRICi32122987. VBIEscCol129921_3869.

Organism-specific databases

EchoBASEiEB0089.
EcoGeneiEG10091. asnA.

Phylogenomic databases

eggNOGiENOG4105CU9. Bacteria.
COG2502. LUCA.
HOGENOMiHOG000284502.
InParanoidiP00963.
KOiK01914.
OMAiQSRICMF.
OrthoDBiEOG64V2FB.
PhylomeDBiP00963.

Enzyme and pathway databases

UniPathwayiUPA00134; UER00194.
BioCyciEcoCyc:ASNSYNA-MONOMER.
ECOL316407:JW3722-MONOMER.
MetaCyc:ASNSYNA-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP00963.
PROiP00963.

Family and domain databases

HAMAPiMF_00555. AsnA.
InterProiIPR006195. aa-tRNA-synth_II.
IPR004618. AsnA.
[Graphical view]
PfamiPF03590. AsnA. 1 hit.
[Graphical view]
PIRSFiPIRSF001555. Asp_ammon_ligase. 1 hit.
TIGRFAMsiTIGR00669. asnA. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the asnA gene coding for asparagine synthetase of E. coli K-12."
    Nakamura M., Yamada M., Hirota Y., Sugimoto K., Oka A., Takanami M.
    Nucleic Acids Res. 9:4669-4676(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "The replication origin region of Escherichia coli: nucleotide sequence and functional units."
    Buhk H.-J., Messer W.
    Gene 24:265-279(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication."
    Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.
    Genomics 16:551-561(1993) [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. "Structural and functional properties of the Escherichia coli origin of DNA replication."
    Hirota Y., Yasuda S., Yamada M., Nishimura A., Sugimoto K., Sugisaki H., Oka A., Takanami M.
    Cold Spring Harb. Symp. Quant. Biol. 43:129-138(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-252.
  7. "Overexpression and purification of asparagine synthetase from Escherichia coli."
    Sugiyama A., Kato H., Nishioka T., Oda J.
    Biosci. Biotechnol. Biochem. 56:376-379(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-5.
    Strain: K12.
  8. "A linear pentapeptide is a quorum-sensing factor required for mazEF-mediated cell death in Escherichia coli."
    Kolodkin-Gal I., Hazan R., Gaathon A., Carmeli S., Engelberg-Kulka H.
    Science 318:652-655(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PRODUCTION OF EXTRACELLULAR DEATH FACTOR (EDF), DISRUPTION PHENOTYPE.
  9. "Crystal structure of asparagine synthetase reveals a close evolutionary relationship to class II aminoacyl-tRNA synthetase."
    Nakatsu T., Kato H., Oda J.
    Nat. Struct. Biol. 5:15-19(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    Strain: K12.

Entry informationi

Entry nameiASNA_ECOLI
AccessioniPrimary (citable) accession number: P00963
Secondary accession number(s): Q2M862
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 6, 2016
This is version 149 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, Direct protein sequencing, 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

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 one 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.