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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

  • 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
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
ChainiPRO_00001958731 – 330Aspartate--ammonia ligaseAdd BLAST330

Proteomic databases

EPDiP00963.
PaxDbiP00963.
PRIDEiP00963.

2D gel databases

SWISS-2DPAGEP00963.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

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

Structurei

Secondary structure

1330
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 27Combined sources23
Beta strandi29 – 31Combined sources3
Beta strandi36 – 39Combined sources4
Turni48 – 51Combined sources4
Beta strandi60 – 62Combined sources3
Beta strandi67 – 69Combined sources3
Helixi76 – 83Combined sources8
Beta strandi91 – 99Combined sources9
Beta strandi112 – 122Combined sources11
Helixi130 – 154Combined sources25
Beta strandi166 – 169Combined sources4
Helixi170 – 176Combined sources7
Beta strandi177 – 180Combined sources4
Helixi182 – 193Combined sources12
Beta strandi194 – 199Combined sources6
Beta strandi202 – 204Combined sources3
Beta strandi206 – 208Combined sources3
Beta strandi210 – 212Combined sources3
Turni216 – 218Combined sources3
Beta strandi222 – 224Combined sources3
Beta strandi228 – 230Combined sources3
Beta strandi232 – 240Combined sources9
Turni241 – 244Combined sources4
Beta strandi245 – 255Combined sources11
Helixi258 – 268Combined sources11
Helixi273 – 275Combined sources3
Helixi277 – 283Combined sources7
Beta strandi290 – 296Combined sources7
Helixi297 – 305Combined sources9
Helixi310 – 312Combined sources3
Helixi320 – 325Combined sources6

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP00963.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

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

Family and domain databases

CDDicd00645. AsnA. 1 hit.
HAMAPiMF_00555. AsnA. 1 hit.
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.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
11ASX-ray2.50A/B1-330[»]
12ASX-ray2.20A/B1-330[»]
ProteinModelPortaliP00963.
SMRiP00963.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263263. 101 interactors.
DIPiDIP-9176N.
IntActiP00963. 5 interactors.
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.
PATRICi32122987. VBIEscCol129921_3869.

Organism-specific databases

EchoBASEiEB0089.
EcoGeneiEG10091. asnA.

Phylogenomic databases

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

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP00963.
PROiP00963.

Family and domain databases

CDDicd00645. AsnA. 1 hit.
HAMAPiMF_00555. AsnA. 1 hit.
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...

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: November 30, 2016
This is version 153 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.