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P22106

- ASNB_ECOLI

UniProt

P22106 - ASNB_ECOLI

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Protein
Asparagine synthetase B [glutamine-hydrolyzing]
Gene
asnB, b0674, JW0660
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the ATP-dependent conversion of aspartate into asparagine, using glutamine as a source of nitrogen. Can also use ammonia as the nitrogen source in vitro, albeit with lower efficiency. As nucleotide substrates, ATP and dATP are utilized at a similar rate in both the glutamine- and ammonia-dependent reactions, whereas GTP utilization is only 15% that of ATP, and CTP, UTP, ITP and XTP are very poor or not substrates. Also exhibits glutaminase activity.3 Publications

Catalytic activityi

ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate.2 Publications

Enzyme regulationi

Glutamine-dependent asparagine synthesis activity can be inhibited by aspartic acid analogs (such as a sulfinate derivative and (2S,3R)-2-amino-3-methylsuccinate) in vitro; the inhibition is competitive with respect to aspartate.1 Publication

Kineticsi

  1. KM=17 mM for ammonia3 Publications
  2. KM=0.53 mM for aspartate (when assaying the ammonia-dependent synthetase reaction)
  3. KM=0.85 mM for aspartate (when assaying the glutamine-dependent synthetase reaction)
  4. KM=0.26 mM for ATP (when assaying the glutamine-dependent synthetase reaction)
  5. KM=0.66 mM for glutamine (when assaying the glutamine-dependent synthetase reaction)

pH dependencei

Optimum pH is 6.5-8.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei2 – 21For GATase activity
Binding sitei99 – 991Glutamine
Binding sitei233 – 2331ATP; via carbonyl oxygen
Binding sitei273 – 2731ATP; via amide nitrogen and carbonyl oxygen
Sitei349 – 3491Important for beta-aspartyl-AMP intermediate formation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi347 – 3482ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. amino acid binding Source: UniProtKB
  3. asparagine synthase (glutamine-hydrolyzing) activity Source: UniProtKB
  4. aspartate-ammonia ligase activity Source: UniProtKB
  5. identical protein binding Source: IntAct

GO - Biological processi

  1. L-asparagine biosynthetic process Source: UniProtKB-UniPathway
  2. asparagine biosynthetic process Source: UniProtKB
  3. cellular amino acid biosynthetic process Source: EcoliWiki
  4. cellular amino acid catabolic process Source: EcoliWiki
  5. glutamine metabolic process Source: EcoliWiki
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:ASNSYNB-MONOMER.
ECOL316407:JW0660-MONOMER.
MetaCyc:ASNSYNB-MONOMER.
UniPathwayiUPA00134; UER00195.

Protein family/group databases

MEROPSiC44.976.

Names & Taxonomyi

Protein namesi
Recommended name:
Asparagine synthetase B [glutamine-hydrolyzing] (EC:6.3.5.4)
Short name:
AS-B
Gene namesi
Name:asnB
Ordered Locus Names:b0674, JW0660
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10092. asnB.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: EcoliWiki
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 21C → A or S: Loss of glutamine-dependent activity but no effect on ammonia-dependent asparagine synthetase activity. 1 Publication
Mutagenesisi30 – 301H → A: 4,5-fold decrease in glutamine affinity. 1 Publication
Mutagenesisi34 – 341D → N or E: Little effect on the kinetic properties. 1 Publication
Mutagenesisi81 – 811H → A: 5-fold decrease in glutamine affinity. 1 Publication
Mutagenesisi105 – 1051A → H: Little effect on the kinetic properties. 1 Publication
Mutagenesisi349 – 3491E → A or Q: Loss of glutamine- and ammonia-dependent synthetase activity, but still exhibits glutaminase activity. 1 Publication
Mutagenesisi349 – 3491E → D: 5-fold increase in affinity for asparate when assaying both the glutamine- and ammonia-dependent synthetase reactions, and 2-fold decrease in kcat for these reactions. Modifies the product glutamate/asparagine stoichiometry. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 554553Asparagine synthetase B [glutamine-hydrolyzing]
PRO_0000056931Add
BLAST

Proteomic databases

PaxDbiP22106.
PRIDEiP22106.

Expressioni

Gene expression databases

GenevestigatoriP22106.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-549123,EBI-549123

Protein-protein interaction databases

DIPiDIP-9177N.
IntActiP22106. 7 interactions.
MINTiMINT-1306603.
STRINGi511145.b0674.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 97
Helixi14 – 2613
Helixi27 – 315
Beta strandi35 – 406
Beta strandi42 – 509
Turni56 – 583
Beta strandi61 – 644
Beta strandi70 – 789
Helixi81 – 888
Turni89 – 913
Helixi99 – 1013
Helixi102 – 1109
Turni111 – 1144
Helixi115 – 1173
Beta strandi120 – 1289
Turni129 – 1324
Beta strandi133 – 1386
Beta strandi147 – 1504
Beta strandi156 – 1616
Helixi162 – 1643
Turni165 – 1684
Beta strandi170 – 1745
Beta strandi179 – 1824
Turni183 – 1853
Beta strandi187 – 1904
Helixi195 – 1973
Helixi199 – 2024
Helixi209 – 22315
Beta strandi230 – 2334
Helixi238 – 25013
Beta strandi269 – 2757
Helixi279 – 29113
Beta strandi294 – 2996
Helixi302 – 31615
Helixi321 – 33919
Beta strandi344 – 3463
Helixi351 – 3555
Helixi359 – 3635
Helixi367 – 38014
Helixi381 – 3833
Helixi385 – 39410
Turni395 – 3973
Beta strandi399 – 4013
Helixi403 – 4053
Helixi407 – 4159
Helixi418 – 4203
Helixi431 – 4377
Helixi438 – 4403
Helixi443 – 4464
Helixi460 – 47213
Helixi475 – 4795
Helixi481 – 4844
Helixi493 – 50513
Helixi509 – 5146

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CT9X-ray2.00A/B/C/D2-554[»]
ProteinModelPortaliP22106.
SMRiP22106. Positions 3-517.

Miscellaneous databases

EvolutionaryTraceiP22106.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 186185Glutamine amidotransferase type-2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni50 – 545Glutamine binding
Regioni75 – 773Glutamine binding

Sequence similaritiesi

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiCOG0367.
HOGENOMiHOG000027493.
KOiK01953.
OMAiWSGIYSS.
OrthoDBiEOG6J48H7.
PhylomeDBiP22106.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
3.60.20.10. 1 hit.
InterProiIPR006426. Asn_synth_AEB.
IPR001962. Asn_synthase.
IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR029055. Ntn_hydrolases_N.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF00733. Asn_synthase. 1 hit.
PF13537. GATase_7. 1 hit.
[Graphical view]
PIRSFiPIRSF001589. Asn_synthetase_glu-h. 1 hit.
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR01536. asn_synth_AEB. 1 hit.
PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P22106-1 [UniParc]FASTAAdd to Basket

« Hide

MCSIFGVFDI KTDAVELRKK ALELSRLMRH RGPDWSGIYA SDNAILAHER    50
LSIVDVNAGA QPLYNQQKTH VLAVNGEIYN HQALRAEYGD RYQFQTGSDC 100
EVILALYQEK GPEFLDDLQG MFAFALYDSE KDAYLIGRDH LGIIPLYMGY 150
DEHGQLYVAS EMKALVPVCR TIKEFPAGSY LWSQDGEIRS YYHRDWFDYD 200
AVKDNVTDKN ELRQALEDSV KSHLMSDVPY GVLLSGGLDS SIISAITKKY 250
AARRVEDQER SEAWWPQLHS FAVGLPGSPD LKAAQEVANH LGTVHHEIHF 300
TVQEGLDAIR DVIYHIETYD VTTIRASTPM YLMSRKIKAM GIKMVLSGEG 350
SDEVFGGYLY FHKAPNAKEL HEETVRKLLA LHMYDCARAN KAMSAWGVEA 400
RVPFLDKKFL DVAMRINPQD KMCGNGKMEK HILRECFEAY LPASVAWRQK 450
EQFSDGVGYS WIDTLKEVAA QQVSDQQLET ARFRFPYNTP TSKEAYLYRE 500
IFEELFPLPS AAECVPGGPS VACSSAKAIE WDEAFKKMDD PSGRAVGVHQ 550
SAYK 554
Length:554
Mass (Da):62,659
Last modified:January 23, 2007 - v3
Checksum:i9091B269112C9F5C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05554 Genomic DNA. Translation: AAA23498.1.
U00096 Genomic DNA. Translation: AAC73768.1.
AP009048 Genomic DNA. Translation: BAA35317.1.
PIRiA36616. AJECN.
RefSeqiNP_415200.1. NC_000913.3.
YP_488954.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73768; AAC73768; b0674.
BAA35317; BAA35317; BAA35317.
GeneIDi12932818.
945281.
KEGGiecj:Y75_p0653.
eco:b0674.
PATRICi32116529. VBIEscCol129921_0697.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05554 Genomic DNA. Translation: AAA23498.1 .
U00096 Genomic DNA. Translation: AAC73768.1 .
AP009048 Genomic DNA. Translation: BAA35317.1 .
PIRi A36616. AJECN.
RefSeqi NP_415200.1. NC_000913.3.
YP_488954.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CT9 X-ray 2.00 A/B/C/D 2-554 [» ]
ProteinModelPortali P22106.
SMRi P22106. Positions 3-517.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-9177N.
IntActi P22106. 7 interactions.
MINTi MINT-1306603.
STRINGi 511145.b0674.

Chemistry

DrugBanki DB00131. Adenosine monophosphate.

Protein family/group databases

MEROPSi C44.976.

Proteomic databases

PaxDbi P22106.
PRIDEi P22106.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73768 ; AAC73768 ; b0674 .
BAA35317 ; BAA35317 ; BAA35317 .
GeneIDi 12932818.
945281.
KEGGi ecj:Y75_p0653.
eco:b0674.
PATRICi 32116529. VBIEscCol129921_0697.

Organism-specific databases

EchoBASEi EB0090.
EcoGenei EG10092. asnB.

Phylogenomic databases

eggNOGi COG0367.
HOGENOMi HOG000027493.
KOi K01953.
OMAi WSGIYSS.
OrthoDBi EOG6J48H7.
PhylomeDBi P22106.

Enzyme and pathway databases

UniPathwayi UPA00134 ; UER00195 .
BioCyci EcoCyc:ASNSYNB-MONOMER.
ECOL316407:JW0660-MONOMER.
MetaCyc:ASNSYNB-MONOMER.

Miscellaneous databases

EvolutionaryTracei P22106.
PROi P22106.

Gene expression databases

Genevestigatori P22106.

Family and domain databases

Gene3Di 3.40.50.620. 1 hit.
3.60.20.10. 1 hit.
InterProi IPR006426. Asn_synth_AEB.
IPR001962. Asn_synthase.
IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR029055. Ntn_hydrolases_N.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view ]
Pfami PF00733. Asn_synthase. 1 hit.
PF13537. GATase_7. 1 hit.
[Graphical view ]
PIRSFi PIRSF001589. Asn_synthetase_glu-h. 1 hit.
SUPFAMi SSF56235. SSF56235. 1 hit.
TIGRFAMsi TIGR01536. asn_synth_AEB. 1 hit.
PROSITEi PS51278. GATASE_TYPE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of Escherichia coli asnB and deduced amino acid sequence of asparagine synthetase B."
    Scofield M.A., Lewis W.S., Schuster S.M.
    J. Biol. Chem. 265:12895-12902(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "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.
  5. "Glutamine-dependent nitrogen transfer in Escherichia coli asparagine synthetase B. Searching for the catalytic triad."
    Boehlein S.K., Richards N.G., Schuster S.M.
    J. Biol. Chem. 269:7450-7457(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF N-TERMINUS, CLEAVAGE OF INITIATOR METHIONINE, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-2; HIS-30; ASP-34; HIS-81 AND ALA-105.
    Strain: K12.
  6. "Genetic and biomedical studies demonstrating a second gene coding for asparagine synthetase in Escherichia coli."
    Humbert R., Simoni R.D.
    J. Bacteriol. 142:212-220(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ASPARAGINE BIOSYNTHESIS.
    Strain: K12.
  7. "Mapping the aspartic acid binding site of Escherichia coli asparagine synthetase B using substrate analogs."
    Parr I.B., Boehlein S.K., Dribben A.B., Schuster S.M., Richards N.G.
    J. Med. Chem. 39:2367-2378(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, INHIBITION STUDIES.
  8. "Revisiting the steady state kinetic mechanism of glutamine-dependent asparagine synthetase from Escherichia coli."
    Tesson A.R., Soper T.S., Ciustea M., Richards N.G.
    Arch. Biochem. Biophys. 413:23-31(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: KINETIC PARAMETERS.
    Strain: K12.
  9. "A conserved glutamate controls the commitment to acyl-adenylate formation in asparagine synthetase."
    Meyer M.E., Gutierrez J.A., Raushel F.M., Richards N.G.
    Biochemistry 49:9391-9401(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-349, KINETIC MODEL.
    Strain: K12.
  10. "Three-dimensional structure of Escherichia coli asparagine synthetase B: a short journey from substrate to product."
    Larsen T.M., Boehlein S.K., Schuster S.M., Richards N.G.J., Thoden J.B., Holden H.M., Rayment I.
    Biochemistry 38:16146-16157(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-554 OF MUTANT ALA-2 IN COMPLEX WITH AMP AND L-GLUTAMINE, SUBUNIT.
    Strain: K12.

Entry informationi

Entry nameiASNB_ECOLI
AccessioniPrimary (citable) accession number: P22106
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 129 of the entry and version 3 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

External Data

Dasty 3

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