UniProtKB - P22106 (ASNB_ECOLI)
Asparagine synthetase B [glutamine-hydrolyzing]
asnB
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 PublicationsCatalytic activityi
- ATP + H2O + L-aspartate + L-glutamine = AMP + diphosphate + H+ + L-asparagine + L-glutamate2 PublicationsEC:6.3.5.42 Publications
Activity regulationi
Kineticsi
- KM=17 mM for ammonia2 Publications
- KM=0.53 mM for aspartate (when assaying the ammonia-dependent synthetase reaction)2 Publications
- KM=0.85 mM for aspartate (when assaying the glutamine-dependent synthetase reaction)2 Publications
- KM=0.26 mM for ATP (when assaying the glutamine-dependent synthetase reaction)2 Publications
- KM=0.66 mM for glutamine (when assaying the glutamine-dependent synthetase reaction)2 Publications
pH dependencei
: L-asparagine biosynthesis Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes L-asparagine from L-aspartate (L-Gln route). 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 (L-Gln route), the pathway L-asparagine biosynthesis and in Amino-acid biosynthesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 2 | For GATase activity | 1 | |
Binding sitei | 99 | Glutamine | 1 | |
Binding sitei | 233 | ATP; via carbonyl oxygen | 1 | |
Binding sitei | 273 | ATP; via amide nitrogen and carbonyl oxygen | 1 | |
Sitei | 349 | Important for beta-aspartyl-AMP intermediate formation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 347 – 348 | ATP | 2 |
GO - Molecular functioni
- amino acid binding Source: UniProtKB
- asparagine synthase (glutamine-hydrolyzing) activity Source: UniProtKB
- aspartate-ammonia ligase activity Source: UniProtKB
- ATP binding Source: UniProtKB
- identical protein binding Source: IntAct
GO - Biological processi
- asparagine biosynthetic process Source: UniProtKB
- cellular amino acid biosynthetic process Source: EcoliWiki
- cellular amino acid catabolic process Source: EcoliWiki
- glutamine metabolic process Source: EcoliWiki
- L-asparagine biosynthetic process Source: UniProtKB-UniPathway
Keywordsi
Molecular function | Ligase |
Biological process | Amino-acid biosynthesis, Asparagine biosynthesis |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:ASNSYNB-MONOMER |
BRENDAi | 6.3.5.4, 2026 |
UniPathwayi | UPA00134;UER00195 |
Protein family/group databases
MEROPSi | C44.976 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:asnB Ordered Locus Names:b0674, JW0660 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 2 | C → A or S: Loss of glutamine-dependent activity but no effect on ammonia-dependent asparagine synthetase activity. 1 Publication | 1 | |
Mutagenesisi | 30 | H → A: 4,5-fold decrease in glutamine affinity. 1 Publication | 1 | |
Mutagenesisi | 34 | D → N or E: Little effect on the kinetic properties. 1 Publication | 1 | |
Mutagenesisi | 81 | H → A: 5-fold decrease in glutamine affinity. 1 Publication | 1 | |
Mutagenesisi | 105 | A → H: Little effect on the kinetic properties. 1 Publication | 1 | |
Mutagenesisi | 349 | E → A or Q: Loss of glutamine- and ammonia-dependent synthetase activity, but still exhibits glutaminase activity. 1 Publication | 1 | |
Mutagenesisi | 349 | E → D: 5-fold increase in affinity for aspartate 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 | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed1 Publication | |||
ChainiPRO_0000056931 | 2 – 554 | Asparagine synthetase B [glutamine-hydrolyzing]Add BLAST | 553 |
Proteomic databases
jPOSTi | P22106 |
PaxDbi | P22106 |
PRIDEi | P22106 |
Interactioni
Subunit structurei
Homodimer.
1 PublicationBinary interactionsi
P22106
With | #Exp. | IntAct |
---|---|---|
itself | 3 | EBI-549123,EBI-549123 |
GO - Molecular functioni
- identical protein binding Source: IntAct
Protein-protein interaction databases
BioGRIDi | 4261812, 416 interactors 849659, 1 interactor |
DIPi | DIP-9177N |
IntActi | P22106, 7 interactors |
STRINGi | 511145.b0674 |
Structurei
Secondary structure
3D structure databases
SMRi | P22106 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P22106 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 2 – 186 | Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd BLAST | 185 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 50 – 54 | Glutamine binding | 5 | |
Regioni | 75 – 77 | Glutamine binding | 3 |
Sequence similaritiesi
Keywords - Domaini
Glutamine amidotransferasePhylogenomic databases
eggNOGi | COG0367, Bacteria |
HOGENOMi | CLU_014658_2_2_6 |
InParanoidi | P22106 |
PhylomeDBi | P22106 |
Family and domain databases
CDDi | cd01991, Asn_Synthase_B_C, 1 hit cd00712, AsnB, 1 hit |
Gene3Di | 3.40.50.620, 1 hit 3.60.20.10, 1 hit |
InterProi | View protein in InterPro IPR006426, Asn_synth_AEB IPR001962, Asn_synthase IPR033738, AsnB_N IPR017932, GATase_2_dom IPR029055, Ntn_hydrolases_N IPR014729, Rossmann-like_a/b/a_fold |
Pfami | View protein in Pfam PF00733, Asn_synthase, 1 hit PF13537, GATase_7, 1 hit |
PIRSFi | PIRSF001589, Asn_synthetase_glu-h, 1 hit |
SUPFAMi | SSF56235, SSF56235, 1 hit |
TIGRFAMsi | TIGR01536, asn_synth_AEB, 1 hit |
PROSITEi | View protein in PROSITE PS51278, GATASE_TYPE_2, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MCSIFGVFDI KTDAVELRKK ALELSRLMRH RGPDWSGIYA SDNAILAHER
60 70 80 90 100
LSIVDVNAGA QPLYNQQKTH VLAVNGEIYN HQALRAEYGD RYQFQTGSDC
110 120 130 140 150
EVILALYQEK GPEFLDDLQG MFAFALYDSE KDAYLIGRDH LGIIPLYMGY
160 170 180 190 200
DEHGQLYVAS EMKALVPVCR TIKEFPAGSY LWSQDGEIRS YYHRDWFDYD
210 220 230 240 250
AVKDNVTDKN ELRQALEDSV KSHLMSDVPY GVLLSGGLDS SIISAITKKY
260 270 280 290 300
AARRVEDQER SEAWWPQLHS FAVGLPGSPD LKAAQEVANH LGTVHHEIHF
310 320 330 340 350
TVQEGLDAIR DVIYHIETYD VTTIRASTPM YLMSRKIKAM GIKMVLSGEG
360 370 380 390 400
SDEVFGGYLY FHKAPNAKEL HEETVRKLLA LHMYDCARAN KAMSAWGVEA
410 420 430 440 450
RVPFLDKKFL DVAMRINPQD KMCGNGKMEK HILRECFEAY LPASVAWRQK
460 470 480 490 500
EQFSDGVGYS WIDTLKEVAA QQVSDQQLET ARFRFPYNTP TSKEAYLYRE
510 520 530 540 550
IFEELFPLPS AAECVPGGPS VACSSAKAIE WDEAFKKMDD PSGRAVGVHQ
SAYK
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi 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 WP_000337077.1, NZ_SSZK01000045.1 |
Genome annotation databases
EnsemblBacteriai | AAC73768; AAC73768; b0674 BAA35317; BAA35317; BAA35317 |
GeneIDi | 60901229 945281 |
KEGGi | ecj:JW0660 eco:b0674 |
PATRICi | fig|1411691.4.peg.1605 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi 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 WP_000337077.1, NZ_SSZK01000045.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1CT9 | X-ray | 2.00 | A/B/C/D | 2-554 | [»] | |
SMRi | P22106 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4261812, 416 interactors 849659, 1 interactor |
DIPi | DIP-9177N |
IntActi | P22106, 7 interactors |
STRINGi | 511145.b0674 |
Protein family/group databases
MEROPSi | C44.976 |
Proteomic databases
jPOSTi | P22106 |
PaxDbi | P22106 |
PRIDEi | P22106 |
Genome annotation databases
EnsemblBacteriai | AAC73768; AAC73768; b0674 BAA35317; BAA35317; BAA35317 |
GeneIDi | 60901229 945281 |
KEGGi | ecj:JW0660 eco:b0674 |
PATRICi | fig|1411691.4.peg.1605 |
Organism-specific databases
EchoBASEi | EB0090 |
Phylogenomic databases
eggNOGi | COG0367, Bacteria |
HOGENOMi | CLU_014658_2_2_6 |
InParanoidi | P22106 |
PhylomeDBi | P22106 |
Enzyme and pathway databases
UniPathwayi | UPA00134;UER00195 |
BioCyci | EcoCyc:ASNSYNB-MONOMER |
BRENDAi | 6.3.5.4, 2026 |
Miscellaneous databases
EvolutionaryTracei | P22106 |
PROi | PR:P22106 |
Family and domain databases
CDDi | cd01991, Asn_Synthase_B_C, 1 hit cd00712, AsnB, 1 hit |
Gene3Di | 3.40.50.620, 1 hit 3.60.20.10, 1 hit |
InterProi | View protein in InterPro IPR006426, Asn_synth_AEB IPR001962, Asn_synthase IPR033738, AsnB_N IPR017932, GATase_2_dom IPR029055, Ntn_hydrolases_N IPR014729, Rossmann-like_a/b/a_fold |
Pfami | View protein in Pfam PF00733, Asn_synthase, 1 hit PF13537, GATase_7, 1 hit |
PIRSFi | PIRSF001589, Asn_synthetase_glu-h, 1 hit |
SUPFAMi | SSF56235, SSF56235, 1 hit |
TIGRFAMsi | TIGR01536, asn_synth_AEB, 1 hit |
PROSITEi | View protein in PROSITE PS51278, GATASE_TYPE_2, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | ASNB_ECOLI | |
Accessioni | P22106Primary (citable) accession number: P22106 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 1, 1991 |
Last sequence update: | January 23, 2007 | |
Last modified: | February 23, 2022 | |
This is version 176 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families