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Protein

Asparagine synthetase B [glutamine-hydrolyzing]

Gene

asnB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: 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 ammonia2 Publications
  2. KM=0.53 mM for aspartate (when assaying the ammonia-dependent synthetase reaction)2 Publications
  3. KM=0.85 mM for aspartate (when assaying the glutamine-dependent synthetase reaction)2 Publications
  4. KM=0.26 mM for ATP (when assaying the glutamine-dependent synthetase reaction)2 Publications
  5. KM=0.66 mM for glutamine (when assaying the glutamine-dependent synthetase reaction)2 Publications

    pH dependencei

    Optimum pH is 6.5-8.1 Publication

    Pathwayi: L-asparagine biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes L-asparagine from L-aspartate (L-Gln route).
    Proteins known to be involved in this subpathway in this organism are:
    1. Asparagine synthetase B [glutamine-hydrolyzing] (asnB)
    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 keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei2For GATase activity1
    Binding sitei99Glutamine1
    Binding sitei233ATP; via carbonyl oxygen1
    Binding sitei273ATP; via amide nitrogen and carbonyl oxygen1
    Sitei349Important for beta-aspartyl-AMP intermediate formation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi347 – 348ATP2

    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
    • protein homodimerization activity Source: GO_Central

    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
    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.
    BRENDAi6.3.5.4. 2026.
    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10092. asnB.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: EcoliWiki
    • cytosol Source: EcoCyc
    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi2C → A or S: Loss of glutamine-dependent activity but no effect on ammonia-dependent asparagine synthetase activity. 1 Publication1
    Mutagenesisi30H → A: 4,5-fold decrease in glutamine affinity. 1 Publication1
    Mutagenesisi34D → N or E: Little effect on the kinetic properties. 1 Publication1
    Mutagenesisi81H → A: 5-fold decrease in glutamine affinity. 1 Publication1
    Mutagenesisi105A → H: Little effect on the kinetic properties. 1 Publication1
    Mutagenesisi349E → A or Q: Loss of glutamine- and ammonia-dependent synthetase activity, but still exhibits glutaminase activity. 1 Publication1
    Mutagenesisi349E → 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 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00000569312 – 554Asparagine synthetase B [glutamine-hydrolyzing]Add BLAST553

    Proteomic databases

    EPDiP22106.
    PaxDbiP22106.
    PRIDEiP22106.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Binary interactionsi

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

    GO - Molecular functioni

    Protein-protein interaction databases

    BioGridi4261812. 406 interactors.
    DIPiDIP-9177N.
    IntActiP22106. 7 interactors.
    MINTiMINT-1306603.
    STRINGi511145.b0674.

    Structurei

    Secondary structure

    1554
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi3 – 9Combined sources7
    Helixi14 – 26Combined sources13
    Helixi27 – 31Combined sources5
    Beta strandi35 – 40Combined sources6
    Beta strandi42 – 50Combined sources9
    Turni56 – 58Combined sources3
    Beta strandi61 – 64Combined sources4
    Beta strandi70 – 78Combined sources9
    Helixi81 – 88Combined sources8
    Turni89 – 91Combined sources3
    Helixi99 – 101Combined sources3
    Helixi102 – 110Combined sources9
    Turni111 – 114Combined sources4
    Helixi115 – 117Combined sources3
    Beta strandi120 – 128Combined sources9
    Turni129 – 132Combined sources4
    Beta strandi133 – 138Combined sources6
    Beta strandi147 – 150Combined sources4
    Beta strandi156 – 161Combined sources6
    Helixi162 – 164Combined sources3
    Turni165 – 168Combined sources4
    Beta strandi170 – 174Combined sources5
    Beta strandi179 – 182Combined sources4
    Turni183 – 185Combined sources3
    Beta strandi187 – 190Combined sources4
    Helixi195 – 197Combined sources3
    Helixi199 – 202Combined sources4
    Helixi209 – 223Combined sources15
    Beta strandi230 – 233Combined sources4
    Helixi238 – 250Combined sources13
    Beta strandi269 – 275Combined sources7
    Helixi279 – 291Combined sources13
    Beta strandi294 – 299Combined sources6
    Helixi302 – 316Combined sources15
    Helixi321 – 339Combined sources19
    Beta strandi344 – 346Combined sources3
    Helixi351 – 355Combined sources5
    Helixi359 – 363Combined sources5
    Helixi367 – 380Combined sources14
    Helixi381 – 383Combined sources3
    Helixi385 – 394Combined sources10
    Turni395 – 397Combined sources3
    Beta strandi399 – 401Combined sources3
    Helixi403 – 405Combined sources3
    Helixi407 – 415Combined sources9
    Helixi418 – 420Combined sources3
    Helixi431 – 437Combined sources7
    Helixi438 – 440Combined sources3
    Helixi443 – 446Combined sources4
    Helixi460 – 472Combined sources13
    Helixi475 – 479Combined sources5
    Helixi481 – 484Combined sources4
    Helixi493 – 505Combined sources13
    Helixi509 – 514Combined sources6

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1CT9X-ray2.00A/B/C/D2-554[»]
    ProteinModelPortaliP22106.
    SMRiP22106.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP22106.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini2 – 186Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd BLAST185

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni50 – 54Glutamine binding5
    Regioni75 – 77Glutamine binding3

    Sequence similaritiesi

    Belongs to the asparagine synthetase family.Curated
    Contains 1 glutamine amidotransferase type-2 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Glutamine amidotransferase

    Phylogenomic databases

    eggNOGiENOG4105CAQ. Bacteria.
    COG0367. LUCA.
    HOGENOMiHOG000027493.
    InParanoidiP22106.
    KOiK01953.
    OMAiDWSGIYS.
    PhylomeDBiP22106.

    Family and domain databases

    CDDicd01991. Asn_Synthase_B_C. 1 hit.
    cd00712. AsnB. 1 hit.
    Gene3Di3.40.50.620. 1 hit.
    3.60.20.10. 1 hit.
    InterProiIPR006426. Asn_synth_AEB.
    IPR001962. Asn_synthase.
    IPR033738. AsnB_N.
    IPR017932. GATase_2_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]
    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

            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
    Length:554
    Mass (Da):62,659
    Last modified:January 23, 2007 - v3
    Checksum:i9091B269112C9F5C
    GO

    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.
    PIRiA36616. AJECN.
    RefSeqiNP_415200.1. NC_000913.3.
    WP_000337077.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73768; AAC73768; b0674.
    BAA35317; BAA35317; BAA35317.
    GeneIDi945281.
    KEGGiecj:JW0660.
    eco:b0674.
    PATRICi32116529. VBIEscCol129921_0697.

    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.
    PIRiA36616. AJECN.
    RefSeqiNP_415200.1. NC_000913.3.
    WP_000337077.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1CT9X-ray2.00A/B/C/D2-554[»]
    ProteinModelPortaliP22106.
    SMRiP22106.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4261812. 406 interactors.
    DIPiDIP-9177N.
    IntActiP22106. 7 interactors.
    MINTiMINT-1306603.
    STRINGi511145.b0674.

    Protein family/group databases

    MEROPSiC44.976.

    Proteomic databases

    EPDiP22106.
    PaxDbiP22106.
    PRIDEiP22106.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73768; AAC73768; b0674.
    BAA35317; BAA35317; BAA35317.
    GeneIDi945281.
    KEGGiecj:JW0660.
    eco:b0674.
    PATRICi32116529. VBIEscCol129921_0697.

    Organism-specific databases

    EchoBASEiEB0090.
    EcoGeneiEG10092. asnB.

    Phylogenomic databases

    eggNOGiENOG4105CAQ. Bacteria.
    COG0367. LUCA.
    HOGENOMiHOG000027493.
    InParanoidiP22106.
    KOiK01953.
    OMAiDWSGIYS.
    PhylomeDBiP22106.

    Enzyme and pathway databases

    UniPathwayiUPA00134; UER00195.
    BioCyciEcoCyc:ASNSYNB-MONOMER.
    ECOL316407:JW0660-MONOMER.
    MetaCyc:ASNSYNB-MONOMER.
    BRENDAi6.3.5.4. 2026.

    Miscellaneous databases

    EvolutionaryTraceiP22106.
    PROiP22106.

    Family and domain databases

    CDDicd01991. Asn_Synthase_B_C. 1 hit.
    cd00712. AsnB. 1 hit.
    Gene3Di3.40.50.620. 1 hit.
    3.60.20.10. 1 hit.
    InterProiIPR006426. Asn_synth_AEB.
    IPR001962. Asn_synthase.
    IPR033738. AsnB_N.
    IPR017932. GATase_2_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]
    SUPFAMiSSF56235. SSF56235. 1 hit.
    TIGRFAMsiTIGR01536. asn_synth_AEB. 1 hit.
    PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    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: November 2, 2016
    This is version 146 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

    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.