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Protein

Glutamate-ammonia-ligase adenylyltransferase

Gene

glnE

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

Functioni

Adenylation and deadenylation of glutamate--ammonia ligase.1 Publication

Catalytic activityi

ATP + [L-glutamate:ammonia ligase (ADP-forming)]-L-tyrosine = diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-O(4)-(5'-adenylyl)-L-tyrosine.1 Publication

Cofactori

Mg2+1 Publication

Kineticsi

  1. KM=5 µM for [L-glutamate:ammonia ligase (ADP-forming)]1 Publication
  2. KM=150 µM for ATP1 Publication

    pH dependencei

    Optimum pH is 7.6.1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Nucleotidyltransferase, Transferase

    Keywords - Ligandi

    ATP-binding, Magnesium, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:GLNE-MONOMER.
    ECOL316407:JW3025-MONOMER.
    MetaCyc:GLNE-MONOMER.
    BRENDAi2.7.7.42. 2026.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate-ammonia-ligase adenylyltransferase (EC:2.7.7.421 Publication)
    Alternative name(s):
    Glutamine-synthetase adenylyltransferase
    Short name:
    ATase
    [Glutamate--ammonia-ligase] adenylyltransferase
    Gene namesi
    Name:glnE
    Ordered Locus Names:b3053, JW3025
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11602. glnE.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc
    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 946946Glutamate-ammonia-ligase adenylyltransferasePRO_0000209244Add
    BLAST

    Proteomic databases

    PaxDbiP30870.
    PRIDEiP30870.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi4261515. 4 interactions.
    DIPiDIP-9780N.
    IntActiP30870. 2 interactions.
    STRINGi511145.b3053.

    Structurei

    Secondary structure

    1
    946
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 1611Combined sources
    Helixi25 – 273Combined sources
    Helixi30 – 389Combined sources
    Helixi40 – 489Combined sources
    Helixi51 – 588Combined sources
    Helixi63 – 686Combined sources
    Helixi69 – 768Combined sources
    Turni77 – 793Combined sources
    Helixi83 – 10624Combined sources
    Helixi112 – 14130Combined sources
    Beta strandi156 – 1594Combined sources
    Helixi161 – 1644Combined sources
    Beta strandi174 – 1807Combined sources
    Helixi195 – 21117Combined sources
    Helixi230 – 2323Combined sources
    Beta strandi235 – 2384Combined sources
    Helixi239 – 24911Combined sources
    Helixi252 – 2587Combined sources
    Beta strandi262 – 2654Combined sources
    Helixi270 – 28314Combined sources
    Helixi290 – 31021Combined sources
    Turni316 – 3183Combined sources
    Helixi323 – 33715Combined sources
    Turni338 – 3403Combined sources
    Helixi342 – 3443Combined sources
    Helixi349 – 35810Combined sources
    Helixi364 – 38522Combined sources
    Turni386 – 3894Combined sources
    Helixi399 – 40810Combined sources
    Helixi414 – 43421Combined sources
    Helixi450 – 4578Combined sources
    Helixi459 – 4613Combined sources
    Helixi467 – 4693Combined sources
    Helixi474 – 49320Combined sources
    Helixi498 – 51518Combined sources
    Helixi521 – 53515Combined sources
    Helixi539 – 5479Combined sources
    Helixi549 – 56113Combined sources
    Helixi563 – 5719Combined sources
    Helixi573 – 5808Combined sources
    Helixi582 – 5854Combined sources
    Helixi594 – 6018Combined sources
    Turni602 – 6043Combined sources
    Helixi610 – 63324Combined sources
    Helixi639 – 6413Combined sources
    Helixi642 – 66928Combined sources
    Helixi673 – 6753Combined sources
    Beta strandi682 – 6876Combined sources
    Helixi689 – 6924Combined sources
    Beta strandi702 – 7087Combined sources
    Beta strandi715 – 7206Combined sources
    Helixi724 – 74017Combined sources
    Helixi759 – 7613Combined sources
    Beta strandi764 – 7674Combined sources
    Helixi768 – 77710Combined sources
    Helixi781 – 7888Combined sources
    Beta strandi791 – 7944Combined sources
    Helixi797 – 81115Combined sources
    Helixi817 – 83418Combined sources
    Beta strandi842 – 8443Combined sources
    Turni845 – 8473Combined sources
    Helixi852 – 86615Combined sources
    Turni867 – 8693Combined sources
    Helixi871 – 8744Combined sources
    Helixi879 – 88810Combined sources
    Helixi894 – 91623Combined sources
    Beta strandi921 – 9244Combined sources
    Turni925 – 9284Combined sources
    Helixi929 – 94315Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1V4AX-ray2.00A1-440[»]
    3K7DX-ray2.40A/B449-946[»]
    ProteinModelPortaliP30870.
    SMRiP30870. Positions 1-437, 449-945.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP30870.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni91 – 302212GlnE 1Add
    BLAST
    Regioni609 – 830222GlnE 2Add
    BLAST

    Sequence similaritiesi

    Belongs to the GlnE family.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiENOG4105CE6. Bacteria.
    COG1391. LUCA.
    HOGENOMiHOG000256491.
    InParanoidiP30870.
    KOiK00982.
    OMAiTWERIAW.
    OrthoDBiEOG651SRZ.
    PhylomeDBiP30870.

    Family and domain databases

    HAMAPiMF_00802. GlnE.
    InterProiIPR023057. GlnE.
    IPR005190. GlnE_rpt_dom.
    IPR013546. PII_UdlTrfase/GS_AdlTrfase.
    [Graphical view]
    PfamiPF08335. GlnD_UR_UTase. 2 hits.
    PF03710. GlnE. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P30870-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKPLSSPLQQ YWQTVVERLP EPLAEESLSA QAKSVLTFSD FVQDSVIAHP
    60 70 80 90 100
    EWLTELESQP PQADEWQHYA AWLQEALCNV SDEAGLMREL RLFRRRIMVR
    110 120 130 140 150
    IAWAQTLALV TEESILQQLS YLAETLIVAA RDWLYDACCR EWGTPCNAQG
    160 170 180 190 200
    EAQPLLILGM GKLGGGELNF SSDIDLIFAW PEHGCTQGGR RELDNAQFFT
    210 220 230 240 250
    RMGQRLIKVL DQPTQDGFVY RVDMRLRPFG ESGPLVLSFA ALEDYYQEQG
    260 270 280 290 300
    RDWERYAMVK ARIMGDSEGV YANELRAMLR PFVFRRYIDF SVIQSLRNMK
    310 320 330 340 350
    GMIAREVRRR GLTDNIKLGA GGIREIEFIV QVFQLIRGGR EPSLQSRSLL
    360 370 380 390 400
    PTLSAIAELH LLSENDAEQL RVAYLFLRRL ENLLQSINDE QTQTLPSDEL
    410 420 430 440 450
    NRARLAWAMD FADWPQLTGA LTAHMTNVRR VFNELIGDDE SETQEESLSE
    460 470 480 490 500
    QWRELWQDAL QEDDTTPVLA HLSEDDRKQV LTLIADFRKE LDKRTIGPRG
    510 520 530 540 550
    RQVLDHLMPH LLSDVCARED AAVTLSRITA LLVGIVTRTT YLELLSEFPA
    560 570 580 590 600
    ALKHLISLCA ASPMIASQLA RYPLLLDELL DPNTLYQPTA TDAYRDELRQ
    610 620 630 640 650
    YLLRVPEDDE EQQLEALRQF KQAQLLRIAA ADIAGTLPVM KVSDHLTWLA
    660 670 680 690 700
    EAMIDAVVQQ AWVQMVARYG KPNHLNEREG RGFAVVGYGK LGGWELGYSS
    710 720 730 740 750
    DLDLIFLHDC PMDAMTDGER EIDGRQFYLR LAQRIMHLFS TRTSSGILYE
    760 770 780 790 800
    VDARLRPSGA AGMLVTSAEA FADYQKNEAW TWEHQALVRA RVVYGDPQLT
    810 820 830 840 850
    AHFDAVRREI MTLPREGKTL QTEVREMREK MRAHLGNKHR DRFDIKADEG
    860 870 880 890 900
    GITDIEFITQ YLVLRYAHEK PKLTRWSDNV RILELLAQND IMEEQEAMAL
    910 920 930 940
    TRAYTTLRDE LHHLALQELP GHVSEDCFTA ERELVRASWQ KWLVEE
    Length:946
    Mass (Da):108,418
    Last modified:November 1, 1997 - v2
    Checksum:i6FD2D7BDC619DB83
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti524 – 5241Missing in CAA79892 (PubMed:8412694).Curated
    Sequence conflicti624 – 6252QL → PV in CAA79892 (PubMed:8412694).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z21844 Genomic DNA. Translation: CAA79892.1.
    U00096 Genomic DNA. Translation: AAC76089.1.
    AP009048 Genomic DNA. Translation: BAE77104.1.
    PIRiC65093.
    RefSeqiNP_417525.1. NC_000913.3.
    WP_001301081.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76089; AAC76089; b3053.
    BAE77104; BAE77104; BAE77104.
    GeneIDi947552.
    KEGGiecj:JW3025.
    eco:b3053.
    PATRICi32121518. VBIEscCol129921_3146.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z21844 Genomic DNA. Translation: CAA79892.1.
    U00096 Genomic DNA. Translation: AAC76089.1.
    AP009048 Genomic DNA. Translation: BAE77104.1.
    PIRiC65093.
    RefSeqiNP_417525.1. NC_000913.3.
    WP_001301081.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1V4AX-ray2.00A1-440[»]
    3K7DX-ray2.40A/B449-946[»]
    ProteinModelPortaliP30870.
    SMRiP30870. Positions 1-437, 449-945.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4261515. 4 interactions.
    DIPiDIP-9780N.
    IntActiP30870. 2 interactions.
    STRINGi511145.b3053.

    Proteomic databases

    PaxDbiP30870.
    PRIDEiP30870.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76089; AAC76089; b3053.
    BAE77104; BAE77104; BAE77104.
    GeneIDi947552.
    KEGGiecj:JW3025.
    eco:b3053.
    PATRICi32121518. VBIEscCol129921_3146.

    Organism-specific databases

    EchoBASEiEB1559.
    EcoGeneiEG11602. glnE.

    Phylogenomic databases

    eggNOGiENOG4105CE6. Bacteria.
    COG1391. LUCA.
    HOGENOMiHOG000256491.
    InParanoidiP30870.
    KOiK00982.
    OMAiTWERIAW.
    OrthoDBiEOG651SRZ.
    PhylomeDBiP30870.

    Enzyme and pathway databases

    BioCyciEcoCyc:GLNE-MONOMER.
    ECOL316407:JW3025-MONOMER.
    MetaCyc:GLNE-MONOMER.
    BRENDAi2.7.7.42. 2026.

    Miscellaneous databases

    EvolutionaryTraceiP30870.
    PROiP30870.

    Family and domain databases

    HAMAPiMF_00802. GlnE.
    InterProiIPR023057. GlnE.
    IPR005190. GlnE_rpt_dom.
    IPR013546. PII_UdlTrfase/GS_AdlTrfase.
    [Graphical view]
    PfamiPF08335. GlnD_UR_UTase. 2 hits.
    PF03710. GlnE. 2 hits.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "The genes of the glutamine synthetase adenylylation cascade are not regulated by nitrogen in Escherichia coli."
      van Heeswijk W.C., Rabenberg M., Westerhoff H.V., Kahn D.D.
      Mol. Microbiol. 9:443-458(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
      Strain: K12 / CS520.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "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.
    4. "ATP: glutamine synthetase adenylyltransferase from Escherichia coli B. Purification and properties."
      Ebner E., Wolf D., Gancedo C., Elsaesser S., Holzer H.
      Eur. J. Biochem. 14:535-544(1970) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY.
    5. "Structure of the N-terminal domain of Escherichia coli glutamine synthetase adenylyltransferase."
      Xu Y., Zhang R., Joachimiak A., Carr P.D., Huber T., Vasudevan S.G., Ollis D.L.
      Structure 12:861-869(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-440.

    Entry informationi

    Entry nameiGLNE_ECOLI
    AccessioniPrimary (citable) accession number: P30870
    Secondary accession number(s): P78107, Q2M9F2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: November 1, 1997
    Last modified: July 6, 2016
    This is version 121 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. 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.