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Protein

Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme

Gene

glnE

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

Functioni

Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia (PubMed:8412694). When cellular nitrogen levels are high, the C-terminal adenylyl transferase inactivates GlnA by covalent transfer of an adenylyl group from ATP to 'Tyr-398' of GlnA, thus reducing its activity (PubMed:4920894, PubMed:9312015). Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity (PubMed:4893578, PubMed:4920873, PubMed:4934180, PubMed:9312015, PubMed:14766310). The regulatory region of GlnE binds the signal transduction protein PII (GlnB) which indicates the nitrogen status of the cell (PubMed:8412694).8 Publications

Catalytic activityi

[Glutamine synthetase]-O4-(5'-adenylyl)-L-tyrosine + phosphate = [glutamine synthetase]-L-tyrosine + ADP.4 Publications1 Publication
ATP + [glutamine synthetase]-L-tyrosine = diphosphate + [glutamine synthetase]-O4-(5'-adenylyl)-L-tyrosine.1 Publication1 Publication

Cofactori

Mg2+4 PublicationsNote: Can also use Mn2+.4 Publications

Enzyme regulationi

The adenylation activity is stimulated by glutamine and PII (GlnB), and inhibited by 2-oxoglutarate (PubMed:4867671, PubMed:4920894, PubMed:33597, PubMed:9312015). Deadenylation activity is stimulated by PII-UMP (GlnB-UMP) and 2-oxoglutarate, and inhibited by glutamine (PubMed:4893578, PubMed:4934180, PubMed:33597, PubMed:9312015, PubMed:14766310).7 Publications

Kineticsi

  1. KM=4 µM for adenylyl1 Publication
  2. KM=5 µM for [L-glutamate:ammonia ligase (ADP-forming)]1 Publication
  3. KM=150 µM for ATP1 Publication

    pH dependencei

    Optimum pH is between 7.3 and 7.6 (PubMed:4893578, PubMed:4920894). The enzyme is stable between pH 4 and 9 (PubMed:4920894).2 Publications

    GO - Molecular functioni

    • [glutamate-ammonia-ligase] adenylyltransferase activity Source: UniProtKB
    • ATP binding Source: UniProtKB
    • magnesium ion binding Source: UniProtKB

    GO - Biological processi

    Keywordsi

    Molecular functionNucleotidyltransferase, Transferase
    LigandATP-binding, Magnesium, Nucleotide-binding

    Enzyme and pathway databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzymeCurated
    Alternative name(s):
    ATP:glutamine synthetase adenylyltransferase1 Publication
    ATase1 Publication
    Including the following 2 domains:
    Glutamine synthetase adenylyl-L-tyrosine phosphorylase1 Publication (EC:2.7.7.894 Publications1 Publication)
    Alternative name(s):
    Adenylyl removase1 Publication
    Short name:
    AR1 Publication
    Short name:
    AT-N1 Publication
    Short name:
    AT-N4401 Publication
    Short name:
    P-I1 Publication
    Glutamine synthetase adenylyl transferase1 Publication (EC:2.7.7.421 Publication1 Publication)
    Alternative name(s):
    Adenylyl transferase1 Publication
    Short name:
    AT1 Publication
    Short name:
    AT-C1 Publication
    Gene namesi
    Name:glnE1 Publication
    Ordered Locus Names:b3053, JW3025
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11602. glnE.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002092441 – 946Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzymeAdd BLAST946

    Proteomic databases

    PaxDbiP30870.
    PRIDEiP30870.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi4261515. 4 interactors.
    DIPiDIP-9780N.
    IntActiP30870. 2 interactors.
    STRINGi316385.ECDH10B_3228.

    Structurei

    Secondary structure

    1946
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi6 – 16Combined sources11
    Helixi25 – 27Combined sources3
    Helixi30 – 38Combined sources9
    Helixi40 – 48Combined sources9
    Helixi51 – 58Combined sources8
    Helixi63 – 68Combined sources6
    Helixi69 – 76Combined sources8
    Turni77 – 79Combined sources3
    Helixi83 – 106Combined sources24
    Helixi112 – 141Combined sources30
    Beta strandi156 – 159Combined sources4
    Helixi161 – 164Combined sources4
    Beta strandi174 – 180Combined sources7
    Helixi195 – 211Combined sources17
    Helixi230 – 232Combined sources3
    Beta strandi235 – 238Combined sources4
    Helixi239 – 249Combined sources11
    Helixi252 – 258Combined sources7
    Beta strandi262 – 265Combined sources4
    Helixi270 – 283Combined sources14
    Helixi290 – 310Combined sources21
    Turni316 – 318Combined sources3
    Helixi323 – 337Combined sources15
    Turni338 – 340Combined sources3
    Helixi342 – 344Combined sources3
    Helixi349 – 358Combined sources10
    Helixi364 – 385Combined sources22
    Turni386 – 389Combined sources4
    Helixi399 – 408Combined sources10
    Helixi414 – 434Combined sources21
    Helixi450 – 457Combined sources8
    Helixi459 – 461Combined sources3
    Helixi467 – 469Combined sources3
    Helixi474 – 493Combined sources20
    Helixi498 – 515Combined sources18
    Helixi521 – 535Combined sources15
    Helixi539 – 547Combined sources9
    Helixi549 – 561Combined sources13
    Helixi563 – 571Combined sources9
    Helixi573 – 580Combined sources8
    Helixi582 – 585Combined sources4
    Helixi594 – 601Combined sources8
    Turni602 – 604Combined sources3
    Helixi610 – 633Combined sources24
    Helixi639 – 641Combined sources3
    Helixi642 – 669Combined sources28
    Helixi673 – 675Combined sources3
    Beta strandi682 – 687Combined sources6
    Helixi689 – 692Combined sources4
    Beta strandi702 – 708Combined sources7
    Beta strandi715 – 720Combined sources6
    Helixi724 – 740Combined sources17
    Helixi759 – 761Combined sources3
    Beta strandi764 – 767Combined sources4
    Helixi768 – 777Combined sources10
    Helixi781 – 788Combined sources8
    Beta strandi791 – 794Combined sources4
    Helixi797 – 811Combined sources15
    Helixi817 – 834Combined sources18
    Beta strandi842 – 844Combined sources3
    Turni845 – 847Combined sources3
    Helixi852 – 866Combined sources15
    Turni867 – 869Combined sources3
    Helixi871 – 874Combined sources4
    Helixi879 – 888Combined sources10
    Helixi894 – 916Combined sources23
    Beta strandi921 – 924Combined sources4
    Turni925 – 928Combined sources4
    Helixi929 – 943Combined sources15

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiP30870.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni1 – 440Adenylyl removase1 PublicationAdd BLAST440
    Regioni441 – 448Linker1 Publication8
    Regioni449 – 946Adenylyl transferase1 PublicationAdd BLAST498

    Sequence similaritiesi

    Belongs to the GlnE family.Curated

    Phylogenomic databases

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

    Family and domain databases

    HAMAPiMF_00802. GlnE. 1 hit.
    InterProiView protein in InterPro
    IPR023057. GlnE.
    IPR005190. GlnE_rpt_dom.
    IPR013546. PII_UdlTrfase/GS_AdlTrfase.
    PfamiView protein in Pfam
    PF08335. GlnD_UR_UTase. 2 hits.
    PF03710. GlnE. 2 hits.

    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)DescriptionActionsGraphical viewLength
    Sequence conflicti524Missing in CAA79892 (PubMed:8412694).Curated1
    Sequence conflicti624 – 625QL → PV in CAA79892 (PubMed:8412694).Curated2

    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.
    PATRICifig|1411691.4.peg.3678.

    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.

    Entry informationi

    Entry nameiGLNE_ECOLI
    AccessioniPrimary (citable) accession number: P30870
    Secondary accession number(s): P78107, Q2M9F2
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: November 1, 1997
    Last modified: July 5, 2017
    This is version 128 of the entry and version 2 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Multifunctional enzyme, 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