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Protein

Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme

Gene

glnE

Organism
Escherichia coli O81 (strain ED1a)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transduction protein PII (GlnB) which indicates the nitrogen status of the cell.UniRule annotation

Catalytic activityi

[Glutamine synthetase]-O(4)-(5'-adenylyl)-L-tyrosine + phosphate = [glutamine synthetase]-L-tyrosine + ADP.UniRule annotation
ATP + [glutamine synthetase]-L-tyrosine = diphosphate + [glutamine synthetase]-O(4)-(5'-adenylyl)-L-tyrosine.UniRule annotation

Cofactori

Mg2+UniRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywordsi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzymeUniRule annotation
Alternative name(s):
ATP:glutamine synthetase adenylyltransferaseUniRule annotation
ATaseUniRule annotation
Including the following 2 domains:
Glutamine synthetase adenylyl-L-tyrosine phosphorylaseUniRule annotation (EC:2.7.7.89UniRule annotation)
Alternative name(s):
Adenylyl removaseUniRule annotation
Short name:
ARUniRule annotation
Short name:
AT-NUniRule annotation
Glutamine synthetase adenylyl transferaseUniRule annotation (EC:2.7.7.42UniRule annotation)
Alternative name(s):
Adenylyl transferaseUniRule annotation
Short name:
ATUniRule annotation
Short name:
AT-CUniRule annotation
Gene namesi
Name:glnEUniRule annotation
Ordered Locus Names:ECED1_3721
OrganismiEscherichia coli O81 (strain ED1a)
Taxonomic identifieri585397 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000748 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001485431 – 946Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzymeAdd BLAST946

Structurei

3D structure databases

ProteinModelPortaliB7N0K2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 440Adenylyl removaseUniRule annotationAdd BLAST440
Regioni449 – 946Adenylyl transferaseUniRule annotationAdd BLAST498

Sequence similaritiesi

Belongs to the GlnE family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000256491.
KOiK00982.
OMAiEFMVQYA.

Family and domain databases

HAMAPiMF_00802. GlnE. 1 hit.
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.

B7N0K2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPLSSPLQQ YWQTVVERLP EPLAEESLSA QAKSVLTFSD FVQDSVIAHP
60 70 80 90 100
EWLTELESQP PQADEWQHYA AWLQEALSNV SDEAGLMREL RLFRRRIMVR
110 120 130 140 150
IAWAQTLALV TEESILQQLS HLAEMLIVAA 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 ARIMGDSDGV YANELRAMLR PFVFRRYIDF SVIQSLRNMK
310 320 330 340 350
GMIAREVRRR GLTDNIKLGA GGIREIEFIV QVFQLIRGGR EPSLQSRSLL
360 370 380 390 400
PTLSAIAALH LLSENDAEQL RVAYLFLRRL ENLLQSINDE QTQTLPFDEL
410 420 430 440 450
NRARLAWAMD FADWPQLTGV LTAHMANVRR VFNELIGDDE SETQEESLSE
460 470 480 490 500
QWRELWQDAL QEDDTTPVLA HLSEDDRKQV LMLIADFRKE 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):108,423
Last modified:February 10, 2009 - v1
Checksum:iDB01429C7EB7D0B3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU928162 Genomic DNA. Translation: CAR09870.2.
RefSeqiWP_012601759.1. NC_011745.1.

Genome annotation databases

EnsemblBacteriaiCAR09870; CAR09870; ECED1_3721.
KEGGiecq:ECED1_3721.
PATRICi38491478. VBIEscCol8292_3713.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU928162 Genomic DNA. Translation: CAR09870.2.
RefSeqiWP_012601759.1. NC_011745.1.

3D structure databases

ProteinModelPortaliB7N0K2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAR09870; CAR09870; ECED1_3721.
KEGGiecq:ECED1_3721.
PATRICi38491478. VBIEscCol8292_3713.

Phylogenomic databases

HOGENOMiHOG000256491.
KOiK00982.
OMAiEFMVQYA.

Family and domain databases

HAMAPiMF_00802. GlnE. 1 hit.
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...

Entry informationi

Entry nameiGLNE_ECO81
AccessioniPrimary (citable) accession number: B7N0K2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 10, 2009
Last modified: January 18, 2017
This is version 51 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme

Documents

  1. 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.