UniProtKB - P30870 (GLNE_ECOLI)
Protein
Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme
Gene
glnE
Organism
Escherichia coli (strain K12)
Status
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 + ADP4 Publications1 PublicationEC:2.7.7.894 Publications1 Publication
- [glutamine synthetase]-L-tyrosine + ATP = [glutamine synthetase]-O4-(5'-adenylyl)-L-tyrosine + diphosphate1 Publication1 PublicationEC:2.7.7.421 Publication1 Publication
Cofactori
Mg2+4 PublicationsNote: Can also use Mn2+.4 Publications
Activity 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
- KM=4 µM for adenylyl1 Publication
- KM=5 µM for [L-glutamate:ammonia ligase (ADP-forming)]1 Publication
- 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
- [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase Source: UniProtKB-EC
- ATP binding Source: UniProtKB
- magnesium ion binding Source: UniProtKB
GO - Biological processi
- regulation of glutamine family amino acid metabolic process Source: UniProtKB
Keywordsi
Molecular function | Multifunctional enzyme, Nucleotidyltransferase, Transferase |
Ligand | ATP-binding, Magnesium, Nucleotide-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:GLNE-MONOMER MetaCyc:GLNE-MONOMER |
BRENDAi | 2.7.7.42, 2026 |
Names & Taxonomyi
Protein namesi | Recommended name: Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzymeCuratedAlternative 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 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 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000209244 | 1 – 946 | Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzymeAdd BLAST | 946 |
Proteomic databases
jPOSTi | P30870 |
PaxDbi | P30870 |
PRIDEi | P30870 |
Interactioni
Subunit structurei
Monomer.
1 PublicationProtein-protein interaction databases
BioGRIDi | 4261515, 4 interactors |
DIPi | DIP-9780N |
IntActi | P30870, 2 interactors |
STRINGi | 511145.b3053 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P30870 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P30870 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 440 | Adenylyl removase1 PublicationAdd BLAST | 440 | |
Regioni | 441 – 448 | Linker1 Publication | 8 | |
Regioni | 449 – 946 | Adenylyl transferase1 PublicationAdd BLAST | 498 |
Sequence similaritiesi
Belongs to the GlnE family.Curated
Phylogenomic databases
eggNOGi | COG1391, Bacteria |
HOGENOMi | CLU_006233_0_1_6 |
InParanoidi | P30870 |
PhylomeDBi | P30870 |
Family and domain databases
Gene3Di | 3.30.460.10, 1 hit |
HAMAPi | MF_00802, GlnE, 1 hit |
InterProi | View protein in InterPro IPR023057, GlnE IPR005190, GlnE_rpt_dom IPR043519, NT_sf IPR013546, PII_UdlTrfase/GS_AdlTrfase |
PANTHERi | PTHR30621, PTHR30621, 1 hit |
Pfami | View protein in Pfam PF08335, GlnD_UR_UTase, 2 hits PF03710, GlnE, 2 hits |
SUPFAMi | SSF81301, SSF81301, 2 hits |
i Sequence
Sequence statusi: Complete.
P30870-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 524 | Missing in CAA79892 (PubMed:8412694).Curated | 1 | |
Sequence conflicti | 624 – 625 | QL → PV in CAA79892 (PubMed:8412694).Curated | 2 |
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 |
PIRi | C65093 |
RefSeqi | NP_417525.1, NC_000913.3 WP_001301081.1, NZ_SSZK01000028.1 |
Genome annotation databases
EnsemblBacteriai | AAC76089; AAC76089; b3053 BAE77104; BAE77104; BAE77104 |
GeneIDi | 947552 |
KEGGi | ecj:JW3025 eco:b3053 |
PATRICi | fig|1411691.4.peg.3678 |
Similar proteinsi
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 |
PIRi | C65093 |
RefSeqi | NP_417525.1, NC_000913.3 WP_001301081.1, NZ_SSZK01000028.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1V4A | X-ray | 2.00 | A | 1-440 | [»] | |
3K7D | X-ray | 2.40 | A/B | 449-946 | [»] | |
SMRi | P30870 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4261515, 4 interactors |
DIPi | DIP-9780N |
IntActi | P30870, 2 interactors |
STRINGi | 511145.b3053 |
Proteomic databases
jPOSTi | P30870 |
PaxDbi | P30870 |
PRIDEi | P30870 |
Genome annotation databases
EnsemblBacteriai | AAC76089; AAC76089; b3053 BAE77104; BAE77104; BAE77104 |
GeneIDi | 947552 |
KEGGi | ecj:JW3025 eco:b3053 |
PATRICi | fig|1411691.4.peg.3678 |
Organism-specific databases
EchoBASEi | EB1559 |
Phylogenomic databases
eggNOGi | COG1391, Bacteria |
HOGENOMi | CLU_006233_0_1_6 |
InParanoidi | P30870 |
PhylomeDBi | P30870 |
Enzyme and pathway databases
BioCyci | EcoCyc:GLNE-MONOMER MetaCyc:GLNE-MONOMER |
BRENDAi | 2.7.7.42, 2026 |
Miscellaneous databases
EvolutionaryTracei | P30870 |
PROi | PR:P30870 |
Family and domain databases
Gene3Di | 3.30.460.10, 1 hit |
HAMAPi | MF_00802, GlnE, 1 hit |
InterProi | View protein in InterPro IPR023057, GlnE IPR005190, GlnE_rpt_dom IPR043519, NT_sf IPR013546, PII_UdlTrfase/GS_AdlTrfase |
PANTHERi | PTHR30621, PTHR30621, 1 hit |
Pfami | View protein in Pfam PF08335, GlnD_UR_UTase, 2 hits PF03710, GlnE, 2 hits |
SUPFAMi | SSF81301, SSF81301, 2 hits |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | GLNE_ECOLI | |
Accessioni | P30870Primary (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: | April 7, 2021 | |
This is version 148 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families