ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P30870


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name GLNE_ECOLI
Primary accession number P30870
Secondary accession numbers P78107 Q2M9F2
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on November 1, 1997 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 60)
Name and origin of the protein
Protein name Glutamate-ammonia-ligase adenylyltransferase
Synonyms EC 2.7.7.42
[Glutamate--ammonia-ligase] adenylyltransferase
Glutamine-synthetase adenylyltransferase
ATase
Gene name
Name: glnE
OrderedLocusNames: b3053, JW3025
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
STRAIN=K12 / CS520;
PubMed=8412694 [NCBI, ExPASy, EBI, Israel, Japan]
van Heeswijk W.C., Rabenberg M., Westerhoff H.V., Kahn D.D.;
"The genes of the glutamine synthetase adenylylation cascade are not regulated by nitrogen in Escherichia coli.";
Mol. Microbiol. 9:443-458(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[4]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-440.
DOI=10.1016/j.str.2004.02.029; PubMed=15130478 [NCBI, ExPASy, EBI, Israel, Japan]
Xu Y., Zhang R., Joachimiak A., Carr P.D., Huber T., Vasudevan S.G., Ollis D.L.;
"Structure of the N-terminal domain of Escherichia coli glutamine synthetase adenylyltransferase.";
Structure 12:861-869(2004).
Comments
  • FUNCTION: Adenylation and deadenylation of glutamine synthetase.
  • CATALYTIC ACTIVITY: ATP + [L-glutamate:ammonia ligase (ADP-forming)] = diphosphate + adenylyl-[L-glutamate:ammonia ligase (ADP-forming)].
  • SIMILARITY: Belongs to the glnE family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Z21844; CAA79892.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC76089.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE77104.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR C65093; C65093.
RefSeq AP_003603.1; -.
NP_417525.1; -.
3D structure databases
PDB
1V4A; X-ray; 2.00 A; A=1-440.[ExPASy / RCSB / EBI]
PDBsum 1V4A; -.
ModBase P30870.
Protein-protein interaction databases
IntAct P30870; -.
Enzyme and pathway databases
BioCyc EcoCyc:GLNE-MON; -.
Organism-specific databases
EchoBASE EB1559; -.
EcoGene EG11602; glnE.
Ontologies
GO
GO:0008882; Molecular function: [glutamate-ammonia-ligase] adenylyltransferase activity (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00802; -; 1.
PBIL [Tree]
InterPro IPR005190; GlnE.
Graphical view of domain structure.
Pfam PF03710; GlnE; 2.
Pfam graphical view of domain structure.
BLOCKS P30870.
ProtoNet P30870.
Genome annotation databases
GeneID 947552; -.
GenomeReviews U00096_GR; b3053.
AP009048_GR; JW3025.
KEGG ecj:JW3025; -.
eco:b3053; -.
Phylogenomic databases
HOGENOM P30870; -.
Genome annotation databases
CMR P30870; b3053.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Nucleotidyltransferase; Repeat; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   946  946     Glutamate-ammonia-ligase adenylyltransferase. PRO_0000209244
REGION   91   302  212     GlnE 1. 
REGION   609   830  222     GlnE 2. 
CONFLICT   524   524        Missing (in Ref. 1; CAA79892). 
CONFLICT   624   625        QL -> PV (in Ref. 1; CAA79892). 
HELIX   6    16  11      
HELIX   25    27  3      
HELIX   30    38  9      
HELIX   40    48  9      
HELIX   51    58  8      
HELIX   63    68  6      
HELIX   69    76  8      
TURN   77    79  3      
HELIX   83   106  24      
HELIX   112   141  30      
STRAND   156   159  4      
HELIX   161   164  4      
STRAND   174   180  7      
HELIX   195   211  17      
HELIX   230   232  3      
STRAND   235   238  4      
HELIX   239   249  11      
HELIX   252   258  7      
STRAND   262   265  4      
HELIX   270   283  14      
HELIX   290   310  21      
TURN   316   318  3      
HELIX   323   337  15      
TURN   338   340  3      
HELIX   342   344  3      
HELIX   349   358  10      
HELIX   364   385  22      
TURN   386   389  4      
HELIX   399   408  10      
HELIX   414   434  21      
Sequence information
Length: 946 AA [This is the length of the unprocessed precursor] Molecular weight: 108418 Da [This is the MW of the unprocessed precursor] CRC64: 6FD2D7BDC619DB83 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKPLSSPLQQ YWQTVVERLP EPLAEESLSA QAKSVLTFSD FVQDSVIAHP EWLTELESQP 

        70         80         90        100        110        120 
PQADEWQHYA AWLQEALCNV SDEAGLMREL RLFRRRIMVR IAWAQTLALV TEESILQQLS 

       130        140        150        160        170        180 
YLAETLIVAA RDWLYDACCR EWGTPCNAQG EAQPLLILGM GKLGGGELNF SSDIDLIFAW 

       190        200        210        220        230        240 
PEHGCTQGGR RELDNAQFFT RMGQRLIKVL DQPTQDGFVY RVDMRLRPFG ESGPLVLSFA 

       250        260        270        280        290        300 
ALEDYYQEQG RDWERYAMVK ARIMGDSEGV YANELRAMLR PFVFRRYIDF SVIQSLRNMK 

       310        320        330        340        350        360 
GMIAREVRRR GLTDNIKLGA GGIREIEFIV QVFQLIRGGR EPSLQSRSLL PTLSAIAELH 

       370        380        390        400        410        420 
LLSENDAEQL RVAYLFLRRL ENLLQSINDE QTQTLPSDEL NRARLAWAMD FADWPQLTGA 

       430        440        450        460        470        480 
LTAHMTNVRR VFNELIGDDE SETQEESLSE QWRELWQDAL QEDDTTPVLA HLSEDDRKQV 

       490        500        510        520        530        540 
LTLIADFRKE LDKRTIGPRG RQVLDHLMPH LLSDVCARED AAVTLSRITA LLVGIVTRTT 

       550        560        570        580        590        600 
YLELLSEFPA ALKHLISLCA ASPMIASQLA RYPLLLDELL DPNTLYQPTA TDAYRDELRQ 

       610        620        630        640        650        660 
YLLRVPEDDE EQQLEALRQF KQAQLLRIAA ADIAGTLPVM KVSDHLTWLA EAMIDAVVQQ 

       670        680        690        700        710        720 
AWVQMVARYG KPNHLNEREG RGFAVVGYGK LGGWELGYSS DLDLIFLHDC PMDAMTDGER 

       730        740        750        760        770        780 
EIDGRQFYLR LAQRIMHLFS TRTSSGILYE VDARLRPSGA AGMLVTSAEA FADYQKNEAW 

       790        800        810        820        830        840 
TWEHQALVRA RVVYGDPQLT AHFDAVRREI MTLPREGKTL QTEVREMREK MRAHLGNKHR 

       850        860        870        880        890        900 
DRFDIKADEG GITDIEFITQ YLVLRYAHEK PKLTRWSDNV RILELLAQND IMEEQEAMAL 

       910        920        930        940 
TRAYTTLRDE LHHLALQELP GHVSEDCFTA ERELVRASWQ KWLVEE 

P30870 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by au flag APAF Australia Mirror sites: Brazil  Canada  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!