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Reviewed, UniProtKB/Swiss-Prot A9N5X9 (GLNE_SALPB)

Last modified June 16, 2009. Version 9. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glutamate-ammonia-ligase adenylyltransferase
    EC=2.7.7.42
Alternative name(s):
    [Glutamate--ammonia-ligase] adenylyltransferase
    Glutamine-synthetase adenylyltransferase
      Short name=ATase
Gene names
Name: glnE
Ordered Locus Names: SPAB_03996
OrganismSalmonella paratyphi B (strain ATCC BAA-1250 / SPB7) [Complete proteome] [HAMAP]
Taxonomic identifier272994 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonellaSalmonella enterica subsp. enterica serovar Paratyphi B

Protein attributes

Sequence length947 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Adenylation and deadenylation of glutamine synthetase By similarity.

Catalytic activity

ATP + [L-glutamate:ammonia ligase (ADP-forming)] = diphosphate + adenylyl-[L-glutamate:ammonia ligase (ADP-forming)]. HAMAP MF_00802

Sequence similarities

Belongs to the glnE family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 947947Glutamate-ammonia-ligase adenylyltransferase HAMAP MF_00802
PRO_1000083702

Regions

Region91 – 302212GlnE 1 HAMAP MF_00802
Region610 – 831222GlnE 2 HAMAP MF_00802

Sequences

Sequence LengthMass (Da)Tools
A9N5X9-1 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 8B93CB49F3B2AC9C

FASTA947108,025
        10         20         30         40         50         60 
MTPLSSPLSQ YWQTVVERLP EGFTETSLSA QAKSVLTFSD FALDSVIAHP EWLAELESAS 

        70         80         90        100        110        120 
PQADEWRHYA GWLQEALAGV CDDASLMREL RFFRRRIMVR IAWAQTLSLV DDETILQQLS 

       130        140        150        160        170        180 
HLAETLIVGA RDWLYAACCR EWGTPCNPQG VPQPLLILGM GKLGGGELNF SSDIDLIFAW 

       190        200        210        220        230        240 
PEHGETRGGR RELDNAQFFT RLGQRLIKAL DQPTMDGFVY RVDMRLRPFG DSGPLVLSFA 

       250        260        270        280        290        300 
ALEDYYQEQG RDWERYAMVK ARLMGDNDDA WSRELRAMLR PFVFRRYIDF SVIQSLRNMK 

       310        320        330        340        350        360 
GMIAREVRRR GLKDNIKLGA GGIREIEFIV QVFQLIRGGR EPSLQSRSLL PTLDAIAALH 

       370        380        390        400        410        420 
LLPENDVAQL RVAYLFLRRL ENLLQSINDE QTQTLPADDL NRARLAWGMK AENWPQLVGE 

       430        440        450        460        470        480 
LTDHMANVRR VFNELIGDDE ADTPQEEERS EPWREVWQDA LQEDDSTPVL AHLADEDRRQ 

       490        500        510        520        530        540 
VLTLIADFRK ELDKRPIGPR GRQVLDQLMP HLLADVCSRE DAAVTLSRIT PLLAGIVTRT 

       550        560        570        580        590        600 
TYLELLSEFP GALKHLIMLC AASPMIASQL ARYPLLLDEL LDPGTLYQPT ATDAYRDELR 

       610        620        630        640        650        660 
QYLLRVPEED EEQQLEALRQ FKQAQLLRIA AADIAGTLPV MKVSDHLTWL AEAMIDAVVQ 

       670        680        690        700        710        720 
QAWTQMVARY GQPAHLDERQ GRGFAVVGYG KLGGWELGYS SDLDLIFLHD CPMDVMTNGE 

       730        740        750        760        770        780 
REIDGRQFYL RLAQRIMHLF STRTSSGILY EVDARLRPSG AAGMLVTSAD AFADYQQHEA 

       790        800        810        820        830        840 
WTWEHQALVR ARVVYGDPQL TSQFDTVRRT IMTTARDGKT LQTEVREMRE KMRAHLGNKH 

       850        860        870        880        890        900 
RDRFDIKADE GGITDIEFIA QYLVLRYAHE KPKLTRWSDN VRILELLAQN GIMDEHEAQA 

       910        920        930        940 
LTVAYTTLRD ELHHLALQEL PGHVAQTCFS KERALVQASW RKWLVAV 

« Hide

References

[1]McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W., Johnson M., Thiruvilangam P., Wilson R.
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000886 Genomic DNA. Translation: ABX69325.1.
RefSeqYP_001590158.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5778444.
GenomeReviewsGene locus SPAB_03996 in contig CP000886_GR.
KEGGspq:SPAB_03996.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAA9N5X9. WERYAMI.

Family and domain databases

HAMAPMF_00802.
[Tree]
InterProIPR005190. GlnE.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view]
PfamPF08335. GlnD_UR_UTase. 2 hits.
PF03710. GlnE. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLNE_SALPB
AccessionPrimary (citable) accession number: A9N5X9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: June 16, 2009
This is version 9 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents