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G2S349 (G2S349_ENTAL) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 18. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length308 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

L-glutamine + H2O = L-glutamate + NH3. SAAS SAAS012338 HAMAP-Rule MF_00313

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00313 SAAS SAAS012338

Sequence similarities

Belongs to the glutaminase family. HAMAP-Rule MF_00313

Ontologies

Keywords
   Molecular functionHydrolase SAAS SAAS012338 HAMAP-Rule MF_00313
   PTMAcetylation HAMAP-Rule MF_00313
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglutamine metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionglutaminase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Binding site661Substrate By similarity HAMAP-Rule MF_00313
Binding site1171Substrate By similarity HAMAP-Rule MF_00313
Binding site1611Substrate By similarity HAMAP-Rule MF_00313
Binding site1681Substrate By similarity HAMAP-Rule MF_00313
Binding site1921Substrate By similarity HAMAP-Rule MF_00313
Binding site2441Substrate By similarity HAMAP-Rule MF_00313
Binding site2621Substrate; via amide nitrogen By similarity HAMAP-Rule MF_00313

Sequences

Sequence LengthMass (Da)Tools
G2S349 [UniParc].

Last modified November 16, 2011. Version 1.
Checksum: 7C6ECE772A7EC06C

FASTA30833,721
        10         20         30         40         50         60 
MAAVIHNEML EEILAQVRPL LGQGKVADYI PALASVSGNK LGIAICTVDG QRYQAGDATE 

        70         80         90        100        110        120 
RFSIQSISKV LSLVAAMRQY DEDEIWQRVG KDPSGQSFNS LLQLEIEHGK PRNPFINAGA 

       130        140        150        160        170        180 
LVVCDMLQSR LSAPRQRMLE IVRLLCGVPD ITYDPVVARS EFEHSARNAA IAWLMKSFGN 

       190        200        210        220        230        240 
FHNDVAMVLQ NYFHYCALKM SCVELAQTFL FLAHQGYASH LTQEVVSPMQ ARQINALMAT 

       250        260        270        280        290        300 
SGMYQNAGEF AWRVGLPAKS GVGGGVVAIV PHEMAIAVWS PELDETGNSL AGVAVLEQLT 


QRLGRSVY 

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References

[1]"Complete sequence of chromosome of Enterobacter asburiae LF7a."
Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., van der Lelie D., Woyke T.
Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LF7a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP003026 Genomic DNA. Translation: AEN64888.1.
RefSeqYP_004828673.1. NC_015968.1.

3D structure databases

ProteinModelPortalG2S349.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEN64888; AEN64888; Entas_2154.
GeneID11107873.
KEGGeas:Entas_2154.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01425.
OMAMSIAVWS.

Enzyme and pathway databases

BioCycEASB640513:GKDM-2200-MONOMER.

Family and domain databases

Gene3D3.40.710.10. 1 hit.
HAMAPMF_00313. Glutaminase.
InterProIPR012338. Beta-lactam/transpept-like.
IPR015868. Glutaminase.
[Graphical view]
PANTHERPTHR12544. PTHR12544. 1 hit.
PfamPF04960. Glutaminase. 1 hit.
[Graphical view]
SUPFAMSSF56601. SSF56601. 1 hit.
TIGRFAMsTIGR03814. Gln_ase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameG2S349_ENTAL
AccessionPrimary (citable) accession number: G2S349
Entry history
Integrated into UniProtKB/TrEMBL: November 16, 2011
Last sequence update: November 16, 2011
Last modified: June 11, 2014
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)