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P77454 (GLSA1_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutaminase 1

EC=3.5.1.2
Gene names
Name:glsA1
Synonyms:ybaS
Ordered Locus Names:b0485, JW0474
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length310 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

L-glutamine + H2O = L-glutamate + NH3. Ref.5

Subunit structure

Homotetramer. Ref.5

Sequence similarities

Belongs to the glutaminase family.

Biophysicochemical properties

Kinetic parameters:

KM=7.3 mM for glutamine Ref.5

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 310310Glutaminase 1 HAMAP-Rule MF_00313
PRO_0000110607

Sites

Binding site661Substrate By similarity
Binding site1171Substrate By similarity
Binding site1611Substrate By similarity
Binding site1681Substrate By similarity
Binding site1921Substrate By similarity
Binding site2441Substrate By similarity
Binding site2621Substrate; via amide nitrogen By similarity

Amino acid modifications

Modified residue2941N6-acetyllysine Ref.4

Experimental info

Mutagenesis691K → A: Loss of activity. Ref.5
Mutagenesis1171N → A: Loss of activity. Ref.5
Mutagenesis1601S → A: Loss of activity. Ref.5
Mutagenesis1611E → A: Strongly reduced activity. Ref.5
Mutagenesis1621Q → A: No effect. Ref.5
Mutagenesis1681N → A: Loss of activity. Ref.5
Mutagenesis1921Y → A: Loss of activity. Ref.5
Mutagenesis2441Y → A: Loss of activity. Ref.5
Mutagenesis2601S → A: Reduced activity. Ref.5

Secondary structure

................................................ 310
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P77454 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 4448BA0549E3C851

FASTA31032,903
        10         20         30         40         50         60 
MLDANKLQQA VDQAYTQFHS LNGGQNADYI PFLANVPGQL AAVAIVTCDG NVYSAGDSDY 

        70         80         90        100        110        120 
RFALESISKV CTLALALEDV GPQAVQDKIG ADPTGLPFNS VIALELHGGK PLSPLVNAGA 

       130        140        150        160        170        180 
IATTSLINAE NVEQRWQRIL HIQQQLAGEQ VALSDEVNQS EQTTNFHNRA IAWLLYSAGY 

       190        200        210        220        230        240 
LYCDAMEACD VYTRQCSTLL NTIELATLGA TLAAGGVNPL THKRVLQADN VPYILAEMMM 

       250        260        270        280        290        300 
EGLYGRSGDW AYRVGLPGKS GVGGGILAVV PGVMGIAAFS PPLDEDGNSV RGQKMVASVA 

       310 
KQLGYNVFKG 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of minutes 4-25 of Escherichia coli."
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[2]"The complete genome sequence of Escherichia coli K-12."
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.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-294, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[5]"Functional and structural characterization of four glutaminases from Escherichia coli and Bacillus subtilis."
Brown G., Singer A., Proudfoot M., Skarina T., Kim Y., Chang C., Dementieva I., Kuznetsova E., Gonzalez C.F., Joachimiak A., Savchenko A., Yakunin A.F.
Biochemistry 47:5724-5735(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.61 ANGSTROMS), CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-69; ASN-117; SER-160; GLU-161; GLN-162; ASN-168; TYR-192; TYR-244 AND SER-260, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U82664 Genomic DNA. Translation: AAB40239.1.
U00096 Genomic DNA. Translation: AAC73587.1.
AP009048 Genomic DNA. Translation: BAE76264.1.
PIRD64779.
RefSeqNP_415018.1. NC_000913.3.
YP_488776.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1U60X-ray1.61A/B/C/D1-310[»]
ProteinModelPortalP77454.
SMRP77454. Positions 2-310.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-11307N.
IntActP77454. 2 interactions.
STRING511145.b0485.

Proteomic databases

PaxDbP77454.
PRIDEP77454.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73587; AAC73587; b0485.
BAE76264; BAE76264; BAE76264.
GeneID12932991.
946187.
KEGGecj:Y75_p0472.
eco:b0485.
PATRIC32116129. VBIEscCol129921_0506.

Organism-specific databases

EchoBASEEB3036.
EcoGeneEG13247. glsA1.

Phylogenomic databases

eggNOGCOG2066.
HOGENOMHOG000216890.
KOK01425.
OMAQCSVGVT.
OrthoDBEOG6N94BK.
PhylomeDBP77454.

Enzyme and pathway databases

BioCycEcoCyc:G6261-MONOMER.
ECOL316407:JW0474-MONOMER.
MetaCyc:G6261-MONOMER.

Gene expression databases

GenevestigatorP77454.

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...

Other

EvolutionaryTraceP77454.
PROP77454.

Entry information

Entry nameGLSA1_ECOLI
AccessionPrimary (citable) accession number: P77454
Secondary accession number(s): Q2MBU2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: May 14, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene