SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P77454

- GLSA1_ECOLI

UniProt

P77454 - GLSA1_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Glutaminase 1

Gene
glsA1, ybaS, b0485, JW0474
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-glutamine + H2O = L-glutamate + NH3.1 Publication

Kineticsi

  1. KM=7.3 mM for glutamine1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei66 – 661Substrate By similarity
Binding sitei117 – 1171Substrate By similarity
Binding sitei161 – 1611Substrate By similarity
Binding sitei168 – 1681Substrate By similarity
Binding sitei192 – 1921Substrate By similarity
Binding sitei244 – 2441Substrate By similarity
Binding sitei262 – 2621Substrate; via amide nitrogen By similarity

GO - Molecular functioni

  1. glutaminase activity Source: EcoCyc

GO - Biological processi

  1. glutamine metabolic process Source: InterPro
  2. negative regulation of growth Source: EcoliWiki
  3. response to acidity Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Glutaminase 1 (EC:3.5.1.2)
Gene namesi
Name:glsA1
Synonyms:ybaS
Ordered Locus Names:b0485, JW0474
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG13247. glsA1.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi69 – 691K → A: Loss of activity. 1 Publication
Mutagenesisi117 – 1171N → A: Loss of activity. 1 Publication
Mutagenesisi160 – 1601S → A: Loss of activity. 1 Publication
Mutagenesisi161 – 1611E → A: Strongly reduced activity. 1 Publication
Mutagenesisi162 – 1621Q → A: No effect. 1 Publication
Mutagenesisi168 – 1681N → A: Loss of activity. 1 Publication
Mutagenesisi192 – 1921Y → A: Loss of activity. 1 Publication
Mutagenesisi244 – 2441Y → A: Loss of activity. 1 Publication
Mutagenesisi260 – 2601S → A: Reduced activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 310310Glutaminase 1UniRule annotationPRO_0000110607Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei294 – 2941N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP77454.
PRIDEiP77454.

Expressioni

Gene expression databases

GenevestigatoriP77454.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

DIPiDIP-11307N.
IntActiP77454. 2 interactions.
STRINGi511145.b0485.

Structurei

Secondary structure

1
310
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1815
Helixi31 – 344
Beta strandi42 – 476
Beta strandi52 – 576
Helixi65 – 673
Helixi68 – 8013
Helixi82 – 887
Helixi101 – 1066
Turni107 – 1093
Helixi117 – 12610
Helixi132 – 14716
Helixi155 – 1628
Helixi166 – 17813
Helixi185 – 19511
Beta strandi198 – 2003
Helixi202 – 21312
Beta strandi216 – 2183
Turni219 – 2224
Helixi228 – 2303
Helixi231 – 24111
Helixi244 – 2463
Helixi247 – 2537
Beta strandi258 – 2603
Beta strandi264 – 2707
Turni271 – 2733
Beta strandi274 – 2796
Helixi290 – 30314

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1U60X-ray1.61A/B/C/D1-310[»]
ProteinModelPortaliP77454.
SMRiP77454. Positions 2-310.

Miscellaneous databases

EvolutionaryTraceiP77454.

Family & Domainsi

Sequence similaritiesi

Belongs to the glutaminase family.

Phylogenomic databases

eggNOGiCOG2066.
HOGENOMiHOG000216890.
KOiK01425.
OMAiQCSVGVT.
OrthoDBiEOG6N94BK.
PhylomeDBiP77454.

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
HAMAPiMF_00313. Glutaminase.
InterProiIPR012338. Beta-lactam/transpept-like.
IPR015868. Glutaminase.
[Graphical view]
PANTHERiPTHR12544. PTHR12544. 1 hit.
PfamiPF04960. Glutaminase. 1 hit.
[Graphical view]
SUPFAMiSSF56601. SSF56601. 1 hit.
TIGRFAMsiTIGR03814. Gln_ase. 1 hit.

Sequencei

Sequence statusi: Complete.

P77454-1 [UniParc]FASTAAdd to Basket

« Hide

MLDANKLQQA VDQAYTQFHS LNGGQNADYI PFLANVPGQL AAVAIVTCDG    50
NVYSAGDSDY RFALESISKV CTLALALEDV GPQAVQDKIG ADPTGLPFNS 100
VIALELHGGK PLSPLVNAGA IATTSLINAE NVEQRWQRIL HIQQQLAGEQ 150
VALSDEVNQS EQTTNFHNRA IAWLLYSAGY LYCDAMEACD VYTRQCSTLL 200
NTIELATLGA TLAAGGVNPL THKRVLQADN VPYILAEMMM EGLYGRSGDW 250
AYRVGLPGKS GVGGGILAVV PGVMGIAAFS PPLDEDGNSV RGQKMVASVA 300
KQLGYNVFKG 310
Length:310
Mass (Da):32,903
Last modified:February 1, 1997 - v1
Checksum:i4448BA0549E3C851
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U82664 Genomic DNA. Translation: AAB40239.1.
U00096 Genomic DNA. Translation: AAC73587.1.
AP009048 Genomic DNA. Translation: BAE76264.1.
PIRiD64779.
RefSeqiNP_415018.1. NC_000913.3.
YP_488776.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73587; AAC73587; b0485.
BAE76264; BAE76264; BAE76264.
GeneIDi12932991.
946187.
KEGGiecj:Y75_p0472.
eco:b0485.
PATRICi32116129. VBIEscCol129921_0506.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U82664 Genomic DNA. Translation: AAB40239.1 .
U00096 Genomic DNA. Translation: AAC73587.1 .
AP009048 Genomic DNA. Translation: BAE76264.1 .
PIRi D64779.
RefSeqi NP_415018.1. NC_000913.3.
YP_488776.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1U60 X-ray 1.61 A/B/C/D 1-310 [» ]
ProteinModelPortali P77454.
SMRi P77454. Positions 2-310.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-11307N.
IntActi P77454. 2 interactions.
STRINGi 511145.b0485.

Proteomic databases

PaxDbi P77454.
PRIDEi P77454.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73587 ; AAC73587 ; b0485 .
BAE76264 ; BAE76264 ; BAE76264 .
GeneIDi 12932991.
946187.
KEGGi ecj:Y75_p0472.
eco:b0485.
PATRICi 32116129. VBIEscCol129921_0506.

Organism-specific databases

EchoBASEi EB3036.
EcoGenei EG13247. glsA1.

Phylogenomic databases

eggNOGi COG2066.
HOGENOMi HOG000216890.
KOi K01425.
OMAi QCSVGVT.
OrthoDBi EOG6N94BK.
PhylomeDBi P77454.

Enzyme and pathway databases

BioCyci EcoCyc:G6261-MONOMER.
ECOL316407:JW0474-MONOMER.
MetaCyc:G6261-MONOMER.

Miscellaneous databases

EvolutionaryTracei P77454.
PROi P77454.

Gene expression databases

Genevestigatori P77454.

Family and domain databases

Gene3Di 3.40.710.10. 1 hit.
HAMAPi MF_00313. Glutaminase.
InterProi IPR012338. Beta-lactam/transpept-like.
IPR015868. Glutaminase.
[Graphical view ]
PANTHERi PTHR12544. PTHR12544. 1 hit.
Pfami PF04960. Glutaminase. 1 hit.
[Graphical view ]
SUPFAMi SSF56601. SSF56601. 1 hit.
TIGRFAMsi TIGR03814. Gln_ase. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiGLSA1_ECOLI
AccessioniPrimary (citable) accession number: P77454
Secondary accession number(s): Q2MBU2
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi