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P77454

- GLSA1_ECOLI

UniProt

P77454 - GLSA1_ECOLI

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Protein

Glutaminase 1

Gene

glsA1

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 PublicationUniRule annotation

Kineticsi

  1. KM=7.3 mM for glutamine1 Publication

Sites

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

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 acidic pH 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 1UniRule annotation (EC:3.5.1.2UniRule annotation)
Gene namesi
Name:glsA1UniRule annotation
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 1PRO_0000110607Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP77454.
PRIDEiP77454.

Expressioni

Gene expression databases

GenevestigatoriP77454.

Interactioni

Subunit structurei

Homotetramer.1 PublicationUniRule annotation

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 – 1815Combined sources
Helixi31 – 344Combined sources
Beta strandi42 – 476Combined sources
Beta strandi52 – 576Combined sources
Helixi65 – 673Combined sources
Helixi68 – 8013Combined sources
Helixi82 – 887Combined sources
Helixi101 – 1066Combined sources
Turni107 – 1093Combined sources
Helixi117 – 12610Combined sources
Helixi132 – 14716Combined sources
Helixi155 – 1628Combined sources
Helixi166 – 17813Combined sources
Helixi185 – 19511Combined sources
Beta strandi198 – 2003Combined sources
Helixi202 – 21312Combined sources
Beta strandi216 – 2183Combined sources
Turni219 – 2224Combined sources
Helixi228 – 2303Combined sources
Helixi231 – 24111Combined sources
Helixi244 – 2463Combined sources
Helixi247 – 2537Combined sources
Beta strandi258 – 2603Combined sources
Beta strandi264 – 2707Combined sources
Turni271 – 2733Combined sources
Beta strandi274 – 2796Combined sources
Helixi290 – 30314Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP77454.

Family & Domainsi

Sequence similaritiesi

Belongs to the glutaminase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG2066.
HOGENOMiHOG000216890.
InParanoidiP77454.
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

        10         20         30         40         50
MLDANKLQQA VDQAYTQFHS LNGGQNADYI PFLANVPGQL AAVAIVTCDG
60 70 80 90 100
NVYSAGDSDY RFALESISKV CTLALALEDV GPQAVQDKIG ADPTGLPFNS
110 120 130 140 150
VIALELHGGK PLSPLVNAGA IATTSLINAE NVEQRWQRIL HIQQQLAGEQ
160 170 180 190 200
VALSDEVNQS EQTTNFHNRA IAWLLYSAGY LYCDAMEACD VYTRQCSTLL
210 220 230 240 250
NTIELATLGA TLAAGGVNPL THKRVLQADN VPYILAEMMM EGLYGRSGDW
260 270 280 290 300
AYRVGLPGKS GVGGGILAVV PGVMGIAAFS PPLDEDGNSV RGQKMVASVA
310
KQLGYNVFKG
Length:310
Mass (Da):32,903
Last modified:February 1, 1997 - v1
Checksum:i4448BA0549E3C851
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P77454.
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: November 26, 2014
This is version 110 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