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O31465 (GLSA1_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 98. 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:glsA, ybgJ
Ordered Locus Names:BSU02430
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length327 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

L-glutamine + H2O = L-glutamate + NH3. Ref.4

Subunit structure

Homotetramer. Ref.4

Sequence similarities

Belongs to the glutaminase family.

Biophysicochemical properties

Kinetic parameters:

KM=27.6 mM for glutamine Ref.4

Ontologies

Keywords
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Reference 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

Molecule processing

Chain1 – 327327Glutaminase 1 HAMAP-Rule MF_00313
PRO_0000110594

Sites

Binding site741Substrate
Binding site1261Substrate
Binding site1701Substrate
Binding site1771Substrate
Binding site2011Substrate
Binding site2531Substrate
Binding site2711Substrate; via amide nitrogen

Secondary structure

..................................................... 327
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O31465 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: BE3A1C2366460287

FASTA32736,187
        10         20         30         40         50         60 
MKELIKEHQK DINPALQLHD WVEYYRPFAA NGQSANYIPA LGKVNDSQLG ICVLEPDGTM 

        70         80         90        100        110        120 
IHAGDWNVSF TMQSISKVIS FIAACMSRGI PYVLDRVDVE PTGDAFNSII RLEINKPGKP 

       130        140        150        160        170        180 
FNPMINAGAL TIASILPGES AYEKLEFLYS VMETLIGKRP RIHEEVFRSE WETAHRNRAL 

       190        200        210        220        230        240 
AYYLKETNFL EAEVEETLEV YLKQCAMEST TEDIALIGLI LAHDGYHPIR HEQVIPKDVA 

       250        260        270        280        290        300 
KLAKALMLTC GMYNASGKYA AFVGVPAKSG VSGGIMALVP PSARREQPFQ SGCGIGIYGP 

       310        320 
AIDEYGNSLT GGMLLKHMAQ EWELSIF 

« Hide

References

« Hide 'large scale' references
[1]"Sequence analysis of the 70kb region between 17 and 23 degree of the Bacillus subtilis chromosome."
Haga K., Liu H., Yasumoto K., Takahashi H., Yoshikawa H.
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"Enhancement of glutamine utilization in Bacillus subtilis through the GlnK-GlnL two-component regulatory system."
Satomura T., Shimura D., Asai K., Sadaie Y., Hirooka K., Fujita Y.
J. Bacteriol. 187:4813-4821(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, GENE NAME.
Strain: 168.
[4]"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 (2.00 ANGSTROMS) IN COMPLEX WITH INHIBITOR 5-OXO-L-NORLEUCINE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB006424 Genomic DNA. Translation: BAA33141.1.
AL009126 Genomic DNA. Translation: CAB12037.1.
PIRD69751.
RefSeqNP_388125.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MKIX-ray2.00A/B1-327[»]
2OSUX-ray2.29A/B1-327[»]
3AGFX-ray2.60A/B1-327[»]
3BRMX-ray2.29A/B1-327[»]
ProteinModelPortalO31465.
SMRO31465. Positions 1-327.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU02430.

Proteomic databases

PaxDbO31465.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB12037; CAB12037; BSU02430.
GeneID938416.
KEGGbsu:BSU02430.
PATRIC18972037. VBIBacSub10457_0247.

Organism-specific databases

GenoListBSU02430. [Micado]

Phylogenomic databases

eggNOGCOG2066.
HOGENOMHOG000216890.
KOK01425.
OMAAKALMLT.
OrthoDBEOG6N94BK.
ProtClustDBPRK12357.

Enzyme and pathway databases

BioCycBSUB:BSU02430-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...

Other

EvolutionaryTraceO31465.
PROO31465.

Entry information

Entry nameGLSA1_BACSU
AccessionPrimary (citable) accession number: O31465
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: January 1, 1998
Last modified: February 19, 2014
This is version 98 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

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList