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O07637 (GLSA2_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glutaminase 2
EC=3.5.1.2
Gene names
Name:glsA2
Synonyms:ylaM
Ordered Locus Names:BSU14830
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length309 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

L-glutamine + H2O = L-glutamate + NH3. Ref.3

Subunit structure

Homotetramer. Ref.3

Sequence similarities

Belongs to the glutaminase family.

Biophysicochemical properties

Kinetic parameters:

KM=7.6 mM for glutamine Ref.3

Ontologies

Keywords
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglutamine metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionglutaminase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 309309Glutaminase 2 HAMAP-Rule MF_00313
PRO_0000110595

Sites

Binding site651Substrate By similarity
Binding site1171Substrate By similarity
Binding site1621Substrate By similarity
Binding site1691Substrate By similarity
Binding site1931Substrate By similarity
Binding site2451Substrate By similarity
Binding site2631Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
O07637 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: E1DFEF1A0723C1A5

FASTA30934,012
        10         20         30         40         50         60 
MVCQHNDELE ALVKKAKKVT DKGEVASYIP ALAKADKHDL SVAIYYSNNV CLSAGDVEKT 

        70         80         90        100        110        120 
FTLQSISKVL SLALVLMEYG KDKVFSYVGQ EPTGDPFNSI IKLETVNPSK PLNPMINAGA 

       130        140        150        160        170        180 
LVVTSLIRGR TVKERLDYLL SFIRRLTNNQ EITYCREVAE SEYSTSMINR AMCYYMKQYG 

       190        200        210        220        230        240 
IFEDDVEAVM DLYTKQCAIE MNSLDLAKIG SVFALNGRHP ETGEQVISKD VARICKTFMV 

       250        260        270        280        290        300 
TCGMYNASGE FAIKVGIPAK SGVSGGIMGI SPYDFGIGIF GPALDEKGNS IAGVKLLEIM 


SEMYRLSIF

« Hide

References

« Hide 'large scale' references
[1]"Bacillus subtilis chromosomal region downstream nprE."
Purnelle B., Presecan E., Glaser P., Richou A., Danchin A., Goffeau A.
Submitted (JUN-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]"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: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z97025 Genomic DNA. Translation: CAB09718.1.
AL009126 Genomic DNA. Translation: CAB13356.1.
PIRC69873.
RefSeqNP_389366.1. NC_000964.3.

3D structure databases

ProteinModelPortalO07637.
SMRO07637. Positions 4-309.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU14830.

Proteomic databases

PaxDbO07637.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB13356; CAB13356; BSU14830.
GeneID939852.
KEGGbsu:BSU14830.
PATRIC18974763. VBIBacSub10457_1573.

Organism-specific databases

GenoListBSU14830. [Micado]

Phylogenomic databases

eggNOGCOG2066.
HOGENOMHOG000216890.
KOK01425.
ProtClustDBPRK00971.

Enzyme and pathway databases

BioCycBSUB:BSU14830-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. PBP_transp_fold. 1 hit.
TIGRFAMsTIGR03814. Gln_ase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGLSA2_BACSU
AccessionPrimary (citable) accession number: O07637
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: May 1, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents