Skip Header

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

Glutaminase 2

Gene

glsA2

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-glutamine + H2O = L-glutamate + NH3.1 PublicationUniRule annotation

Kineticsi

  1. KM=7.6 mM for glutamine1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei65 – 651SubstrateUniRule annotation
Binding sitei117 – 1171SubstrateUniRule annotation
Binding sitei162 – 1621SubstrateUniRule annotation
Binding sitei169 – 1691SubstrateUniRule annotation
Binding sitei193 – 1931SubstrateUniRule annotation
Binding sitei245 – 2451SubstrateUniRule annotation
Binding sitei263 – 2631Substrate; via amide nitrogenUniRule annotation

GO - Molecular functioni

  1. glutaminase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. glutamine metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciBSUB:BSU14830-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutaminase 2UniRule annotation (EC:3.5.1.2UniRule annotation)
Gene namesi
Name:glsA2UniRule annotation
Synonyms:ylaM
Ordered Locus Names:BSU14830
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU14830. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 309309Glutaminase 2PRO_0000110595Add
BLAST

Proteomic databases

PaxDbiO07637.

Interactioni

Subunit structurei

Homotetramer.1 PublicationUniRule annotation

Protein-protein interaction databases

STRINGi224308.BSU14830.

Structurei

3D structure databases

ProteinModelPortaliO07637.
SMRiO07637. Positions 4-309.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glutaminase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG2066.
HOGENOMiHOG000216890.
InParanoidiO07637.
KOiK01425.
OMAiTKQCAIE.
OrthoDBiEOG6N94BK.
PhylomeDBiO07637.

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.

O07637-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVCQHNDELE ALVKKAKKVT DKGEVASYIP ALAKADKHDL SVAIYYSNNV
60 70 80 90 100
CLSAGDVEKT FTLQSISKVL SLALVLMEYG KDKVFSYVGQ EPTGDPFNSI
110 120 130 140 150
IKLETVNPSK PLNPMINAGA LVVTSLIRGR TVKERLDYLL SFIRRLTNNQ
160 170 180 190 200
EITYCREVAE SEYSTSMINR AMCYYMKQYG IFEDDVEAVM DLYTKQCAIE
210 220 230 240 250
MNSLDLAKIG SVFALNGRHP ETGEQVISKD VARICKTFMV TCGMYNASGE
260 270 280 290 300
FAIKVGIPAK SGVSGGIMGI SPYDFGIGIF GPALDEKGNS IAGVKLLEIM

SEMYRLSIF
Length:309
Mass (Da):34,012
Last modified:July 1, 1997 - v1
Checksum:iE1DFEF1A0723C1A5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z97025 Genomic DNA. Translation: CAB09718.1.
AL009126 Genomic DNA. Translation: CAB13356.1.
PIRiC69873.
RefSeqiNP_389366.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB13356; CAB13356; BSU14830.
GeneIDi939852.
KEGGibsu:BSU14830.
PATRICi18974763. VBIBacSub10457_1573.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z97025 Genomic DNA. Translation: CAB09718.1.
AL009126 Genomic DNA. Translation: CAB13356.1.
PIRiC69873.
RefSeqiNP_389366.1. NC_000964.3.

3D structure databases

ProteinModelPortaliO07637.
SMRiO07637. Positions 4-309.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU14830.

Proteomic databases

PaxDbiO07637.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13356; CAB13356; BSU14830.
GeneIDi939852.
KEGGibsu:BSU14830.
PATRICi18974763. VBIBacSub10457_1573.

Organism-specific databases

GenoListiBSU14830. [Micado]

Phylogenomic databases

eggNOGiCOG2066.
HOGENOMiHOG000216890.
InParanoidiO07637.
KOiK01425.
OMAiTKQCAIE.
OrthoDBiEOG6N94BK.
PhylomeDBiO07637.

Enzyme and pathway databases

BioCyciBSUB:BSU14830-MONOMER.

Miscellaneous databases

PROiO07637.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiGLSA2_BACSU
AccessioniPrimary (citable) accession number: O07637
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: January 7, 2015
This is version 93 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

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.