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 1

Gene

glsA1

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Kineticsi

  1. KM=27.6 mM for glutamine1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei74 – 741Substrate
Binding sitei126 – 1261Substrate
Binding sitei170 – 1701Substrate
Binding sitei177 – 1771Substrate
Binding sitei201 – 2011Substrate
Binding sitei253 – 2531Substrate
Binding sitei271 – 2711Substrate; via amide nitrogen

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:BSU02430-MONOMER.
BRENDAi3.5.1.2. 658.
4.3.3.6. 658.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutaminase 1 (EC:3.5.1.2)
Gene namesi
Name:glsA1
Synonyms:glsA, ybgJ
Ordered Locus Names:BSU02430
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU02430. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 327327Glutaminase 1PRO_0000110594Add
BLAST

Proteomic databases

PaxDbiO31465.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi224308.BSU02430.

Structurei

Secondary structure

1
327
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 2512Combined sources
Helixi26 – 316Combined sources
Helixi39 – 424Combined sources
Beta strandi50 – 545Combined sources
Beta strandi60 – 656Combined sources
Helixi73 – 753Combined sources
Helixi76 – 8813Combined sources
Helixi90 – 945Combined sources
Helixi110 – 1145Combined sources
Beta strandi123 – 1253Combined sources
Helixi126 – 13510Combined sources
Beta strandi136 – 1405Combined sources
Helixi141 – 15616Combined sources
Helixi164 – 17310Combined sources
Helixi175 – 18612Combined sources
Helixi194 – 20512Combined sources
Beta strandi207 – 2093Combined sources
Helixi211 – 22212Combined sources
Turni223 – 2253Combined sources
Turni228 – 2314Combined sources
Helixi237 – 25014Combined sources
Helixi253 – 2553Combined sources
Helixi256 – 2627Combined sources
Beta strandi267 – 2693Combined sources
Beta strandi273 – 2797Combined sources
Turni281 – 2844Combined sources
Turni288 – 2914Combined sources
Beta strandi293 – 2986Combined sources
Beta strandi306 – 3083Combined sources
Helixi309 – 32214Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MKIX-ray2.00A/B1-327[»]
2OSUX-ray2.29A/B1-327[»]
3AGFX-ray2.60A/B1-327[»]
3BRMX-ray2.29A/B1-327[»]
ProteinModelPortaliO31465.
SMRiO31465. Positions 1-327.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO31465.

Family & Domainsi

Sequence similaritiesi

Belongs to the glutaminase family.Curated

Phylogenomic databases

eggNOGiCOG2066.
HOGENOMiHOG000216890.
InParanoidiO31465.
KOiK01425.
OMAiISKAFVF.
OrthoDBiEOG6N94BK.
PhylomeDBiO31465.

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.

O31465-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKELIKEHQK DINPALQLHD WVEYYRPFAA NGQSANYIPA LGKVNDSQLG
60 70 80 90 100
ICVLEPDGTM IHAGDWNVSF TMQSISKVIS FIAACMSRGI PYVLDRVDVE
110 120 130 140 150
PTGDAFNSII RLEINKPGKP FNPMINAGAL TIASILPGES AYEKLEFLYS
160 170 180 190 200
VMETLIGKRP RIHEEVFRSE WETAHRNRAL AYYLKETNFL EAEVEETLEV
210 220 230 240 250
YLKQCAMEST TEDIALIGLI LAHDGYHPIR HEQVIPKDVA KLAKALMLTC
260 270 280 290 300
GMYNASGKYA AFVGVPAKSG VSGGIMALVP PSARREQPFQ SGCGIGIYGP
310 320
AIDEYGNSLT GGMLLKHMAQ EWELSIF
Length:327
Mass (Da):36,187
Last modified:December 31, 1997 - v1
Checksum:iBE3A1C2366460287
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB006424 Genomic DNA. Translation: BAA33141.1.
AL009126 Genomic DNA. Translation: CAB12037.1.
PIRiD69751.
RefSeqiNP_388125.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB12037; CAB12037; BSU02430.
GeneIDi938416.
KEGGibsu:BSU02430.
PATRICi18972037. VBIBacSub10457_0247.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB006424 Genomic DNA. Translation: BAA33141.1.
AL009126 Genomic DNA. Translation: CAB12037.1.
PIRiD69751.
RefSeqiNP_388125.1. NC_000964.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MKIX-ray2.00A/B1-327[»]
2OSUX-ray2.29A/B1-327[»]
3AGFX-ray2.60A/B1-327[»]
3BRMX-ray2.29A/B1-327[»]
ProteinModelPortaliO31465.
SMRiO31465. Positions 1-327.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU02430.

Proteomic databases

PaxDbiO31465.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12037; CAB12037; BSU02430.
GeneIDi938416.
KEGGibsu:BSU02430.
PATRICi18972037. VBIBacSub10457_0247.

Organism-specific databases

GenoListiBSU02430. [Micado]

Phylogenomic databases

eggNOGiCOG2066.
HOGENOMiHOG000216890.
InParanoidiO31465.
KOiK01425.
OMAiISKAFVF.
OrthoDBiEOG6N94BK.
PhylomeDBiO31465.

Enzyme and pathway databases

BioCyciBSUB:BSU02430-MONOMER.
BRENDAi3.5.1.2. 658.
4.3.3.6. 658.

Miscellaneous databases

EvolutionaryTraceiO31465.
PROiO31465.

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. "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 (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(1996) [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(2004) [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(2007) [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.

Entry informationi

Entry nameiGLSA1_BACSU
AccessioniPrimary (citable) accession number: O31465
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2001
Last sequence update: December 31, 1997
Last modified: March 31, 2015
This is version 105 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. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  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

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.