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O31465

- GLSA1_BACSU

UniProt

O31465 - GLSA1_BACSU

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Protein

Glutaminase 1

Gene
glsA1, glsA, ybgJ, BSU02430
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - 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.

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: Chromosome

Organism-specific databases

GenoListiBSU02430. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 327327Glutaminase 1UniRule annotationPRO_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 – 2512
Helixi26 – 316
Helixi39 – 424
Beta strandi50 – 545
Beta strandi60 – 656
Helixi73 – 753
Helixi76 – 8813
Helixi90 – 945
Helixi110 – 1145
Beta strandi123 – 1253
Helixi126 – 13510
Beta strandi136 – 1405
Helixi141 – 15616
Helixi164 – 17310
Helixi175 – 18612
Helixi194 – 20512
Beta strandi207 – 2093
Helixi211 – 22212
Turni223 – 2253
Turni228 – 2314
Helixi237 – 25014
Helixi253 – 2553
Helixi256 – 2627
Beta strandi267 – 2693
Beta strandi273 – 2797
Turni281 – 2844
Turni288 – 2914
Beta strandi293 – 2986
Beta strandi306 – 3083
Helixi309 – 32214

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiO31465.

Family & Domainsi

Sequence similaritiesi

Belongs to the glutaminase family.

Phylogenomic databases

eggNOGiCOG2066.
HOGENOMiHOG000216890.
KOiK01425.
OMAiSANYIPA.
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

MKELIKEHQK DINPALQLHD WVEYYRPFAA NGQSANYIPA LGKVNDSQLG    50
ICVLEPDGTM IHAGDWNVSF TMQSISKVIS FIAACMSRGI PYVLDRVDVE 100
PTGDAFNSII RLEINKPGKP FNPMINAGAL TIASILPGES AYEKLEFLYS 150
VMETLIGKRP RIHEEVFRSE WETAHRNRAL AYYLKETNFL EAEVEETLEV 200
YLKQCAMEST TEDIALIGLI LAHDGYHPIR HEQVIPKDVA KLAKALMLTC 250
GMYNASGKYA AFVGVPAKSG VSGGIMALVP PSARREQPFQ SGCGIGIYGP 300
AIDEYGNSLT GGMLLKHMAQ EWELSIF 327
Length:327
Mass (Da):36,187
Last modified:January 1, 1998 - v1
Checksum:iBE3A1C2366460287
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AB006424 Genomic DNA. Translation: BAA33141.1 .
AL009126 Genomic DNA. Translation: CAB12037.1 .
PIRi D69751.
RefSeqi NP_388125.1. NC_000964.3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MKI X-ray 2.00 A/B 1-327 [» ]
2OSU X-ray 2.29 A/B 1-327 [» ]
3AGF X-ray 2.60 A/B 1-327 [» ]
3BRM X-ray 2.29 A/B 1-327 [» ]
ProteinModelPortali O31465.
SMRi O31465. Positions 1-327.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU02430.

Proteomic databases

PaxDbi O31465.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB12037 ; CAB12037 ; BSU02430 .
GeneIDi 938416.
KEGGi bsu:BSU02430.
PATRICi 18972037. VBIBacSub10457_0247.

Organism-specific databases

GenoListi BSU02430. [Micado ]

Phylogenomic databases

eggNOGi COG2066.
HOGENOMi HOG000216890.
KOi K01425.
OMAi SANYIPA.
OrthoDBi EOG6N94BK.
PhylomeDBi O31465.

Enzyme and pathway databases

BioCyci BSUB:BSU02430-MONOMER.

Miscellaneous databases

EvolutionaryTracei O31465.
PROi O31465.

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 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.
    , 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.

Entry informationi

Entry nameiGLSA1_BACSU
AccessioniPrimary (citable) accession number: O31465
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 100 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

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