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Q8NMT3 (GLSA_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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

EC=3.5.1.2
Gene names
Name:glsA
Ordered Locus Names:Cgl2482, cg2728
OrganismCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025) [Reference proteome] [HAMAP]
Taxonomic identifier196627 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length413 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

L-glutamine + H2O = L-glutamate + NH3. HAMAP-Rule MF_00313

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00313

Sequence similarities

Belongs to the glutaminase family.

Contains 1 STAS domain.

Sequence caution

The sequence BAB99875.1 differs from that shown. Reason: Erroneous initiation.

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: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 413413Glutaminase HAMAP-Rule MF_00313
PRO_0000110606

Regions

Domain316 – 41398STAS
Region23 – 307285Glutaminase HAMAP-Rule MF_00313

Sites

Binding site651Substrate By similarity
Binding site1141Substrate By similarity
Binding site1601Substrate By similarity
Binding site1671Substrate By similarity
Binding site1911Substrate By similarity
Binding site2431Substrate By similarity
Binding site2611Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8NMT3 [UniParc].

Last modified May 24, 2004. Version 2.
Checksum: 91ADD397B9FFE473

FASTA41344,748
        10         20         30         40         50         60 
MLTMPIPEYL HEILDDVRDT TSGELADYIP ELKSADPNPL AVALCTVNGH IYSAGDDDIE 

        70         80         90        100        110        120 
FTMQSISKPF AYALALQECG FDEVSASVAL EPSGEAFNEL SLDGENRPMN PMINAGAIAI 

       130        140        150        160        170        180 
NQLINGSDST VEDRVEKIRH YFSELAGREL TIDRVLAESE LAGADRNLSI AHMLRNYGVI 

       190        200        210        220        230        240 
EDEAHDAVLS YTLQCAIKVT TRDLAVMTAT LAAGGTHPIT GKKLLDARVC RLTLSVMASA 

       250        260        270        280        290        300 
GMYDEAGQWL STVGIPAKSG VAGGLIGILP GQLGIATFSP RLNPKGNSVR GVKIFKQLSD 

       310        320        330        340        350        360 
DMGLHLMSTE QVSGHAVRSI TRDGDTTFIQ MQGAMNFSAS ESFLHAIVEH NFEGTEVVLD 

       370        380        390        400        410 
LTRVLSFHPV AIRMIKEGLK RIRDAGFEVF ILDPDDVLPD FMFSDGTICK ERV 

« Hide

References

[1]"The Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
Ikeda M., Nakagawa S.
Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000036 Genomic DNA. Translation: BAB99875.1. Different initiation.
BX927155 Genomic DNA. Translation: CAF21143.1.
RefSeqNP_601682.1. NC_003450.3.
YP_226722.1. NC_006958.1.

3D structure databases

ProteinModelPortalQ8NMT3.
SMRQ8NMT3. Positions 3-349.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING196627.cg2728.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB99875; BAB99875; BAB99875.
CAF21143; CAF21143; cg2728.
GeneID1020428.
3342801.
KEGGcgb:cg2728.
cgl:NCgl2395.
PATRIC21496976. VBICorGlu203724_2414.

Phylogenomic databases

eggNOGCOG2066.
HOGENOMHOG000216890.
KOK01425.
OMAMGLHLMS.
OrthoDBEOG6N94BK.
ProtClustDBPRK00971.

Family and domain databases

Gene3D3.30.750.24. 1 hit.
3.40.710.10. 1 hit.
HAMAPMF_00313. Glutaminase.
InterProIPR012338. Beta-lactam/transpept-like.
IPR015868. Glutaminase.
IPR002645. STAS_dom.
[Graphical view]
PANTHERPTHR12544. PTHR12544. 1 hit.
PfamPF04960. Glutaminase. 1 hit.
[Graphical view]
SUPFAMSSF52091. SSF52091. 1 hit.
SSF56601. SSF56601. 1 hit.
TIGRFAMsTIGR03814. Gln_ase. 1 hit.
PROSITEPS50801. STAS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLSA_CORGL
AccessionPrimary (citable) accession number: Q8NMT3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: May 24, 2004
Last modified: February 19, 2014
This is version 66 of the entry and version 2 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