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Q7NQH9 (GLSA_CHRVO) 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 attributes

Sequence length304 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.

Ontologies

Keywords
   Molecular functionHydrolase
   Technical termComplete 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 – 304304Glutaminase HAMAP-Rule MF_00313
PRO_0000110601

Sites

Binding site631Substrate By similarity
Binding site1131Substrate By similarity
Binding site1571Substrate By similarity
Binding site1641Substrate By similarity
Binding site1881Substrate By similarity
Binding site2401Substrate By similarity
Binding site2581Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7NQH9 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: A267C6E0E5BE47DC

FASTA30432,747
        10         20         30         40         50         60 
MNLQALIEDI RQQVLPFYDQ GRVADYIPAL ASVPPHQFGI AIHTLDGREH ACGDADTPFS 

        70         80         90        100        110        120 
IQSISKAFML ALTLQADGEQ LWRHVGKEPS GNPFNSLVQL EYEHGIPRNP FINAGALVVT 

       130        140        150        160        170        180 
DRAIGHFGDA HARLLAWLRE ETGNAGLMAD QAIAASERAH GDRNAALAHF MKSYGNLGHP 

       190        200        210        220        230        240 
VETVLDQYFH NCSIAMSCRE LARAGLFLAN HGLSPQTGTQ YLSRSQAKQV NAVMLTCGTY 

       250        260        270        280        290        300 
DAAGEFAYRV GLPVKSGVGG GLLAVIPGKM AIAAWSPQLD ARGNSVLGLE ALDRFTTRTG 


LSIF 

« Hide

References

[1]"The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability."
Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A. expand/collapse author list , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.
Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016825 Genomic DNA. Translation: AAQ61819.1.
RefSeqNP_903828.1. NC_005085.1.

3D structure databases

ProteinModelPortalQ7NQH9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243365.CV_4158.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAQ61819; AAQ61819; CV_4158.
GeneID2549795.
KEGGcvi:CV_4158.
PATRIC21443145. VBIChrVio67196_4072.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2066.
HOGENOMHOG000216890.
KOK01425.
OMARINALML.
OrthoDBEOG6N94BK.
ProtClustDBPRK00971.

Enzyme and pathway databases

BioCycCVIO243365:GHUD-4269-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. SSF56601. 1 hit.
TIGRFAMsTIGR03814. Gln_ase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGLSA_CHRVO
AccessionPrimary (citable) accession number: Q7NQH9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: December 15, 2003
Last modified: February 19, 2014
This is version 66 of the entry and version 1 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