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Q59747 (GLNA1_RHIME) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 90. 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:
Glutamine synthetase 1

EC=6.3.1.2
Alternative name(s):
Glutamate--ammonia ligase I
Glutamine synthetase I
Short name=GSI
Gene names
Name:glnA
Ordered Locus Names:R01640
ORF Names:SMc00948
OrganismRhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) [Complete proteome] [HAMAP]
Taxonomic identifier266834 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium

Protein attributes

Sequence length469 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine.

Enzyme regulation

The activity of this enzyme is controlled by adenylation under conditions of abundant glutamine. The fully adenylated enzyme complex is inactive By similarity.

Subunit structure

Oligomer of 12 subunits arranged in the form of two hexagons By similarity.

Subcellular location

Cytoplasm.

Miscellaneous

Two forms of glutamine synthetase (GSI and GSII) can be found in this nitrogen fixing bacteria, GSI is a typical prokaryotic glutamine synthetase whereas GSII is similar to the eukaryotic enzyme.

Sequence similarities

Belongs to the glutamine synthetase family.

Ontologies

Keywords
   Biological processNitrogen fixation
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglutamine biosynthetic process

Inferred from electronic annotation. Source: InterPro

nitrogen fixation

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate-ammonia ligase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 469469Glutamine synthetase 1
PRO_0000153225

Amino acid modifications

Modified residue3981O-AMP-tyrosine By similarity

Experimental info

Sequence conflict354 – 3563AKR → PNG in AAC44624. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q59747 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: FD1516B434FDF7A3

FASTA46952,122
        10         20         30         40         50         60 
MTTANEVLKQ IKENDVKFVD LRFTDPKGKL QHVTMDVVCV DEDMFADGVM FDGSSIGGWK 

        70         80         90        100        110        120 
AINESDMVLM PDPETAHMDP FFAQSTMVIF CDILDPVSGE AYNRDPRGTA KKAEAYLKAS 

       130        140        150        160        170        180 
GIGDTVFVGP EAEFFVFDDV KYKADPYNTG FKLDSSELPS NDDTDYETGN LGHRPRVKGG 

       190        200        210        220        230        240 
YFPVPPVDSS QDMRSEMLTV LSEMGVTVEK HHHEVAAAQH ELGVKFDALV RNADKMQIYK 

       250        260        270        280        290        300 
YVVHQVANAY GKTATFMPKP IFGDNGSGMH VHLSIWKDGK PTFAGDEYAG LSESCLYFIG 

       310        320        330        340        350        360 
GIIKHAKALN AFTNPSTNSY KRLVPGYEAP VLLAYSARNR SASCRIPFGT NPKAKRVEVR 

       370        380        390        400        410        420 
FPDPTANPYL AFAAMLMAGL DGIKNKLHPG KAMDKDLYDL PPKELKKIPT VCGSLREALE 

       430        440        450        460 
SLDKDRKFLT AGGVFDDDQI DSFIELKMQE VMRFEMTPHP VEFDMYYSV 

« Hide

References

« Hide 'large scale' references
[1]"Symbiotic nitrogen fixation does not require adenylylation of glutamine synthetase I in Rhizobium meliloti."
Arcondeguy T., Huez I., Fourment J., Kahn D.
FEMS Microbiol. Lett. 145:33-40(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: RCR2011 / SU47.
[2]"Analysis of the chromosome sequence of the legume symbiont Sinorhizobium meliloti strain 1021."
Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D. expand/collapse author list , Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F.
Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1021.
[3]"The composite genome of the legume symbiont Sinorhizobium meliloti."
Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., Cowie A. expand/collapse author list , Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S., Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I., Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S., Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C., Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R., Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H., Wong K., Yeh K.-C., Batut J.
Science 293:668-672(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1021.
[4]"The glutamine synthetases of rhizobia: phylogenetics and evolutionary implications."
Turner S.L., Young J.P.W.
Mol. Biol. Evol. 17:309-319(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 49-362.
Strain: ATCC 9930 / USDA 1002 / DSM 30135 / JCM 20682 / LMG 6133 / NBRC 14782 / NRRL L-45.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U50385 Genomic DNA. Translation: AAC44624.1.
AL591688 Genomic DNA. Translation: CAC46219.1.
AF169573 Genomic DNA. Translation: AAF18968.1.
RefSeqNP_385746.1. NC_003047.1.

3D structure databases

ProteinModelPortalQ59747.
SMRQ59747. Positions 3-469.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266834.SMc00948.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC46219; CAC46219; SMc00948.
GeneID1233299.
KEGGsme:SMc00948.
PATRIC23632655. VBISinMel96828_3073.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0174.
HOGENOMHOG000005157.
KOK01915.
OMARAHHEVG.
OrthoDBEOG6B360N.
ProtClustDBCLSK862961.

Enzyme and pathway databases

BioCycSMEL266834:GJF6-1681-MONOMER.

Family and domain databases

Gene3D3.10.20.70. 1 hit.
3.30.590.10. 1 hit.
InterProIPR008147. Gln_synt_beta.
IPR014746. Gln_synth/guanido_kin_cat_dom.
IPR008146. Gln_synth_cat_dom.
IPR027303. Gln_synth_gly_rich_site.
IPR004809. Gln_synth_I.
IPR001637. Gln_synth_I_adenylation_site.
IPR027302. Gln_synth_N_conserv_site.
[Graphical view]
PfamPF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
[Graphical view]
SUPFAMSSF54368. SSF54368. 1 hit.
TIGRFAMsTIGR00653. GlnA. 1 hit.
PROSITEPS00180. GLNA_1. 1 hit.
PS00182. GLNA_ADENYLATION. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLNA1_RHIME
AccessionPrimary (citable) accession number: Q59747
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 30, 2000
Last modified: November 13, 2013
This is version 90 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