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Q59747

- GLNA1_RHIME

UniProt

Q59747 - GLNA1_RHIME

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Protein

Glutamine synthetase 1

Gene

glnA

Organism
Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Catalytic activityi

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

Enzyme regulationi

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. glutamate-ammonia ligase activity Source: UniProtKB-EC

GO - Biological processi

  1. glutamine biosynthetic process Source: InterPro
  2. nitrogen fixation Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Nitrogen fixation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciSMEL266834:GJF6-1681-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamine synthetase 1 (EC:6.3.1.2)
Alternative name(s):
Glutamate--ammonia ligase I
Glutamine synthetase I
Short name:
GSI
Gene namesi
Name:glnA
Ordered Locus Names:R01640
ORF Names:SMc00948
OrganismiRhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Taxonomic identifieri266834 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium
ProteomesiUP000001976: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 469469Glutamine synthetase 1PRO_0000153225Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei398 – 3981O-AMP-tyrosineBy similarity

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi266834.SMc00948.

Structurei

3D structure databases

ProteinModelPortaliQ59747.
SMRiQ59747. Positions 3-469.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glutamine synthetase family.Curated

Phylogenomic databases

eggNOGiCOG0174.
HOGENOMiHOG000005157.
KOiK01915.
OMAiDMLLMPI.
OrthoDBiEOG6B360N.

Family and domain databases

Gene3Di3.10.20.70. 1 hit.
3.30.590.10. 1 hit.
InterProiIPR008147. 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]
PfamiPF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
[Graphical view]
SUPFAMiSSF54368. SSF54368. 1 hit.
TIGRFAMsiTIGR00653. GlnA. 1 hit.
PROSITEiPS00180. GLNA_1. 1 hit.
PS00182. GLNA_ADENYLATION. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q59747-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTTANEVLKQ IKENDVKFVD LRFTDPKGKL QHVTMDVVCV DEDMFADGVM
60 70 80 90 100
FDGSSIGGWK AINESDMVLM PDPETAHMDP FFAQSTMVIF CDILDPVSGE
110 120 130 140 150
AYNRDPRGTA KKAEAYLKAS GIGDTVFVGP EAEFFVFDDV KYKADPYNTG
160 170 180 190 200
FKLDSSELPS NDDTDYETGN LGHRPRVKGG YFPVPPVDSS QDMRSEMLTV
210 220 230 240 250
LSEMGVTVEK HHHEVAAAQH ELGVKFDALV RNADKMQIYK YVVHQVANAY
260 270 280 290 300
GKTATFMPKP IFGDNGSGMH VHLSIWKDGK PTFAGDEYAG LSESCLYFIG
310 320 330 340 350
GIIKHAKALN AFTNPSTNSY KRLVPGYEAP VLLAYSARNR SASCRIPFGT
360 370 380 390 400
NPKAKRVEVR FPDPTANPYL AFAAMLMAGL DGIKNKLHPG KAMDKDLYDL
410 420 430 440 450
PPKELKKIPT VCGSLREALE SLDKDRKFLT AGGVFDDDQI DSFIELKMQE
460
VMRFEMTPHP VEFDMYYSV
Length:469
Mass (Da):52,122
Last modified:May 30, 2000 - v2
Checksum:iFD1516B434FDF7A3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti354 – 3563AKR → PNG in AAC44624. (PubMed:8931324)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U50385 Genomic DNA. Translation: AAC44624.1.
AL591688 Genomic DNA. Translation: CAC46219.1.
AF169573 Genomic DNA. Translation: AAF18968.1.
RefSeqiNP_385746.1. NC_003047.1.

Genome annotation databases

EnsemblBacteriaiCAC46219; CAC46219; SMc00948.
GeneIDi1233299.
KEGGisme:SMc00948.
PATRICi23632655. VBISinMel96828_3073.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U50385 Genomic DNA. Translation: AAC44624.1 .
AL591688 Genomic DNA. Translation: CAC46219.1 .
AF169573 Genomic DNA. Translation: AAF18968.1 .
RefSeqi NP_385746.1. NC_003047.1.

3D structure databases

ProteinModelPortali Q59747.
SMRi Q59747. Positions 3-469.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 266834.SMc00948.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAC46219 ; CAC46219 ; SMc00948 .
GeneIDi 1233299.
KEGGi sme:SMc00948.
PATRICi 23632655. VBISinMel96828_3073.

Phylogenomic databases

eggNOGi COG0174.
HOGENOMi HOG000005157.
KOi K01915.
OMAi DMLLMPI.
OrthoDBi EOG6B360N.

Enzyme and pathway databases

BioCyci SMEL266834:GJF6-1681-MONOMER.

Family and domain databases

Gene3Di 3.10.20.70. 1 hit.
3.30.590.10. 1 hit.
InterProi IPR008147. 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 ]
Pfami PF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
[Graphical view ]
SUPFAMi SSF54368. SSF54368. 1 hit.
TIGRFAMsi TIGR00653. GlnA. 1 hit.
PROSITEi PS00180. GLNA_1. 1 hit.
PS00182. GLNA_ADENYLATION. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 1021.
  3. 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.

Entry informationi

Entry nameiGLNA1_RHIME
AccessioniPrimary (citable) accession number: Q59747
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 30, 2000
Last modified: October 29, 2014
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3