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Protein

Glutamine synthetase 3

Gene

glnT

Organism
Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine.1 Publication

Cofactori

Mg2+1 Publication

Enzyme regulationi

Inhibited by methionine sulfoximine, ADP and pyrophosphate, but not by various nitrogen-containing metabolites that inhibit other GS enzymes.1 Publication

Kineticsi

  1. KM=13.3 mM for glutamate1 Publication
  2. KM=33 mM for ammonium1 Publication

pH dependencei

Optimum pH is 6.8.1 Publication

Temperature dependencei

Optimum temperature is 50 degrees Celsius.1 Publication

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, Magnesium, Nucleotide-binding

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-6286-MONOMER.
SMEL266834:GJF6-96-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamine synthetase 31 Publication (EC:6.3.1.21 Publication)
Alternative name(s):
Glutamate--ammonia ligase IIICurated
Glutamine synthetase III1 Publication
Short name:
GSIII1 Publication
Gene namesi
Name:glnT1 Publication
Ordered Locus Names:R00090
ORF Names:SMc02613
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-SubCell
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 435435Glutamine synthetase 3PRO_0000153227Add
BLAST

Interactioni

Subunit structurei

Homooctamer.1 Publication

Protein-protein interaction databases

STRINGi266834.SMc02613.

Structurei

3D structure databases

ProteinModelPortaliO87393.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0174.
HOGENOMiHOG000005156.
KOiK01915.
OMAiTQWERDS.
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.
IPR017536. Glutamine_synthetase_typeIII.
[Graphical view]
PfamiPF00120. Gln-synt_C. 1 hit.
[Graphical view]
SUPFAMiSSF54368. SSF54368. 1 hit.
TIGRFAMsiTIGR03105. gln_synth_III. 1 hit.
PROSITEiPS00181. GLNA_ATP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O87393-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLDLSTFAR EKGVKYFMIS YTDLFGGQRA KLVPAEAIAD MQKGGAGFAG
60 70 80 90 100
FATWFDLTPA HPDLFALPDA SAVIQLPWKK DVAWVAADCI MDDAPVEQAP
110 120 130 140 150
RVVLKKLVAE AAQEGLRVKT GVEPEFFLIS PDGSKISDTF DTAEKPCYDQ
160 170 180 190 200
QAIMRRYDVI AEICDYMLEL GWKPYQNDHE DANGQFEMNW EYDDALRTAD
210 220 230 240 250
KHSFFKFMVK SIAEKHGLRA TFMPKPFKGL TGNGCHCHIS VWDLAGEVNA
260 270 280 290 300
FADNKAEFGL SAEGRHFLGG IMKHASALAA VTNPTVNSYK RINAPRTISG
310 320 330 340 350
ATWAPNSVTW TGNNRTHMVR VPGPGRFELR LPDGAVNPYL LQAIIIAAGL
360 370 380 390 400
SGVRSKADPG RHYDIDMYKD GHKVTDAPKL PLNLLDALRE YNRDEELQEA
410 420 430
LGREFSAAYL KLKQGEWNTY CSQFTEWEHQ TTLDV
Length:435
Mass (Da):48,481
Last modified:November 1, 1998 - v1
Checksum:i90DE8275496E5400
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF055582 Genomic DNA. Translation: AAC62223.1.
AL591688 Genomic DNA. Translation: CAC41477.1.
RefSeqiNP_384196.1. NC_003047.1.
WP_003532529.1. NC_003047.1.

Genome annotation databases

EnsemblBacteriaiCAC41477; CAC41477; SMc02613.
GeneIDi1231721.
KEGGisme:SMc02613.
PATRICi23629349. VBISinMel96828_1447.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF055582 Genomic DNA. Translation: AAC62223.1.
AL591688 Genomic DNA. Translation: CAC41477.1.
RefSeqiNP_384196.1. NC_003047.1.
WP_003532529.1. NC_003047.1.

3D structure databases

ProteinModelPortaliO87393.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi266834.SMc02613.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC41477; CAC41477; SMc02613.
GeneIDi1231721.
KEGGisme:SMc02613.
PATRICi23629349. VBISinMel96828_1447.

Phylogenomic databases

eggNOGiCOG0174.
HOGENOMiHOG000005156.
KOiK01915.
OMAiTQWERDS.
OrthoDBiEOG6B360N.

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-6286-MONOMER.
SMEL266834:GJF6-96-MONOMER.

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.
IPR017536. Glutamine_synthetase_typeIII.
[Graphical view]
PfamiPF00120. Gln-synt_C. 1 hit.
[Graphical view]
SUPFAMiSSF54368. SSF54368. 1 hit.
TIGRFAMsiTIGR03105. gln_synth_III. 1 hit.
PROSITEiPS00181. GLNA_ATP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Powers E.L., Vuyyuru V., Kahn M.L.
    Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 1021.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 1021.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 1021.
  4. "Isolation and characterization of a novel glutamine synthetase from Rhizobium meliloti."
    Shatters R.G., Liu Y., Kahn M.L.
    J. Biol. Chem. 268:469-475(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    Strain: 104A14.

Entry informationi

Entry nameiGLNA3_RHIME
AccessioniPrimary (citable) accession number: O87393
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1998
Last modified: February 4, 2015
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Can grow, in the absence of GSI and GSII glutamine synthetases, without a glutamine supplement in minimal medium that contains both ammonium and glutamate. However, given the high glutamate and ammonium substrate Km values, glutamine synthase is probably a secondary activity of GlnT.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.