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Q9LVI8 (GLN13_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 cytosolic isozyme 1-3

Short name=GS1
EC=6.3.1.2
Alternative name(s):
Glutamate--ammonia ligase GLN1;3
Short name=GLN1;3
Gene names
Name:GLN1-3
Ordered Locus Names:At3g17820
ORF Names:MEB5.4
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length354 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Low-affinity glutamine synthetase. May contribute to the homeostatic control of glutamine synthesis in roots.

Catalytic activity

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

Subunit structure

Homooctamer By similarity.

Subcellular location

Cytoplasm.

Tissue specificity

Expressed in the pericycle in the region of mature root. Ref.7

Induction

By sucrose, glucose and fructose. Down-regulated by ammonium supply. Ref.6 Ref.7

Sequence similarities

Belongs to the glutamine synthetase family.

Biophysicochemical properties

Kinetic parameters:

Measured at pH 7.8 and 30 degrees Celsius for all experiments.

KM=3.9 mM for glutamate Ref.7

KM=1210 µM for ammonium

KM=850 µM for ATP

Vmax=162 nmol/sec/mg enzyme with glutamate as substrate

Vmax=93.9 nmol/sec/mg enzyme with ammonium as substrate

Vmax=100 nmol/sec/mg enzyme with ATP as substrate

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 354353Glutamine synthetase cytosolic isozyme 1-3
PRO_0000153168

Amino acid modifications

Modified residue21N-acetylserine Ref.9
Modified residue21Phosphoserine By similarity
Modified residue481Phosphoserine By similarity

Experimental info

Mutagenesis491K → Q: 3-fold increase in affinity for ammonium and catalytic efficiency. Ref.8
Mutagenesis1741A → S: 4-fold increase in affinity for ammonium and catalytic efficiency. Ref.8
Sequence conflict851G → D in AAO42253. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9LVI8 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 750441568FA1D7B9

FASTA35438,595
        10         20         30         40         50         60 
MSLLSDLVNL NLTDATGKII AEYIWIGGSG MDIRSKARTL PGPVTDPSKL PKWNYDGSST 

        70         80         90        100        110        120 
GQAAGEDSEV ILYPQAIFKD PFRKGNNILV MCDAYTPAGD PIPTNKRHNA AKIFSHPDVA 

       130        140        150        160        170        180 
KEEPWYGIEQ EYTLMQKDVN WPIGWPVGGY PGPQGPYYCG VGADKAIGRD IVDAHYKACL 

       190        200        210        220        230        240 
YAGIGISGIN GEVMPGQWEF QVGPVEGISS GDQVWVARYL LERITEISGV IVSFDPKPVP 

       250        260        270        280        290        300 
GDWNGAGAHC NYSTKTMRND GGLEVIKKAI GKLQLKHKEH IAAYGEGNER RLTGKHETAD 

       310        320        330        340        350 
INTFSWGVAN RGASVRVGRD TEKEGKGYFE DRRPASNMDP YVVTSMIAET TILG 

« Hide

References

« Hide 'large scale' references
[1]"Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones."
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.
DNA Res. 7:131-135(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"Arabidopsis ORF clones."
Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[6]"Carbon and amino acids reciprocally modulate the expression of glutamine synthetase in Arabidopsis."
Oliveira I.C., Coruzzi G.M.
Plant Physiol. 121:301-310(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[7]"Kinetic properties and ammonium-dependent regulation of cytosolic isoenzymes of glutamine synthetase in Arabidopsis."
Ishiyama K., Inoue E., Watanabe-Takahashi A., Obara M., Yamaya T., Takahashi H.
J. Biol. Chem. 279:16598-16605(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, INDUCTION.
[8]"Gln49 and Ser174 residues play critical roles in determining the catalytic efficiencies of plant glutamine synthetase."
Ishiyama K., Inoue E., Yamaya T., Takahashi H.
Plant Cell Physiol. 47:299-303(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF LYS-49 AND ALA-174.
[9]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB019230 Genomic DNA. Translation: BAB02705.1.
CP002686 Genomic DNA. Translation: AEE76011.1.
BT004249 mRNA. Translation: AAO42253.1.
AY088312 mRNA. Translation: AAM65851.1.
BT020327 mRNA. Translation: AAV85682.1.
BT020432 mRNA. Translation: AAW28559.1.
RefSeqNP_188409.1. NM_112663.2.
UniGeneAt.26821.

3D structure databases

ProteinModelPortalQ9LVI8.
SMRQ9LVI8. Positions 4-353.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid6383. 1 interaction.

Proteomic databases

PaxDbQ9LVI8.
PRIDEQ9LVI8.

Protocols and materials databases

DNASU821050.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G17820.1; AT3G17820.1; AT3G17820.
GeneID821050.
KEGGath:AT3G17820.

Organism-specific databases

TAIRAT3G17820.

Phylogenomic databases

eggNOGCOG0174.
HOGENOMHOG000061500.
InParanoidQ9LVI8.
KOK01915.
OMAIASFDCK.
PhylomeDBQ9LVI8.
ProtClustDBPLN02284.

Enzyme and pathway databases

BRENDA6.3.1.2. 399.
SABIO-RKQ9LVI8.

Gene expression databases

ArrayExpressQ9LVI8.
GenevestigatorQ9LVI8.

Family and domain databases

Gene3D3.30.590.10. 1 hit.
InterProIPR008147. Gln_synt_beta.
IPR014746. Gln_synth/guanido_kin_cat_dom.
IPR008146. Gln_synth_cat_dom.
IPR027303. Gln_synth_gly_rich_site.
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.
PROSITEPS00180. GLNA_1. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLN13_ARATH
AccessionPrimary (citable) accession number: Q9LVI8
Secondary accession number(s): Q5PNX0, Q84W44
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names