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Q9FMD9 (GLN14_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 81. 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 1-4

EC=6.3.1.2
Alternative name(s):
Glutamate--ammonia ligase GLN1;4
Short name=GLN1;4
Gene names
Name:GLN1-4
Ordered Locus Names:At5g16570
ORF Names:MTG13.1
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length356 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

High-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 lateral root emergence. Ref.4

Induction

Down-regulated by ammonium supply. Ref.4

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=0.6 mM for glutamate Ref.4

KM=48 µM for ammonium

KM=400 µM for ATP

Vmax=79.2 nmol/sec/mg enzyme with glutamate as substrate

Vmax=65.7 nmol/sec/mg enzyme with ammonium as substrate

Vmax=73.9 nmol/sec/mg enzyme with ATP as substrate

Ontologies

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

Inferred from electronic annotation. Source: InterPro

nitrate assimilation

Traceable author statement Ref.5. Source: TAIR

nitrogen fixation

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytosol

Non-traceable author statement Ref.5. Source: TAIR

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate-ammonia ligase activity

Inferred from direct assay Ref.4. Source: TAIR

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 356355Glutamine synthetase cytosolic isozyme 1-4
PRO_0000239820

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue21Phosphoserine By similarity
Modified residue481Phosphoserine By similarity

Experimental info

Mutagenesis491Q → K: 6-fold decrease in affinity for ammonium and catalytic efficiency; when associated with A-174. Ref.5
Mutagenesis1741S → A: 6-fold decrease in affinity for ammonium and catalytic efficiency; when associated with K-49. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9FMD9 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: A8F39CE8835592D4

FASTA35638,987
        10         20         30         40         50         60 
MSSLADLINL DLSDSTDQII AEYIWIGGSG LDMRSKARTL PGPVTDPSQL PKWNYDGSST 

        70         80         90        100        110        120 
GQAPGDDSEV IIYPQAIFKD PFRRGNNILV MCDAYTPAGE PIPTNKRHAA AKIFEDPSVV 

       130        140        150        160        170        180 
AEETWYGIEQ EYTLLQKDIK WPVGWPVGGF PGPQGPYYCG VGADKAFGRD IVDSHYKACL 

       190        200        210        220        230        240 
YAGINVSGTN GEVMPGQWEF QVGPTVGIAA ADQVWVARYI LERITELAGV VLSLDPKPIP 

       250        260        270        280        290        300 
GDWNGAGAHT NYSTKSMRED GGYEVIKKAI EKLGLRHKEH IAAYGEGNER RLTGKHETAD 

       310        320        330        340        350 
INTFLWGVAN RGASIRVGRD TEQAGKGYFE DRRPASNMDP YTVTSMIAES TILWKP 

« Hide

References

« Hide 'large scale' references
[1]"Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence features of the regions of 1,191,918 bp covered by seventeen physically assigned P1 clones."
Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N., Tabata S.
DNA Res. 4:401-414(1997) [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]"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.
[5]"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 GLN-49 AND SER-174.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB008270 Genomic DNA. Translation: BAB10184.1.
CP002688 Genomic DNA. Translation: AED92312.1.
AY059932 mRNA. Translation: AAL24414.1.
AY128749 mRNA. Translation: AAM91149.1.
RefSeqNP_568335.1. NM_121663.2.
UniGeneAt.24254.

3D structure databases

ProteinModelPortalQ9FMD9.
SMRQ9FMD9. Positions 4-355.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid16795. 1 interaction.
STRING3702.AT5G16570.1-P.

Proteomic databases

PaxDbQ9FMD9.
PRIDEQ9FMD9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G16570.1; AT5G16570.1; AT5G16570.
GeneID831519.
KEGGath:AT5G16570.

Organism-specific databases

TAIRAT5G16570.

Phylogenomic databases

eggNOGCOG0174.
HOGENOMHOG000061500.
InParanoidQ9FMD9.
KOK01915.
OMAAESTILW.
PhylomeDBQ9FMD9.
ProtClustDBPLN02284.

Enzyme and pathway databases

BioCycARA:AT5G16570-MONOMER.
MetaCyc:AT5G16570-MONOMER.
BRENDA6.3.1.2. 399.
SABIO-RKQ9FMD9.

Gene expression databases

GenevestigatorQ9FMD9.

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 nameGLN14_ARATH
AccessionPrimary (citable) accession number: Q9FMD9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: March 1, 2001
Last modified: March 19, 2014
This is version 81 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