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Q43127 (GLNA2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. 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, chloroplastic/mitochondrial

EC=6.3.1.2
Alternative name(s):
GS2
Glutamate--ammonia ligase
Gene names
Name:GLN2
Synonyms:GSLI
Ordered Locus Names:At5g35630
ORF Names:MJE4.9
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length430 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The light-modulated chloroplast/mitochondrial enzyme, encoded by a nuclear gene and expressed primarily in leaves, is responsible for the reassimilation of the ammonia generated by photorespiration. Ref.8

Catalytic activity

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

Subunit structure

Homooctamer By similarity.

Subcellular location

Plastidchloroplast. Mitochondrion Ref.8.

Tissue specificity

Expressed in mesophyll and epidermal cells of leaves. Ref.8

Induction

By light, sucrose, glucose and fructose. Ref.7

Sequence similarities

Belongs to the glutamine synthetase family.

Ontologies

Keywords
   Cellular componentChloroplast
Mitochondrion
Plastid
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Traceable author statement PubMed 10444084. Source: TAIR

ammonia assimilation cycle

Traceable author statement PubMed 16338958. Source: TAIR

glutamine biosynthetic process

Inferred from electronic annotation. Source: InterPro

response to cadmium ion

Inferred from expression pattern PubMed 20005002. Source: TAIR

response to salt stress

Inferred from expression pattern PubMed 17916636. Source: TAIR

   Cellular_componentapoplast

Inferred from direct assay PubMed 18538804. Source: TAIR

chloroplast

Inferred from direct assay PubMed 15028209Ref.8PubMed 18431481. Source: TAIR

chloroplast envelope

Inferred from direct assay PubMed 12938931. Source: TAIR

chloroplast stroma

Inferred from direct assay PubMed 16207701PubMed 18633119PubMed 20061580. Source: TAIR

chloroplast thylakoid membrane

Inferred from direct assay PubMed 15322131. Source: TAIR

cytosolic ribosome

Inferred from direct assay PubMed 15821981. Source: TAIR

membrane

Inferred from direct assay PubMed 17432890. Source: TAIR

mitochondrion

Inferred from direct assay Ref.8. Source: TAIR

thylakoid

Inferred from direct assay PubMed 16648217. Source: TAIR

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate-ammonia ligase activity

Inferred from direct assay Ref.8. Source: TAIR

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4545Chloroplast and mitochondrion Potential
Chain46 – 430385Glutamine synthetase, chloroplastic/mitochondrial
PRO_0000011174

Amino acid modifications

Modified residue1061Phosphoserine Ref.9

Sequences

Sequence LengthMass (Da)Tools
Q43127 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 664029BC06572295

FASTA43047,411
        10         20         30         40         50         60 
MAQILAASPT CQMRVPKHSS VIASSSKLWS SVVLKQKKQS NNKVRGFRVL ALQSDNSTVN 

        70         80         90        100        110        120 
RVETLLNLDT KPYSDRIIAE YIWIGGSGID LRSKSRTIEK PVEDPSELPK WNYDGSSTGQ 

       130        140        150        160        170        180 
APGEDSEVIL YPQAIFRDPF RGGNNILVIC DTWTPAGEPI PTNKRAKAAE IFSNKKVSGE 

       190        200        210        220        230        240 
VPWFGIEQEY TLLQQNVKWP LGWPVGAFPG PQGPYYCGVG ADKIWGRDIS DAHYKACLYA 

       250        260        270        280        290        300 
GINISGTNGE VMPGQWEFQV GPSVGIDAGD HVWCARYLLE RITEQAGVVL TLDPKPIEGD 

       310        320        330        340        350        360 
WNGAGCHTNY STKSMREEGG FEVIKKAILN LSLRHKEHIS AYGEGNERRL TGKHETASID 

       370        380        390        400        410        420 
QFSWGVANRG CSIRVGRDTE AKGKGYLEDR RPASNMDPYI VTSLLAETTL LWEPTLEAEA 

       430 
LAAQKLSLNV 

« Hide

References

« Hide 'large scale' references
[1]"The glutamine synthetase gene family of Arabidopsis thaliana: light-regulation and differential expression in leaves, roots and seeds."
Peterman T.K., Goodman H.M.
Mol. Gen. Genet. 230:145-154(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Nucleotide sequences of genes for cytosolic and chloroplastic glutamine synthetase from Arabidopsis thaliana."
Arimura G., Fujii M., Takahashi M., Goshima N., Morikawa H.
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence features of the regions of 1,367,185 bp covered by 19 physically assigned P1 and TAC clones."
Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N., Tabata S.
DNA Res. 5:203-216(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[5]"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.
[6]"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].
[7]"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.
[8]"Arabidopsis thaliana GLN2-encoded glutamine synthetase is dual targeted to leaf mitochondria and chloroplasts."
Taira M., Valtersson U., Burkhardt B., Ludwig R.A.
Plant Cell 16:2048-2058(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[9]"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S69727 mRNA. Translation: AAB20558.1.
AB015045 Genomic DNA. Translation: BAA88761.1.
AB013393 Genomic DNA. Translation: BAB09304.1.
CP002688 Genomic DNA. Translation: AED93993.1.
CP002688 Genomic DNA. Translation: AED93994.1.
CP002688 Genomic DNA. Translation: AED93995.1.
AF428319 mRNA. Translation: AAL16249.1.
AF428461 mRNA. Translation: AAL16230.1.
AY081252 mRNA. Translation: AAL91141.1.
AY091114 mRNA. Translation: AAM14064.1.
AY122977 mRNA. Translation: AAM67510.1.
AY088222 mRNA. Translation: AAM65763.1.
PIRS18600.
RefSeqNP_001031969.1. NM_001036892.1.
NP_001078639.1. NM_001085170.1.
NP_198413.1. NM_122954.3.
UniGeneAt.24218.

3D structure databases

ProteinModelPortalQ43127.
SMRQ43127. Positions 65-413.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid18788. 4 interactions.
DIPDIP-32735N.
IntActQ43127. 1 interaction.

2D gel databases

SWISS-2DPAGEQ43127.

Proteomic databases

PaxDbQ43127.
PRIDEQ43127.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G35630.1; AT5G35630.1; AT5G35630.
AT5G35630.2; AT5G35630.2; AT5G35630.
AT5G35630.3; AT5G35630.3; AT5G35630.
GeneID833535.
KEGGath:AT5G35630.

Organism-specific databases

TAIRAT5G35630.

Phylogenomic databases

eggNOGCOG0174.
HOGENOMHOG000061500.
InParanoidQ43127.
KOK01915.
OMAGTPYGWP.
PhylomeDBQ43127.
ProtClustDBPLN03036.

Enzyme and pathway databases

BioCycARA:AT5G35630-MONOMER.
ARA:GQT-2612-MONOMER.
ARA:GQT-2613-MONOMER.
MetaCyc:AT5G35630-MONOMER.

Gene expression databases

ArrayExpressQ43127.
GenevestigatorQ43127.

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 nameGLNA2_ARATH
AccessionPrimary (citable) accession number: Q43127
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 115 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