Q9FMD9 (GLN14_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	356 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Nitrogen fixation
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	glutamine 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 component	cytosol Non-traceable author statement Ref.5. Source: TAIR
Molecular function	ATP 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 356	356	Glutamine synthetase cytosolic isozyme 1-4		PRO_0000239820
Experimental info
	Mutagenesis	49	1	Q → K: 6-fold decrease in affinity for ammonium and catalytic efficiency; when associated with A-174. Ref.5
	Mutagenesis	174	1	S → A: 6-fold decrease in affinity for ammonium and catalytic efficiency; when associated with K-49. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q9FMD9 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: A8F39CE8835592D4	FASTA	356	38,987
	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

References

	« Hide 'large scale' referencesShow '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: 9501997] [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. , 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: 14593172] [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: 14757761] [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: 16338958] [Abstract] Cited for: MUTAGENESIS OF GLN-49 AND SER-174.
+	Additional computationally mapped references.

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.
IPI	IPI00535907.
RefSeq	NP_568335.1. NM_121663.2.
UniGene	At.24254.
3D structure databases
ProteinModelPortal	Q9FMD9.
SMR	Q9FMD9. Positions 4-355.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9FMD9.
Proteomic databases
PRIDE	Q9FMD9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G16570.1; AT5G16570.1; AT5G16570.
GeneID	831519.
GenomeReviews	Gene locus AT5G16570 in contig BA000015_GR.
KEGG	ath:AT5G16570.
NMPDR	fig|3702.1.peg.23813.
Organism-specific databases
TAIR	At5g16570.
Phylogenomic databases
eggNOG	KOG0683.
GeneTree	EPGT00050000002349.
HOGENOM	HBG299709.
InParanoid	Q9FMD9.
OMA	SPNTALD.
PhylomeDB	Q9FMD9.
ProtClustDB	PLN02284.
Enzyme and pathway databases
BRENDA	6.3.1.2. 399.
Gene expression databases
ArrayExpress	Q9FMD9.
Genevestigator	Q9FMD9.
GermOnline	AT5G16570. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR008147. Gln_synt_beta. IPR014746. Gln_synth/guanido_kin_cat_dom. IPR008146. Gln_synth_cat_dom. [Graphical view]
Gene3D	G3DSA:3.30.590.10. ATP-gua_Ptrans. 1 hit.
KO	K01915.
Pfam	PF00120. Gln-synt_C. 1 hit. PF03951. Gln-synt_N. 1 hit. [Graphical view]
SUPFAM	SSF54368. Gln_synt_beta. 1 hit.
PROSITE	PS00180. GLNA_1. 1 hit. PS00181. GLNA_ATP. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLN14_ARATH

Accession

Primary (citable) accession number: Q9FMD9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 13, 2006
Last sequence update:	March 1, 2001
Last modified:	November 16, 2011
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program