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P13564

- GLNA2_HORVU

UniProt

P13564 - GLNA2_HORVU

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Protein

Glutamine synthetase leaf isozyme, chloroplastic

Gene
N/A
Organism
Hordeum vulgare (Barley)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

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

Catalytic activityi

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

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
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamine synthetase leaf isozyme, chloroplastic (EC:6.3.1.2)
Alternative name(s):
GS2
Glutamate--ammonia ligase
OrganismiHordeum vulgare (Barley)
Taxonomic identifieri4513 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeHordeum

Organism-specific databases

GrameneiP13564.

Subcellular locationi

GO - Cellular componenti

  1. chloroplast Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5454ChloroplastAdd
BLAST
Chaini55 – 434380Glutamine synthetase leaf isozyme, chloroplasticPRO_0000011178Add
BLAST

Expressioni

Gene expression databases

GenevestigatoriP13564.

Interactioni

Subunit structurei

Homooctamer.

Structurei

3D structure databases

ProteinModelPortaliP13564.
SMRiP13564. Positions 66-417.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glutamine synthetase family.Curated

Keywords - Domaini

Transit peptide

Family and domain databases

Gene3Di3.30.590.10. 1 hit.
InterProiIPR008147. Gln_synt_beta.
IPR014746. Gln_synth/guanido_kin_cat_dom.
IPR008146. Gln_synth_cat_dom.
IPR027303. Gln_synth_gly_rich_site.
IPR027302. Gln_synth_N_conserv_site.
[Graphical view]
PfamiPF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
[Graphical view]
SUPFAMiSSF54368. SSF54368. 1 hit.
PROSITEiPS00180. GLNA_1. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P13564-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQVRRDDDGA GGCAGDAVPG GGEGQDGVPA RQPAGRVWGV SRAARATSGF
60 70 80 90 100
KVLALGPETT GVIQRMQQLL DMDTTPFTDK IIAEYIWVGG SGIDLRSKSR
110 120 130 140 150
TISKPVEDPS ELPKWNYDGS STGQAPGEDS EVILYPQAIF KDPFRGGNNI
160 170 180 190 200
LVICDTYTPQ GEPIPTNKRH MAAQIFSDPK VTSQVPWFGI EQEYTLMQRD
210 220 230 240 250
VNWPLGWPVG GYPGPQGPYY CAVGSDKSFG RDISDAHYKA CLYAGIEISG
260 270 280 290 300
TNGEVMPGQW EYQVGPSVGI DAGDHIWASR YILERITEQA GVVLTLDPKP
310 320 330 340 350
IQGDWNGAGC HTNYSTLSMR EDGGFDVIKK AILNLSLRHD LHIAAYGEGN
360 370 380 390 400
ERRLTGLHET ASISDFSWGV ANRGCSIRVG RDTEAKGKGY LEDRRPASNM
410 420 430
DPYTVTALLA ETTILWEPTL EAEALAAKKL ALKV
Length:434
Mass (Da):47,094
Last modified:November 1, 1990 - v2
Checksum:iFC47F5685EFC0D1E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 2719GAGGC…EGQDG → AQAVVQAMQCQVGVRGRTA in CAA34131. (PubMed:1983286)CuratedAdd
BLAST
Sequence conflicti41 – 411S → R in CAA34131. (PubMed:1983286)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53580 mRNA. Translation: CAA37643.1.
X16000 mRNA. Translation: CAA34131.1.
PIRiS11865. AJBHQ.
UniGeneiHv.733.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53580 mRNA. Translation: CAA37643.1 .
X16000 mRNA. Translation: CAA34131.1 .
PIRi S11865. AJBHQ.
UniGenei Hv.733.

3D structure databases

ProteinModelPortali P13564.
SMRi P13564. Positions 66-417.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

Gramenei P13564.

Gene expression databases

Genevestigatori P13564.

Family and domain databases

Gene3Di 3.30.590.10. 1 hit.
InterProi IPR008147. 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 ]
Pfami PF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
[Graphical view ]
SUPFAMi SSF54368. SSF54368. 1 hit.
PROSITEi PS00180. GLNA_1. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "A cDNA sequence coding for glutamine synthetase in Hordeum vulgare L."
    Stroman P., Baima S., Casadoro G.
    Plant Mol. Biol. 15:161-163(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Molecular analysis of barley mutants deficient in chloroplast glutamine synthetase."
    Freeman J., Marquez A.J., Wallsgrove R.M., Saarelainen R., Forde B.G.
    Plant Mol. Biol. 14:297-311(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-434.
    Strain: cv. Maris Mink.
    Tissue: Leaf.
  3. "Characterization of a cDNA clone for barley leaf glutamine synthetase."
    Baima S., Haegi A., Stroman P., Casadoro G.
    Carlsberg Res. Commun. 54:1-9(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 48-434.

Entry informationi

Entry nameiGLNA2_HORVU
AccessioniPrimary (citable) accession number: P13564
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: November 1, 1990
Last modified: October 29, 2014
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

In barley, there are distinct isozymes in the chloroplast, and cytoplasm.

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3