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P15102

- GLNA4_PHAVU

UniProt

P15102 - GLNA4_PHAVU

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Protein

Glutamine synthetase leaf isozyme, chloroplastic

Gene
N/A
Organism
Phaseolus vulgaris (Kidney bean) (French bean)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein 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
  2. nitrogen fixation Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Nitrogen fixation

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):
Glutamate--ammonia ligase
Isozyme delta
OrganismiPhaseolus vulgaris (Kidney bean) (French bean)
Taxonomic identifieri3885 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaePhaseolus

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 – 5050ChloroplastBy similarityAdd
BLAST
Chaini51 – 429379Glutamine synthetase leaf isozyme, chloroplasticPRO_0000011183Add
BLAST

Proteomic databases

PRIDEiP15102.
ProMEXiP15102.

Expressioni

Tissue specificityi

Expressed in leaves and stems. Low levels detected in roots and nodules.1 Publication

Interactioni

Subunit structurei

Homooctamer.

Structurei

3D structure databases

ProteinModelPortaliP15102.
SMRiP15102. Positions 61-412.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glutamine synthetase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

KOiK01915.

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.

P15102-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAQILAPSTQ WQMRFTKSSR HASPITSNTW SSLLMKQNKK TSSAKFRVLA
60 70 80 90 100
VKSDGSTINR LEGLLNLDIT PFTDKIIAEY IWIGGTGIDV RSKSRTISKP
110 120 130 140 150
VEHPSELPKW NYDGSSTGQA PGEDSEVILY PQAIFKDPFR GGNNILVICD
160 170 180 190 200
AYTPAGEPIP TNKRHRAAEV FSNPRVIAEV PWFGIEQEYT LLQTNVNWPL
210 220 230 240 250
GWPVGGYPGP QGPYYCSAGA DKSFGRDISD AHYKACLFAG INISGTNGEV
260 270 280 290 300
MPGQWEYQVG PSVGIEAGDH IWASRYILER ITEQAGVVLS LDPKPIEGDW
310 320 330 340 350
NGAGCHTNYS TKSMREDGGF EVIKKAILNL SLRHKEHISA YGEGNERRLT
360 370 380 390 400
GKHETASINT FSWGVANRGC SIRVGRDTEK NGKGYLEDRR PASNMDPYVV
410 420
TSLLAESTLL WEPTLEAEAL AAQKLALKV
Length:429
Mass (Da):47,246
Last modified:April 1, 1990 - v1
Checksum:i0CA55624B1118AF8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12738 mRNA. Translation: CAA31234.1.
PIRiS04031. AJFBQD.
RefSeqiXP_007147796.1. XM_007147734.1.
XP_007147797.1. XM_007147735.1.

Genome annotation databases

GeneIDi18628920.
KEGGipvu:PHAVU_006G155800g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12738 mRNA. Translation: CAA31234.1 .
PIRi S04031. AJFBQD.
RefSeqi XP_007147796.1. XM_007147734.1.
XP_007147797.1. XM_007147735.1.

3D structure databases

ProteinModelPortali P15102.
SMRi P15102. Positions 61-412.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P15102.
ProMEXi P15102.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 18628920.
KEGGi pvu:PHAVU_006G155800g.

Phylogenomic databases

KOi K01915.

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. "The chloroplast-located glutamine synthetase of Phaseolus vulgaris L.: nucleotide sequence, expression in different organs and uptake into isolated chloroplasts."
    Lightfoot D.A., Green N.K., Cullimore J.V.
    Plant Mol. Biol. 11:191-202(1988)
    [AGRICOLA] [Europe PMC]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: cv. Tendergreen.
    Tissue: Leaf.

Entry informationi

Entry nameiGLNA4_PHAVU
AccessioniPrimary (citable) accession number: P15102
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: November 26, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

There are at least four isozymes of this enzyme in P.vulgaris.
Irreversibly inhibited by the herbicide L-phosphinothricin (PPT).

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3