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P15102 (GLNA4_PHAVU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 leaf isozyme, chloroplastic

EC=6.3.1.2
Alternative name(s):
Glutamate--ammonia ligase
Isozyme delta
OrganismPhaseolus vulgaris (Kidney bean) (French bean)
Taxonomic identifier3885 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaePhaseolus

Protein attributes

Sequence length429 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 enzyme, encoded by a nuclear gene and expressed primarily in leaves, is responsible for the reassimilation of the ammonia generated by photorespiration.

Catalytic activity

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

Subunit structure

Homooctamer.

Subcellular location

Plastidchloroplast.

Tissue specificity

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

Miscellaneous

There are at least four isozymes of this enzyme in P.vulgaris.

Irreversibly inhibited by the herbicide L-phosphinothricin (PPT).

Sequence similarities

Belongs to the glutamine synthetase family.

Ontologies

Keywords
   Biological processNitrogen fixation
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
Gene Ontology (GO)
   Biological_processglutamine biosynthetic process

Inferred from electronic annotation. Source: InterPro

nitrogen fixation

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate-ammonia ligase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5050Chloroplast By similarity
Chain51 – 429379Glutamine synthetase leaf isozyme, chloroplastic
PRO_0000011183

Sequences

Sequence LengthMass (Da)Tools
P15102 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 0CA55624B1118AF8

FASTA42947,246
        10         20         30         40         50         60 
MAQILAPSTQ WQMRFTKSSR HASPITSNTW SSLLMKQNKK TSSAKFRVLA VKSDGSTINR 

        70         80         90        100        110        120 
LEGLLNLDIT PFTDKIIAEY IWIGGTGIDV RSKSRTISKP VEHPSELPKW NYDGSSTGQA 

       130        140        150        160        170        180 
PGEDSEVILY PQAIFKDPFR GGNNILVICD AYTPAGEPIP TNKRHRAAEV FSNPRVIAEV 

       190        200        210        220        230        240 
PWFGIEQEYT LLQTNVNWPL GWPVGGYPGP QGPYYCSAGA DKSFGRDISD AHYKACLFAG 

       250        260        270        280        290        300 
INISGTNGEV MPGQWEYQVG PSVGIEAGDH IWASRYILER ITEQAGVVLS LDPKPIEGDW 

       310        320        330        340        350        360 
NGAGCHTNYS TKSMREDGGF EVIKKAILNL SLRHKEHISA YGEGNERRLT GKHETASINT 

       370        380        390        400        410        420 
FSWGVANRGC SIRVGRDTEK NGKGYLEDRR PASNMDPYVV TSLLAESTLL WEPTLEAEAL 


AAQKLALKV 

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References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X12738 mRNA. Translation: CAA31234.1.
PIRAJFBQD. S04031.
RefSeqXP_007147796.1. XM_007147734.1.
XP_007147797.1. XM_007147735.1.

3D structure databases

ProteinModelPortalP15102.
SMRP15102. Positions 61-412.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP15102.
ProMEXP15102.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID18628920.

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 nameGLNA4_PHAVU
AccessionPrimary (citable) accession number: P15102
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: July 9, 2014
This is version 78 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