SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q02154

- GLNA2_RHILP

UniProt

Q02154 - GLNA2_RHILP

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Glutamine synthetase 2
Gene
glnII
Organism
Rhizobium leguminosarum bv. phaseoli
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Enzyme regulationi

Transferase activity is inhibited by NH4Cl.

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. glutamate-ammonia ligase activity Source: UniProtKB-EC
Complete GO annotation...

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 2 (EC:6.3.1.2)
Alternative name(s):
Glutamate--ammonia ligase II
Glutamine synthetase II
Short name:
GSII
Gene namesi
Name:glnII
OrganismiRhizobium leguminosarum bv. phaseoli
Taxonomic identifieri385 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 326325Glutamine synthetase 2
PRO_0000153224Add
BLAST

Interactioni

Subunit structurei

Homooctamer.

Structurei

3D structure databases

ProteinModelPortaliQ02154.

Family & Domainsi

Sequence similaritiesi

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.

Q02154-1 [UniParc]FASTAAdd to Basket

« Hide

MTKFKLEYIW LDGYTPVPNL RGKTQIKEFD EFPTLEQLPL WGFDGSSTMQ    50
AEGSSDCVLK PVAIYPDPAR TNGALVMCEV MMPDGHAHAS NARATILDDE 100
DAWFGFEQEY FFYQNGRPLG FPEQGYPAPQ PYYTGVGYSN VGDVAREIVE 150
EHLDLCLAAG INHEGINAEV AKGQWEFQIF GKGSKKAADQ IWMARYLLQR 200
LTEKYGIDIE YHCKPLGDTD WNGSGMHCNF STKYLREVGG KEYFEALMAS 250
SDKNLMDHIA VYGPDNDKRL TGKHETAPWN KFSYGVADRG ASIRVPHSFI 300
KNDYKGYLED RRPNSQGDPY QIVRRF 326
Length:326
Mass (Da):36,979
Last modified:January 23, 2007 - v3
Checksum:i637AE03B83D1F840
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X67296 Genomic DNA. Translation: CAA47710.1.
PIRiS26216.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X67296 Genomic DNA. Translation: CAA47710.1 .
PIRi S26216.

3D structure databases

ProteinModelPortali Q02154.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

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. "Activation of the Rhizobium leguminosarum glnII gene by NtrC is dependent on upstream DNA sequences."
    Patriarca E.J., Chiurazzi M., Manco G., Riccio A., Lamberti A., Paolis A., Rossi M., Defez R., Iaccarino M.
    Mol. Gen. Genet. 234:337-345(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: LPR1105.
  2. "Dissociation by NH4Cl treatment of the enzymic activities of glutamine synthetase II from Rhizobium leguminosarum biovar viceae."
    Manco G., Rossi M., Defez R., Lamberti A., Percuoco G., Iaccarino M.
    J. Gen. Microbiol. 138:1453-1460(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-27.
    Strain: LPR1105.

Entry informationi

Entry nameiGLNA2_RHILP
AccessioniPrimary (citable) accession number: Q02154
Secondary accession number(s): Q9R5J0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: October 16, 2013
This is version 69 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Two forms of glutamine synthetase (GSI and GSII) can be found in this nitrogen fixing bacteria, GSI is a typical prokaryotic glutamine synthetase whereas GSII is similar to the eukaryotic enzyme.

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi