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P10583

- GLNA_AZOBR

UniProt

P10583 - GLNA_AZOBR

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Protein

Glutamine synthetase

Gene
glnA
Organism
Azospirillum brasilense
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Catalytic activityi

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

Enzyme regulationi

The activity of this enzyme is controlled by adenylation under conditions of abundant glutamine. The fully adenylated enzyme complex is inactive By similarity.

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 (EC:6.3.1.2)
Alternative name(s):
Glutamate--ammonia ligase
Gene namesi
Name:glnA
OrganismiAzospirillum brasilense
Taxonomic identifieri192 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeAzospirillum

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
Chaini1 – 468468Glutamine synthetasePRO_0000153229Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei398 – 3981O-AMP-tyrosine By similarity

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Oligomer of 12 subunits arranged in the form of two hexagons.

Structurei

3D structure databases

ProteinModelPortaliP10583.
SMRiP10583. Positions 7-468.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.10.20.70. 1 hit.
3.30.590.10. 1 hit.
InterProiIPR008147. Gln_synt_beta.
IPR014746. Gln_synth/guanido_kin_cat_dom.
IPR008146. Gln_synth_cat_dom.
IPR027303. Gln_synth_gly_rich_site.
IPR004809. Gln_synth_I.
IPR001637. Gln_synth_I_adenylation_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.
TIGRFAMsiTIGR00653. GlnA. 1 hit.
PROSITEiPS00180. GLNA_1. 1 hit.
PS00182. GLNA_ADENYLATION. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P10583-1 [UniParc]FASTAAdd to Basket

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MSDISKVFDL IKEHDVKYVD LRFTDPRGKL HHTAQHVSTI DEDVFEDGIM    50
FDGSSIAGWK AINESDMILQ LDPTTAVMDP FSAQPTLNIL CDVYEPSTGQ 100
PYARCPRGIA KAAEKYMASA GIADTAYFGP EAEFFVFDDV KFKVEMNKVS 150
YEFDSEEGPY TSDKDYEDGN LGHRPGVKGG YFPVAPVDSG SDLRAEMLSV 200
LAEMGVPVEK HHHEVAASQH ELGIKFDTLV RTGDNMQYYK YVVHNVAHAY 250
GKTATFMPKP VFGDNGSGMH MHQSIWKEGQ PLFAGNQYAD LSELALYYIG 300
GIIKHAKALN AFTNPTTNSY KRLVPGYEAP VLLAYSARNR SASCRIPYVA 350
SPKGKRVEVR FPDPSANPYL AFAALLMAGL DGIQNKIHPG EAMDKNLYDL 400
PAEELAKVPT VCGSREALDS LKADSAFLQK GDVFTKDMIE SYIDLRTEEL 450
LAFETMPHPI EYKMYYSV 468
Length:468
Mass (Da):51,976
Last modified:July 1, 1989 - v1
Checksum:i356AA3803E024F1A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M26107 Genomic DNA. Translation: AAA22183.1.
PIRiA24714. AJKCQB.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M26107 Genomic DNA. Translation: AAA22183.1 .
PIRi A24714. AJKCQB.

3D structure databases

ProteinModelPortali P10583.
SMRi P10583. Positions 7-468.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.10.20.70. 1 hit.
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.
IPR004809. Gln_synth_I.
IPR001637. Gln_synth_I_adenylation_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.
TIGRFAMsi TIGR00653. GlnA. 1 hit.
PROSITEi PS00180. GLNA_1. 1 hit.
PS00182. GLNA_ADENYLATION. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Nucleotide sequence of the Azospirillum brasilense Sp7 glutamine synthetase structural gene."
    Bozouklian H., Elmerich C.
    Biochimie 68:1181-1187(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 29145 / Sp7 / DSM 1690 / IMET 11303.

Entry informationi

Entry nameiGLNA_AZOBR
AccessioniPrimary (citable) accession number: P10583
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: September 3, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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