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Protein

Glutamine synthetase

Gene

glnA

Organism
Thermococcus kodakaraensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1))
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Carries out the ATP-dependent synthesis of glutamine from ammonium nitrogen and glutamate. Exhibits both L-gamma-glutamylhydroxamate synthetase and gamma-glutamyltransferase activities when using hydroxylamine as substrate; in fact, the enzyme possesses low biosynthetic activity, suggesting that the reaction is biased towards the degradation of glutamine under ammonia-rich conditions. Might play some role in ammonia assimilation under ammonia-starvation conditions. Can also use GTP instead of ATP in the synthetase reaction, but not CTP or UTP.1 Publication

Catalytic activityi

ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine.1 Publication
ATP + L-glutamate + hydroxylamine = ADP + phosphate + L-gamma-glutamylhydroxamate.1 Publication

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).By similarity

Kineticsi

kcat is 2190 min(-1) towards L-glutamate in the synthetase reaction and 3900 min(-1) towards L-glutamine in the transferase reaction.

  1. KM=23.5 mM for L-glutamate (at pH 7.8 and 60 degrees Celsius)1 Publication
  2. KM=15.2 mM for hydroxylamine (when a high concentration is used, at pH 7.8 and 60 degrees Celsius)1 Publication
  3. KM=1.6 mM for hydroxylamine (when a low concentration is used, at pH 7.8 and 60 degrees Celsius)1 Publication
  4. KM=28.0 mM for ATP (at pH 7.8 and 60 degrees Celsius)1 Publication
  5. KM=5.0 mM for L-glutamine (at pH 7.2 and 60 degrees Celsius)1 Publication
  6. KM=6.3 mM for ADP (at pH 7.2 and 60 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 7.8 for the synthetase reaction and pH 7.2 for the transferase reaction.1 Publication

Temperature dependencei

Optimum temperature is 60 degrees Celsius for both transferase and synthetase activities.1 Publication

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: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciTKOD69014:GH72-1833-MONOMER.
BRENDAi6.3.1.2. 5027.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamine synthetase (EC:6.3.1.2)
Short name:
GS
Alternative name(s):
Glutamate--ammonia ligase
Gene namesi
Name:glnA
Ordered Locus Names:TK1796
OrganismiThermococcus kodakaraensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1))
Taxonomic identifieri69014 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus
ProteomesiUP000000536 Componenti: Chromosome

Subcellular locationi

Cytoplasm Curated

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 – 443443Glutamine synthetasePRO_0000153211Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei362 – 3621O-AMP-tyrosineBy similarity

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Homododecamer.1 Publication

Protein-protein interaction databases

IntActiO08467. 1 interaction.
MINTiMINT-8377176.
STRINGi69014.TK1796.

Structurei

3D structure databases

ProteinModelPortaliO08467.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glutamine synthetase family.Curated

Phylogenomic databases

eggNOGiCOG0174.
HOGENOMiHOG000005156.
InParanoidiO08467.
KOiK01915.
OMAiKVLNQVG.

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.
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.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O08467-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNEIKGIERA VQVEVPRPRF LLLAFTDING SLKGMEIPME RYEEAVEDGV
60 70 80 90 100
SFDGSSIPGF EGIEDSDLIF KADPSTYAEI PWEGIGRVYG YIYKGDEPYQ
110 120 130 140 150
ADPRGILKRV LERLEKEGLK AHIGPEPEFY IFKKNGTWEL HIPDSGGYFD
160 170 180 190 200
LVGLDKAREI RREIALYMPY LGLKPEVLHH EVGKAQHEID FRYDEALRTA
210 220 230 240 250
DNIVSFKHVV KAVAELHGYY ATFMPKPIYG FPGNGMHLHI SLWKDGENVF
260 270 280 290 300
IGEDGLSDTA LHFIGGILKH AKALAALTNP TVNSYKRLVP GYEAPVYISW
310 320 330 340 350
GYRNRSALIR VPAFKGSGAR IEYRCPDPSA NPYLALAGIL MVGLDGIKKK
360 370 380 390 400
VEPDSYVETN VYEMDDAERE RLGIDTLPGS LGEALEELKK DKTVREALGG
410 420 430 440
AYKNFIDYKE REWEEYIEYL SSRDIPIDTK KVTEWELERY FYV
Length:443
Mass (Da):50,308
Last modified:March 29, 2005 - v2
Checksum:i94357E45D5F18168
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti402 – 4021Y → N in BAA20530 (PubMed:9172372).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86222 Genomic DNA. Translation: BAA20530.1.
AP006878 Genomic DNA. Translation: BAD85985.1.
RefSeqiYP_184209.1. NC_006624.1.

Genome annotation databases

EnsemblBacteriaiBAD85985; BAD85985; TK1796.
GeneIDi3233803.
KEGGitko:TK1796.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86222 Genomic DNA. Translation: BAA20530.1.
AP006878 Genomic DNA. Translation: BAD85985.1.
RefSeqiYP_184209.1. NC_006624.1.

3D structure databases

ProteinModelPortaliO08467.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO08467. 1 interaction.
MINTiMINT-8377176.
STRINGi69014.TK1796.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD85985; BAD85985; TK1796.
GeneIDi3233803.
KEGGitko:TK1796.

Phylogenomic databases

eggNOGiCOG0174.
HOGENOMiHOG000005156.
InParanoidiO08467.
KOiK01915.
OMAiKVLNQVG.

Enzyme and pathway databases

BioCyciTKOD69014:GH72-1833-MONOMER.
BRENDAi6.3.1.2. 5027.

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.
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.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of recombinant glutamine synthetase from the hyperthermophilic archaeon Pyrococcus sp. strain KOD1."
    Adul Rahman R.N.Z., Jongsareejit B., Fujiwara S., Imanaka T.
    Appl. Environ. Microbiol. 63:2472-2476(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, GENE NAME, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    Strain: ATCC BAA-918 / JCM 12380 / KOD1.
  2. "Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes."
    Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.
    Genome Res. 15:352-363(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-918 / JCM 12380 / KOD1.

Entry informationi

Entry nameiGLNA_THEKO
AccessioniPrimary (citable) accession number: O08467
Secondary accession number(s): Q5JJ67
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: March 29, 2005
Last modified: April 1, 2015
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.