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.

O08467

- GLNA_THEKO

UniProt

O08467 - GLNA_THEKO

(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
Gene
glnA, TK1796
Organism
Thermococcus kodakaraensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1))
Status
Reviewed - 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.

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

pH dependencei

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

Temperature dependencei

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

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.

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: Chromosome

Subcellular locationi

Cytoplasm Reviewed prediction

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 synthetase
PRO_0000153211Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei362 – 3621O-AMP-tyrosine By 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.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0174.
HOGENOMiHOG000005156.
KOiK01915.

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

MNEIKGIERA VQVEVPRPRF LLLAFTDING SLKGMEIPME RYEEAVEDGV    50
SFDGSSIPGF EGIEDSDLIF KADPSTYAEI PWEGIGRVYG YIYKGDEPYQ 100
ADPRGILKRV LERLEKEGLK AHIGPEPEFY IFKKNGTWEL HIPDSGGYFD 150
LVGLDKAREI RREIALYMPY LGLKPEVLHH EVGKAQHEID FRYDEALRTA 200
DNIVSFKHVV KAVAELHGYY ATFMPKPIYG FPGNGMHLHI SLWKDGENVF 250
IGEDGLSDTA LHFIGGILKH AKALAALTNP TVNSYKRLVP GYEAPVYISW 300
GYRNRSALIR VPAFKGSGAR IEYRCPDPSA NPYLALAGIL MVGLDGIKKK 350
VEPDSYVETN VYEMDDAERE RLGIDTLPGS LGEALEELKK DKTVREALGG 400
AYKNFIDYKE REWEEYIEYL SSRDIPIDTK KVTEWELERY FYV 443
Length:443
Mass (Da):50,308
Last modified:March 29, 2005 - v2
Checksum:i94357E45D5F18168
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti402 – 4021Y → N in BAA20530. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
D86222 Genomic DNA. Translation: BAA20530.1 .
AP006878 Genomic DNA. Translation: BAD85985.1 .
RefSeqi YP_184209.1. NC_006624.1.

3D structure databases

ProteinModelPortali O08467.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi O08467. 1 interaction.
MINTi MINT-8377176.
STRINGi 69014.TK1796.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAD85985 ; BAD85985 ; TK1796 .
GeneIDi 3233803.
KEGGi tko:TK1796.

Phylogenomic databases

eggNOGi COG0174.
HOGENOMi HOG000005156.
KOi K01915.

Enzyme and pathway databases

BioCyci TKOD69014:GH72-1833-MONOMER.

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

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(1997) [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(2005) [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: September 3, 2014
This is version 91 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