Skip Header

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

Glutamine synthetase

Gene

glnA

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed-Annotation score: 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).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: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-502.

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:TM_0943
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
ProteomesiUP000008183 Componenti: Chromosome

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 – 439439Glutamine synthetasePRO_0000153273Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei369 – 3691O-AMP-tyrosineBy similarity

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi243274.TM0943.

Structurei

3D structure databases

ProteinModelPortaliP36205.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glutamine synthetase family.Curated

Phylogenomic databases

eggNOGiCOG0174.
InParanoidiP36205.
KOiK01915.
OMAiKVLNQVG.
OrthoDBiEOG6B360N.

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.

P36205-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTIETIKRII EEENVRFIRL QFTDINGTLK NLEITPDVFL ESWEDGIMFD
60 70 80 90 100
GSSIEGFVRI EESDMYLKPV LDTFAVLPWT VDGAKSARVI CDVYTPDGKP
110 120 130 140 150
FEGDPRYRLR RMMEKAEQLG YTPYAGPEME FFILPINEKG EPVPEFLDHG
160 170 180 190 200
GYFDLLPLSK VEEIRRDIAI ALEKMGITVE ATHHEVAPSQ HEVDFRYDTF
210 220 230 240 250
LRTADNAQTV KLVIKTMAIF HGYHATFMPK PFYGVNGSGM HVHMSLFRGD
260 270 280 290 300
KNAFYDPDDP LGLSKELRYF VGGILKHAKA LAAVTNPTIN SYKRLVPGYE
310 320 330 340 350
APVYISWSVG NRSALIRIPK ARGKATRLEY RSPDPSCNIY LAFAAILAAG
360 370 380 390 400
LDGIINKIEP PAPVEENIYH MTSERREELN IESLPGSLKE AVEELKKDDV
410 420 430
IIDALGEHIF EKFVEAAEKD WKEFSTYVTN WELQRYLYL
Length:439
Mass (Da):50,035
Last modified:May 30, 2000 - v2
Checksum:iABE3E674BD2F2359
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti204 – 2041A → G in CAA42729 (PubMed:1348781).Curated
Sequence conflicti280 – 2801A → R in CAA42729 (PubMed:1348781).Curated
Sequence conflicti336 – 3361S → T in CAA42729 (PubMed:1348781).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60160 Genomic DNA. Translation: CAA42729.1.
AE000512 Genomic DNA. Translation: AAD36024.1.
PIRiB72313.
RefSeqiNP_228751.1. NC_000853.1.
YP_007977295.1. NC_021214.1.
YP_008991957.1. NC_023151.1.

Genome annotation databases

EnsemblBacteriaiAAD36024; AAD36024; TM_0943.
GeneIDi898680.
KEGGitma:TM0943.
tmi:THEMA_09630.
PATRICi23936817. VBITheMar51294_0957.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60160 Genomic DNA. Translation: CAA42729.1.
AE000512 Genomic DNA. Translation: AAD36024.1.
PIRiB72313.
RefSeqiNP_228751.1. NC_000853.1.
YP_007977295.1. NC_021214.1.
YP_008991957.1. NC_023151.1.

3D structure databases

ProteinModelPortaliP36205.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243274.TM0943.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD36024; AAD36024; TM_0943.
GeneIDi898680.
KEGGitma:TM0943.
tmi:THEMA_09630.
PATRICi23936817. VBITheMar51294_0957.

Phylogenomic databases

eggNOGiCOG0174.
InParanoidiP36205.
KOiK01915.
OMAiKVLNQVG.
OrthoDBiEOG6B360N.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-502.

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. "The glnA gene of the extremely thermophilic eubacterium Thermotoga maritima: cloning, primary structure, and expression in Escherichia coli."
    Sanangelantoni A.M., Forlani G., Ambroselli F., Cammarano P., Tiboni O.
    J. Gen. Microbiol. 138:383-393(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.

Entry informationi

Entry nameiGLNA_THEMA
AccessioniPrimary (citable) accession number: P36205
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: May 30, 2000
Last modified: April 1, 2015
This is version 105 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.