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Protein

Glutamine synthetase

Gene

glnA1

Organism
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in nitrogen metabolism via ammonium assimilation (PubMed:24112767). Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia (PubMed:24112767). Also plays a key role in controlling the ammonia levels within infected host cells and so contributes to the pathogens capacity to inhibit phagosome acidification and phagosome-lysosome fusion (By similarity). Involved in cell wall biosynthesis via the production of the major component poly-L-glutamine (PLG) (PubMed:24112767). PLG synthesis in the cell wall occurs only in nitrogen limiting conditions and on the contrary high nitrogen conditions inhibit PLG synthesis (PubMed:24112767).By similarity1 Publication

Catalytic activityi

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

Cofactori

Mg2+By similarityNote: Binds 2 Mg2+ ions per subunit.By similarity

Enzyme regulationi

When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) of GlnE inhibits GlnA by covalent transfer of an adenylyl group from ATP to Tyr-406 (PubMed:15037612). Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) of GlnE activates GlnA by removing the adenylyl group by phosphorolysis (PubMed:15037612). The fully adenylated enzyme complex is inactive (Probable).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi133Magnesium 1By similarity1
Metal bindingi135Magnesium 2By similarity1
Binding sitei214ATPBy similarity1
Metal bindingi219Magnesium 2By similarity1
Metal bindingi227Magnesium 2By similarity1
Binding sitei272L-glutamate; via oxygen carbonylBy similarity1
Metal bindingi276Magnesium 1; via pros nitrogenBy similarity1
Binding sitei280ATPBy similarity1
Binding sitei329L-glutamateBy similarity1
Binding sitei335L-glutamateBy similarity1
Binding sitei347ATPBy similarity1
Binding sitei347L-glutamateBy similarity1
Binding sitei352ATPBy similarity1
Binding sitei361ATPBy similarity1
Metal bindingi366Magnesium 1By similarity1
Binding sitei368L-glutamateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi230 – 232ATPBy similarity3
Nucleotide bindingi278 – 280ATPBy similarity3

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLigase
Biological processVirulence
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi6.3.1.2. 3494.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamine synthetase1 Publication (EC:6.3.1.21 Publication)
Short name:
GS1 Publication
Alternative name(s):
Glutamate--ammonia ligaseBy similarity
Glutamine synthetase I betaBy similarity
Short name:
GSI betaBy similarity
Gene namesi
Name:glnA11 Publication
Synonyms:glnA
Ordered Locus Names:Mb2244
OrganismiMycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Taxonomic identifieri233413 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001419 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm By similarity

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001532441 – 478Glutamine synthetaseAdd BLAST478

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei406O-AMP-tyrosineBy similarity1

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP0A591.
SMRiP0A591.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni271 – 272L-glutamate bindingBy similarity2

Sequence similaritiesi

Belongs to the glutamine synthetase family.Curated

Phylogenomic databases

HOGENOMiHOG000005157.
KOiK01915.
OMAiKVLNQVG.

Family and domain databases

Gene3Di3.10.20.70. 1 hit.
3.30.590.10. 1 hit.
InterProiView protein in InterPro
IPR008147. Gln_synt_b-grasp.
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.
PfamiView protein in Pfam
PF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
SMARTiView protein in SMART
SM01230. Gln-synt_C. 1 hit.
SUPFAMiSSF54368. SSF54368. 1 hit.
TIGRFAMsiTIGR00653. GlnA. 1 hit.
PROSITEiView protein in PROSITE
PS00180. GLNA_1. 1 hit.
PS00182. GLNA_ADENYLATION. 1 hit.
PS00181. GLNA_ATP. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A591-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEKTPDDVF KLAKDEKVEY VDVRFCDLPG IMQHFTIPAS AFDKSVFDDG
60 70 80 90 100
LAFDGSSIRG FQSIHESDML LLPDPETARI DPFRAAKTLN INFFVHDPFT
110 120 130 140 150
LEPYSRDPRN IARKAENYLI STGIADTAYF GAEAEFYIFD SVSFDSRANG
160 170 180 190 200
SFYEVDAISG WWNTGAATEA DGSPNRGYKV RHKGGYFPVA PNDQYVDLRD
210 220 230 240 250
KMLTNLINSG FILEKGHHEV GSGGQAEINY QFNSLLHAAD DMQLYKYIIK
260 270 280 290 300
NTAWQNGKTV TFMPKPLFGD NGSGMHCHQS LWKDGAPLMY DETGYAGLSD
310 320 330 340 350
TARHYIGGLL HHAPSLLAFT NPTVNSYKRL VPGYEAPINL VYSQRNRSAC
360 370 380 390 400
VRIPITGSNP KAKRLEFRSP DSSGNPYLAF SAMLMAGLDG IKNKIEPQAP
410 420 430 440 450
VDKDLYELPP EEAASIPQTP TQLSDVIDRL EADHEYLTEG GVFTNDLIET
460 470
WISFKRENEI EPVNIRPHPY EFALYYDV
Length:478
Mass (Da):53,570
Last modified:March 15, 2005 - v1
Checksum:i576E30073484136D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF458290 Genomic DNA. Translation: AAL58468.1.
BX248333 Genomic DNA. Translation: CDO43498.1.
RefSeqiNP_855893.1. NC_002945.3.
WP_003411475.1. NC_002945.3.

Genome annotation databases

EnsemblBacteriaiCDO43498; CDO43498; Mb2244.
GeneIDi1091369.
KEGGimbo:Mb2244.
PATRICi18006628. VBIMycBov88188_2460.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF458290 Genomic DNA. Translation: AAL58468.1.
BX248333 Genomic DNA. Translation: CDO43498.1.
RefSeqiNP_855893.1. NC_002945.3.
WP_003411475.1. NC_002945.3.

3D structure databases

ProteinModelPortaliP0A591.
SMRiP0A591.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCDO43498; CDO43498; Mb2244.
GeneIDi1091369.
KEGGimbo:Mb2244.
PATRICi18006628. VBIMycBov88188_2460.

Phylogenomic databases

HOGENOMiHOG000005157.
KOiK01915.
OMAiKVLNQVG.

Enzyme and pathway databases

BRENDAi6.3.1.2. 3494.

Family and domain databases

Gene3Di3.10.20.70. 1 hit.
3.30.590.10. 1 hit.
InterProiView protein in InterPro
IPR008147. Gln_synt_b-grasp.
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.
PfamiView protein in Pfam
PF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
SMARTiView protein in SMART
SM01230. Gln-synt_C. 1 hit.
SUPFAMiSSF54368. SSF54368. 1 hit.
TIGRFAMsiTIGR00653. GlnA. 1 hit.
PROSITEiView protein in PROSITE
PS00180. GLNA_1. 1 hit.
PS00182. GLNA_ADENYLATION. 1 hit.
PS00181. GLNA_ATP. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiGLN1B_MYCBO
AccessioniPrimary (citable) accession number: P0A591
Secondary accession number(s): Q10377, X2BKH2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: May 10, 2017
This is version 75 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.