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Protein

Glutamine synthetase

Gene

glnA

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia.1 Publication

Catalytic activityi

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

Cofactori

Mn2+4 PublicationsNote: Binds 2 Mn2+ ions per subunit.4 Publications

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-398. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) of GlnE activates GlnA by removing the adenylyl group by phosphorolysis. The fully adenylated enzyme complex is inactive.By similarity

Kineticsi

  1. KM=0.58 mM for ATP1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi130Manganese 1Combined sources3 Publications1
    Metal bindingi132Manganese 2Combined sources3 Publications1
    Binding sitei208ATPCombined sources1 Publication1
    Metal bindingi213Manganese 2Combined sources3 Publications1
    Metal bindingi221Manganese 2Combined sources3 Publications1
    Binding sitei266L-glutamate; via oxygen carbonylBy similarity1
    Metal bindingi270Manganese 1; via pros nitrogenCombined sources3 Publications1
    Binding sitei274ATPBy similarity1
    Binding sitei322L-glutamateCombined sources1 Publication1 Publication1
    Binding sitei328L-glutamateCombined sources1 Publication1
    Binding sitei340ATPBy similarity1
    Binding sitei340L-glutamateBy similarity1
    Binding sitei345ATPBy similarity1
    Binding sitei353ATPBy similarity1
    Metal bindingi358Manganese 1Combined sources4 Publications1
    Binding sitei360L-glutamateCombined sources1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi272 – 274ATPCombined sources1 Publication3

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionLigase
    LigandATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi6.3.1.2. 5542.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamine synthetase1 Publication (EC:6.3.1.21 Publication)
    Short name:
    GS1 Publication
    Alternative name(s):
    Glutamate--ammonia ligaseCurated
    Glutamine synthetase I betaCurated
    Short name:
    GSI betaCurated
    Gene namesi
    Name:glnA1 Publication
    Ordered Locus Names:STM4007
    OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
    Taxonomic identifieri99287 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
    Proteomesi
    • UP000001014 Componenti: Chromosome

    Subcellular locationi

    • Cytoplasm By similarity

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Chemistry databases

    ChEMBLiCHEMBL5089.
    DrugBankiDB02663. 2-Amino-4-(Hydroxymethyl-Phosphinyl)Butanoic Acid.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001532531 – 469Glutamine synthetaseAdd BLAST469

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei398O-AMP-tyrosineBy similarity1

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP0A1P6.
    PRIDEiP0A1P6.

    Interactioni

    Subunit structurei

    Oligomer of 12 subunits arranged in the form of two hexameric ring.4 Publications

    Protein-protein interaction databases

    DIPiDIP-61253N.
    STRINGi99287.STM4007.

    Chemistry databases

    BindingDBiP0A1P6.

    Structurei

    Secondary structure

    1469
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi3 – 12Combined sources10
    Beta strandi17 – 23Combined sources7
    Beta strandi25 – 27Combined sources3
    Beta strandi29 – 35Combined sources7
    Helixi36 – 38Combined sources3
    Helixi41 – 46Combined sources6
    Beta strandi48 – 51Combined sources4
    Helixi52 – 54Combined sources3
    Beta strandi55 – 57Combined sources3
    Turni61 – 63Combined sources3
    Beta strandi65 – 70Combined sources6
    Helixi72 – 74Combined sources3
    Beta strandi77 – 81Combined sources5
    Beta strandi85 – 93Combined sources9
    Turni95 – 97Combined sources3
    Helixi105 – 118Combined sources14
    Beta strandi123 – 144Combined sources22
    Beta strandi147 – 153Combined sources7
    Helixi158 – 162Combined sources5
    Turni176 – 178Combined sources3
    Beta strandi180 – 182Combined sources3
    Turni184 – 186Combined sources3
    Helixi190 – 202Combined sources13
    Beta strandi207 – 212Combined sources6
    Turni216 – 218Combined sources3
    Beta strandi219 – 224Combined sources6
    Helixi229 – 249Combined sources21
    Beta strandi253 – 255Combined sources3
    Beta strandi260 – 264Combined sources5
    Beta strandi269 – 277Combined sources9
    Beta strandi284 – 287Combined sources4
    Helixi288 – 290Combined sources3
    Helixi293 – 304Combined sources12
    Helixi306 – 313Combined sources8
    Helixi317 – 321Combined sources5
    Beta strandi323 – 325Combined sources3
    Beta strandi327 – 329Combined sources3
    Beta strandi332 – 338Combined sources7
    Beta strandi342 – 345Combined sources4
    Helixi352 – 354Combined sources3
    Beta strandi357 – 359Combined sources3
    Helixi368 – 384Combined sources17
    Beta strandi398 – 400Combined sources3
    Turni403 – 407Combined sources5
    Helixi415 – 424Combined sources10
    Helixi427 – 430Combined sources4
    Helixi431 – 433Combined sources3
    Helixi437 – 456Combined sources20
    Helixi460 – 466Combined sources7

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1F1HX-ray2.67A/B/C/D/E/F/G/H/I/J/K/L2-469[»]
    1F52X-ray2.49A/B/C/D/E/F/G/H/I/J/K/L2-469[»]
    1FPYX-ray2.89A/B/C/D/E/F/G/H/I/J/K/L2-469[»]
    1LGRX-ray2.79A/B/C/D/E/F/G/H/I/J/K/L2-469[»]
    2GLSX-ray3.50A/B/C/D/E/F/G/H/I/J/K/L1-469[»]
    2LGSX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L2-469[»]
    ProteinModelPortaliP0A1P6.
    SMRiP0A1P6.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A1P6.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni265 – 266L-glutamate bindingCombined sources1 Publication2 Publications2

    Sequence similaritiesi

    Belongs to the glutamine synthetase family.Curated

    Phylogenomic databases

    eggNOGiENOG4105C5F. Bacteria.
    COG0174. LUCA.
    HOGENOMiHOG000005157.
    KOiK01915.
    OMAiKVLNQVG.
    PhylomeDBiP0A1P6.

    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.

    P0A1P6-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSAEHVLTML NEHEVKFVDL RFTDTKGKEQ HVTIPAHQVN AEFFEEGKMF
    60 70 80 90 100
    DGSSIGGWKG INESDMVLMP DASTAVIDPF FADSTLIIRC DILEPGTLQG
    110 120 130 140 150
    YDRDPRSIAK RAEDYLRATG IADTVLFGPE PEFFLFDDIR FGASISGSHV
    160 170 180 190 200
    AIDDIEGAWN SSTKYEGGNK GHRPGVKGGY FPVPPVDSAQ DIRSEMCLVM
    210 220 230 240 250
    EQMGLVVEAH HHEVATAGQN EVATRFNTMT KKADEIQIYK YVVHNVAHRF
    260 270 280 290 300
    GKTATFMPKP MFGDNGSGMH CHMSLAKNGT NLFSGDKYAG LSEQALYYIG
    310 320 330 340 350
    GVIKHAKAIN ALANPTTNSY KRLVPGYEAP VMLAYSARNR SASIRIPVVA
    360 370 380 390 400
    SPKARRIEVR FPDPAANPYL CFAALLMAGL DGIKNKIHPG EAMDKNLYDL
    410 420 430 440 450
    PPEEAKEIPQ VAGSLEEALN ALDLDREFLK AGGVFTDEAI DAYIALRREE
    460
    DDRVRMTPHP VEFELYYSV
    Length:469
    Mass (Da):51,786
    Last modified:January 23, 2007 - v2
    Checksum:iCD4303E758871E10
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti223A → R in CAA59423 (Ref. 3) Curated1
    Sequence conflicti392A → P in AAA27134 (PubMed:2879772).Curated1
    Sequence conflicti392A → P in CAA59423 (Ref. 3) Curated1
    Sequence conflicti448R → P in AAA27134 (PubMed:2879772).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M14536 Genomic DNA. Translation: AAA27134.1.
    AE006468 Genomic DNA. Translation: AAL22846.1.
    X85104 Genomic DNA. Translation: CAA59423.1.
    PIRiA25818. AJEBQT.
    RefSeqiNP_462887.1. NC_003197.2.
    WP_001271699.1. NC_003197.2.

    Genome annotation databases

    EnsemblBacteriaiAAL22846; AAL22846; STM4007.
    GeneIDi1255533.
    KEGGistm:STM4007.
    PATRICi32386886. VBISalEnt20916_4223.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M14536 Genomic DNA. Translation: AAA27134.1.
    AE006468 Genomic DNA. Translation: AAL22846.1.
    X85104 Genomic DNA. Translation: CAA59423.1.
    PIRiA25818. AJEBQT.
    RefSeqiNP_462887.1. NC_003197.2.
    WP_001271699.1. NC_003197.2.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1F1HX-ray2.67A/B/C/D/E/F/G/H/I/J/K/L2-469[»]
    1F52X-ray2.49A/B/C/D/E/F/G/H/I/J/K/L2-469[»]
    1FPYX-ray2.89A/B/C/D/E/F/G/H/I/J/K/L2-469[»]
    1LGRX-ray2.79A/B/C/D/E/F/G/H/I/J/K/L2-469[»]
    2GLSX-ray3.50A/B/C/D/E/F/G/H/I/J/K/L1-469[»]
    2LGSX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L2-469[»]
    ProteinModelPortaliP0A1P6.
    SMRiP0A1P6.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-61253N.
    STRINGi99287.STM4007.

    Chemistry databases

    BindingDBiP0A1P6.
    ChEMBLiCHEMBL5089.
    DrugBankiDB02663. 2-Amino-4-(Hydroxymethyl-Phosphinyl)Butanoic Acid.

    Proteomic databases

    PaxDbiP0A1P6.
    PRIDEiP0A1P6.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAL22846; AAL22846; STM4007.
    GeneIDi1255533.
    KEGGistm:STM4007.
    PATRICi32386886. VBISalEnt20916_4223.

    Phylogenomic databases

    eggNOGiENOG4105C5F. Bacteria.
    COG0174. LUCA.
    HOGENOMiHOG000005157.
    KOiK01915.
    OMAiKVLNQVG.
    PhylomeDBiP0A1P6.

    Enzyme and pathway databases

    BRENDAi6.3.1.2. 5542.

    Miscellaneous databases

    EvolutionaryTraceiP0A1P6.

    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_SALTY
    AccessioniPrimary (citable) accession number: P0A1P6
    Secondary accession number(s): P06201, Q60007
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 23, 2007
    Last modified: April 12, 2017
    This is version 86 of the entry and version 2 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. 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.