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P0A1P6

- GLNA_SALTY

UniProt

P0A1P6 - GLNA_SALTY

Protein

Glutamine synthetase

Gene

glnA

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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

    Keywords - Molecular functioni

    Ligase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciSENT99287:GCTI-4036-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamine synthetase (EC:6.3.1.2)
    Alternative name(s):
    Glutamate--ammonia ligase
    Gene namesi
    Name:glnA
    Ordered Locus Names:STM4007
    OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
    Taxonomic identifieri99287 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
    ProteomesiUP000001014: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 469468Glutamine synthetasePRO_0000153253Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei398 – 3981O-AMP-tyrosineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP0A1P6.
    PRIDEiP0A1P6.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi99287.STM4007.

    Structurei

    Secondary structure

    1
    469
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1210
    Beta strandi17 – 237
    Beta strandi25 – 273
    Beta strandi29 – 357
    Helixi36 – 383
    Helixi41 – 466
    Beta strandi48 – 514
    Helixi52 – 543
    Beta strandi55 – 573
    Turni61 – 633
    Beta strandi65 – 706
    Helixi72 – 743
    Beta strandi77 – 815
    Beta strandi85 – 939
    Turni95 – 973
    Helixi105 – 11814
    Beta strandi123 – 14422
    Beta strandi147 – 1537
    Helixi158 – 1625
    Turni176 – 1783
    Beta strandi180 – 1823
    Turni184 – 1863
    Helixi190 – 20213
    Beta strandi207 – 2126
    Turni216 – 2183
    Beta strandi219 – 2246
    Helixi229 – 24921
    Beta strandi253 – 2553
    Beta strandi260 – 2645
    Beta strandi269 – 2779
    Beta strandi284 – 2874
    Helixi288 – 2903
    Helixi293 – 30412
    Helixi306 – 3138
    Helixi317 – 3215
    Beta strandi323 – 3253
    Beta strandi327 – 3293
    Beta strandi332 – 3387
    Beta strandi342 – 3454
    Helixi352 – 3543
    Beta strandi357 – 3593
    Helixi368 – 38417
    Beta strandi398 – 4003
    Turni403 – 4075
    Helixi415 – 42410
    Helixi427 – 4304
    Helixi431 – 4333
    Helixi437 – 45620
    Helixi460 – 4667

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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. Positions 2-469.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A1P6.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glutamine synthetase family.Curated

    Phylogenomic databases

    eggNOGiCOG0174.
    HOGENOMiHOG000005157.
    KOiK01915.
    OMAiDMLLMPI.
    OrthoDBiEOG6B360N.
    PhylomeDBiP0A1P6.

    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.
    IPR001637. Gln_synth_I_adenylation_site.
    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.
    PS00182. GLNA_ADENYLATION. 1 hit.
    PS00181. GLNA_ATP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0A1P6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSAEHVLTML NEHEVKFVDL RFTDTKGKEQ HVTIPAHQVN AEFFEEGKMF    50
    DGSSIGGWKG INESDMVLMP DASTAVIDPF FADSTLIIRC DILEPGTLQG 100
    YDRDPRSIAK RAEDYLRATG IADTVLFGPE PEFFLFDDIR FGASISGSHV 150
    AIDDIEGAWN SSTKYEGGNK GHRPGVKGGY FPVPPVDSAQ DIRSEMCLVM 200
    EQMGLVVEAH HHEVATAGQN EVATRFNTMT KKADEIQIYK YVVHNVAHRF 250
    GKTATFMPKP MFGDNGSGMH CHMSLAKNGT NLFSGDKYAG LSEQALYYIG 300
    GVIKHAKAIN ALANPTTNSY KRLVPGYEAP VMLAYSARNR SASIRIPVVA 350
    SPKARRIEVR FPDPAANPYL CFAALLMAGL DGIKNKIHPG EAMDKNLYDL 400
    PPEEAKEIPQ VAGSLEEALN ALDLDREFLK AGGVFTDEAI DAYIALRREE 450
    DDRVRMTPHP VEFELYYSV 469
    Length:469
    Mass (Da):51,786
    Last modified:January 23, 2007 - v2
    Checksum:iCD4303E758871E10
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti223 – 2231A → R in CAA59423. 1 PublicationCurated
    Sequence conflicti392 – 3921A → P(PubMed:2879772)Curated
    Sequence conflicti392 – 3921A → P1 PublicationCurated
    Sequence conflicti448 – 4481R → P in AAA27134. (PubMed:2879772)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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_003197.1.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14536 Genomic DNA. Translation: AAA27134.1 .
    AE006468 Genomic DNA. Translation: AAL22846.1 .
    X85104 Genomic DNA. Translation: CAA59423.1 .
    PIRi A25818. AJEBQT.
    RefSeqi NP_462887.1. NC_003197.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1F1H X-ray 2.67 A/B/C/D/E/F/G/H/I/J/K/L 2-469 [» ]
    1F52 X-ray 2.49 A/B/C/D/E/F/G/H/I/J/K/L 2-469 [» ]
    1FPY X-ray 2.89 A/B/C/D/E/F/G/H/I/J/K/L 2-469 [» ]
    1LGR X-ray 2.79 A/B/C/D/E/F/G/H/I/J/K/L 2-469 [» ]
    2GLS X-ray 3.50 A/B/C/D/E/F/G/H/I/J/K/L 1-469 [» ]
    2LGS X-ray 2.80 A/B/C/D/E/F/G/H/I/J/K/L 2-469 [» ]
    ProteinModelPortali P0A1P6.
    SMRi P0A1P6. Positions 2-469.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 99287.STM4007.

    Chemistry

    BindingDBi P0A1P6.
    ChEMBLi CHEMBL5089.
    DrugBanki DB00131. Adenosine monophosphate.

    Proteomic databases

    PaxDbi P0A1P6.
    PRIDEi P0A1P6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAL22846 ; AAL22846 ; STM4007 .
    GeneIDi 1255533.
    KEGGi stm:STM4007.
    PATRICi 32386886. VBISalEnt20916_4223.

    Phylogenomic databases

    eggNOGi COG0174.
    HOGENOMi HOG000005157.
    KOi K01915.
    OMAi DMLLMPI.
    OrthoDBi EOG6B360N.
    PhylomeDBi P0A1P6.

    Enzyme and pathway databases

    BioCyci SENT99287:GCTI-4036-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A1P6.
    PROi P0A1P6.

    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.
    IPR001637. Gln_synth_I_adenylation_site.
    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.
    PS00182. GLNA_ADENYLATION. 1 hit.
    PS00181. GLNA_ATP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence of glutamine synthetase from Salmonella typhimurium and implications for the protein structure."
      Janson C.A., Kayne P.S., Almassy R.J., Grunstein M., Eisenberg D.
      Gene 46:297-300(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: LT2 / SGSC1412 / ATCC 700720.
    3. Kustu S.G.
      Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 133-469.
      Strain: LT2.
    4. "Refined atomic model of glutamine synthetase at 3.5-A resolution."
      Yamashita M.Y., Almassy R.J., Janson C.A., Cascio D., Eisenberg D.
      J. Biol. Chem. 264:17681-17690(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
    5. "The crystal structure of phosphinothricin in the active site of glutamine synthetase illuminates the mechanism of enzymatic inhibition."
      Gill H.S., Eisenberg D.
      Biochemistry 40:1903-1912(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS).

    Entry informationi

    Entry nameiGLNA_SALTY
    AccessioniPrimary (citable) accession number: P0A1P6
    Secondary accession number(s): P06201, Q60007
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 69 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

    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

    External Data

    Dasty 3