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P0A1P6

- GLNA_SALTY

UniProt

P0A1P6 - GLNA_SALTY

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Protein

Glutamine synthetase

Gene

glnA

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

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

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-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        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)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:
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_003197.1.

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 .
PIRi A25818. AJEBQT.
RefSeqi NP_462887.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 71 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