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P0A9C8

- GLNA_SHIFL

UniProt

P0A9C8 - GLNA_SHIFL

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Protein

Glutamine synthetase

Gene

glnA

Organism
Shigella flexneri
Status
Reviewed - 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

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:SF3940, S3806
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
ProteomesiUP000001006: Chromosome, UP000002673: Chromosome

Subcellular locationi

Cytoplasm Curated

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 – 11RemovedBy similarity
Chaini2 – 469468Glutamine synthetasePRO_0000153254Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP0A9C8.
PRIDEiP0A9C8.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi198214.SF3940.

Structurei

3D structure databases

ProteinModelPortaliP0A9C8.
SMRiP0A9C8. Positions 2-469.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glutamine synthetase family.Curated

Phylogenomic databases

eggNOGiCOG0174.
HOGENOMiHOG000005157.
KOiK01915.
OMAiDMLLMPI.
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.
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.

P0A9C8-1 [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 RAEDYLRSTG IADTVLFGPE PEFFLFDDIR FGSSISGSHV
160 170 180 190 200
AIDDIEGAWN SSTQYEGGNK GHRPAVKGGY FPVPPVDSAQ DIRSEMCLVM
210 220 230 240 250
EQMGLVVEAH HHEVATAGQN EVATRFNTMT KKADEIQIYK YVVHNVAHRF
260 270 280 290 300
GKTATFMPKP MFGDNGSGMH CHMSLSKNGV NLFAGDKYAG LSEQALYYIG
310 320 330 340 350
GVIKHAKAIN ALANPTTNSY KRLVPGYEAP VMLAYSARNR SASIRIPVVS
360 370 380 390 400
SPKARRIEVR FPDPAANPYL CFAALLMAGL DGIKNKIHPG EAMDKNLYDL
410 420 430 440 450
PPEEAKEIPQ VAGSLEEALN ELDLDREFLK AGGVFTDEAI DAYIALRREE
460
DDRVRMTPHP VEFELYYSV
Length:469
Mass (Da):51,904
Last modified:January 23, 2007 - v2
Checksum:i0AFC05724CDEBA36
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005674 Genomic DNA. Translation: AAN45375.1.
AE014073 Genomic DNA. Translation: AAP18823.1.
RefSeqiNP_709668.1. NC_004337.2.
NP_839012.1. NC_004741.1.

Genome annotation databases

EnsemblBacteriaiAAN45375; AAN45375; SF3940.
AAP18823; AAP18823; S3806.
GeneIDi1025868.
1080021.
KEGGisfl:SF3940.
sfx:S3806.
PATRICi18709477. VBIShiFle31049_4163.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005674 Genomic DNA. Translation: AAN45375.1 .
AE014073 Genomic DNA. Translation: AAP18823.1 .
RefSeqi NP_709668.1. NC_004337.2.
NP_839012.1. NC_004741.1.

3D structure databases

ProteinModelPortali P0A9C8.
SMRi P0A9C8. Positions 2-469.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 198214.SF3940.

Chemistry

BindingDBi P0A9C8.

Proteomic databases

PaxDbi P0A9C8.
PRIDEi P0A9C8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAN45375 ; AAN45375 ; SF3940 .
AAP18823 ; AAP18823 ; S3806 .
GeneIDi 1025868.
1080021.
KEGGi sfl:SF3940.
sfx:S3806.
PATRICi 18709477. VBIShiFle31049_4163.

Phylogenomic databases

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

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. "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
    Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y.
    , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
    Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 301 / Serotype 2a.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700930 / 2457T / Serotype 2a.

Entry informationi

Entry nameiGLNA_SHIFL
AccessioniPrimary (citable) accession number: P0A9C8
Secondary accession number(s): P06711
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 68 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3