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Entry version 114 (13 Feb 2019)
Sequence version 2 (23 Jan 2007)
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Protein

Glutamine synthetase

Gene

glnA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

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

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

The activity of this enzyme could be controlled by adenylation under conditions of abundant glutamine.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi130Magnesium 1By similarity1
Metal bindingi132Magnesium 2By similarity1
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei208ATPBy similarity1
Metal bindingi213Magnesium 2By similarity1
Metal bindingi221Magnesium 2By similarity1
Binding sitei266L-glutamate; via carbonyl oxygenBy similarity1
Metal bindingi270Magnesium 1; via pros nitrogenBy similarity1
Binding sitei274ATPBy similarity1
Binding sitei322L-glutamateBy similarity1
Binding sitei328L-glutamateBy similarity1
Binding sitei340ATPBy similarity1
Binding sitei340L-glutamateBy similarity1
Binding sitei345ATPBy similarity1
Binding sitei353ATPBy similarity1
Metal bindingi358Magnesium 1By similarity1
Binding sitei360L-glutamateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi272 – 274ATPBy similarity3

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • glutamate-ammonia ligase activity Source: EcoCyc
  • identical protein binding Source: IntAct
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • ammonia assimilation cycle Source: EcoCyc
  • glutamine biosynthetic process Source: GO_Central
  • nitrogen utilization Source: EcoCyc
  • response to radiation Source: EcoCyc

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:GLUTAMINESYN-MONOMER
ECOL316407:JW3841-MONOMER
MetaCyc:GLUTAMINESYN-MONOMER

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P0A9C5

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Glutamine synthetaseBy similarity (EC:6.3.1.2By similarity)
Short name:
GSBy similarity
Alternative name(s):
Glutamate--ammonia ligaseCurated
Glutamine synthetase I betaBy similarity
Short name:
GSI betaBy similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:glnABy similarity
Ordered Locus Names:b3870, JW3841
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG10383 glnA

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3789

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001532352 – 469Glutamine synthetaseAdd BLAST468

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei398O-AMP-tyrosine2 Publications1

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P0A9C5

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0A9C5

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P0A9C5

PRoteomics IDEntifications database

More...
PRIDEi
P0A9C5

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...
SWISS-2DPAGEi
P0A9C5

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-909063,EBI-909063

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4262630, 46 interactors

Database of interacting proteins

More...
DIPi
DIP-9777N

Protein interaction database and analysis system

More...
IntActi
P0A9C5, 10 interactors

STRING: functional protein association networks

More...
STRINGi
316385.ECDH10B_4060

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P0A9C5

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P0A9C5

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P0A9C5

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni265 – 266L-glutamate bindingBy similarity2

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the glutamine synthetase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105C5F Bacteria
COG0174 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000005157

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0A9C5

KEGG Orthology (KO)

More...
KOi
K01915

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0A9C5

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.10.20.70, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR008147 Gln_synt_b-grasp
IPR036651 Gln_synt_N
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

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00120 Gln-synt_C, 1 hit
PF03951 Gln-synt_N, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01230 Gln-synt_C, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54368 SSF54368, 1 hit
SSF55931 SSF55931, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00653 GlnA, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00180 GLNA_1, 1 hit
PS00182 GLNA_ADENYLATION, 1 hit
PS00181 GLNA_ATP, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P0A9C5-1 [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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i0AFC05724CDEBA36
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti90C → S in AAA23879 (PubMed:2874141).Curated1
Sequence conflicti108 – 109IA → MS in AAA23879 (PubMed:2874141).Curated2
Sequence conflicti197C → S in AAA23879 (PubMed:2874141).Curated1
Sequence conflicti228T → I in CAA28806 (PubMed:2882477).Curated1
Sequence conflicti247 – 248AH → VRN in CAA28806 (PubMed:2882477).Curated2
Sequence conflicti305 – 306HA → QP in CAA28806 (PubMed:2882477).Curated2
Sequence conflicti394 – 395DK → KD AA sequence (PubMed:5543675).Curated2
Sequence conflicti394 – 395DK → KD AA sequence (PubMed:4904088).Curated2

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X05173 Genomic DNA Translation: CAA28806.1
M13746 Genomic DNA Translation: AAA23879.1
L19201 Genomic DNA Translation: AAB03004.1
U00096 Genomic DNA Translation: AAC76867.1
AP009048 Genomic DNA Translation: BAE77439.1
J01618 Genomic DNA Translation: AAA98066.1
M10421 Genomic DNA Translation: AAA23882.1
K02176 Genomic DNA Translation: AAA23880.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S40815 AJECQ

NCBI Reference Sequences

More...
RefSeqi
NP_418306.1, NC_000913.3
WP_001271717.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC76867; AAC76867; b3870
BAE77439; BAE77439; BAE77439

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
948370

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW3841
eco:b3870

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.2841

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05173 Genomic DNA Translation: CAA28806.1
M13746 Genomic DNA Translation: AAA23879.1
L19201 Genomic DNA Translation: AAB03004.1
U00096 Genomic DNA Translation: AAC76867.1
AP009048 Genomic DNA Translation: BAE77439.1
J01618 Genomic DNA Translation: AAA98066.1
M10421 Genomic DNA Translation: AAA23882.1
K02176 Genomic DNA Translation: AAA23880.1
PIRiS40815 AJECQ
RefSeqiNP_418306.1, NC_000913.3
WP_001271717.1, NZ_LN832404.1

3D structure databases

ProteinModelPortaliP0A9C5
SMRiP0A9C5
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262630, 46 interactors
DIPiDIP-9777N
IntActiP0A9C5, 10 interactors
STRINGi316385.ECDH10B_4060

Chemistry databases

BindingDBiP0A9C5
ChEMBLiCHEMBL3789

2D gel databases

SWISS-2DPAGEiP0A9C5

Proteomic databases

EPDiP0A9C5
jPOSTiP0A9C5
PaxDbiP0A9C5
PRIDEiP0A9C5

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76867; AAC76867; b3870
BAE77439; BAE77439; BAE77439
GeneIDi948370
KEGGiecj:JW3841
eco:b3870
PATRICifig|1411691.4.peg.2841

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB0378
EcoGeneiEG10383 glnA

Phylogenomic databases

eggNOGiENOG4105C5F Bacteria
COG0174 LUCA
HOGENOMiHOG000005157
InParanoidiP0A9C5
KOiK01915
PhylomeDBiP0A9C5

Enzyme and pathway databases

BioCyciEcoCyc:GLUTAMINESYN-MONOMER
ECOL316407:JW3841-MONOMER
MetaCyc:GLUTAMINESYN-MONOMER
SABIO-RKiP0A9C5

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P0A9C5

Family and domain databases

Gene3Di3.10.20.70, 1 hit
InterProiView protein in InterPro
IPR008147 Gln_synt_b-grasp
IPR036651 Gln_synt_N
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
SSF55931 SSF55931, 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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiGLN1B_ECOLI
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0A9C5
Secondary accession number(s): P06711, Q2M8G7
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: February 13, 2019
This is version 114 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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