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Entry version 161 (12 Aug 2020)
Sequence version 3 (23 Jan 2007)
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Protein

Glutamine synthetase

Gene

glnA

Organism
Bacillus subtilis (strain 168)
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

Glutamine synthetase (GS) is an unusual multitasking protein that functions as an enzyme, a transcription coregulator, and a chaperone in ammonium assimilation and in the regulation of genes involved in nitrogen metabolism (PubMed:25691471). It catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia (PubMed:24158439). Feedback-inhibited GlnA interacts with and regulates the activity of the transcriptional regulator TnrA (PubMed:11719184, PubMed:12139611). During nitrogen limitation, TnrA is in its DNA-binding active state and turns on the transcription of genes required for nitrogen assimilation (PubMed:11719184, PubMed:12139611, PubMed:25691471). Under conditions of nitrogen excess, feedback-inhibited GlnA forms a stable complex with TnrA, which inhibits its DNA-binding activity (PubMed:11719184, PubMed:12139611, PubMed:25691471). In contrast, feedback-inhibited GlnA acts as a chaperone to stabilize the DNA-binding activity of GlnR, which represses the transcription of nitrogen assimilation genes (PubMed:25691471).4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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+2 PublicationsNote: Binds 2 Mg2+ ions per subunit.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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

Completely inhibited by glutamine and partially inhibited by glycine, alanine and AMP (PubMed:4149044, PubMed:24158439). Also inhibited by L-methionine-SR-sulphoximine (Met-Sox) (PubMed:8093698, PubMed:24158439).3 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.18 mM for ammonium1 Publication
  2. KM=0.83 mM for hydroxylamine1 Publication
  3. KM=2.3 mM for ATP1 Publication
  4. KM=2.4 mM for ATP1 Publication
  5. KM=12 mM for glutamine1 Publication
  6. KM=24 mM for glutamate1 Publication
  7. KM=27 mM for glutamate1 Publication
  1. Vmax=3.7 µmol/min/mg enzyme1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei62Important for inhibition by glutamine1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi132Magnesium 1Combined sources2 Publications1
Metal bindingi134Magnesium 2Combined sources2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei184ATPBy similarity1
Metal bindingi189Magnesium 2Combined sources2 Publications1
Metal bindingi196Magnesium 2Combined sources2 Publications1
Binding sitei241L-glutamate; via carbonyl oxygenCombined sources2 Publications1
Metal bindingi245Magnesium 1; via pros nitrogenCombined sources2 Publications1
Binding sitei249ATPBy similarity1
Binding sitei298L-glutamateBy similarity1
Binding sitei304L-glutamateBy similarity1
Binding sitei316ATPBy similarity1
Binding sitei316L-glutamateBy similarity1
Binding sitei321ATPBy similarity1
Metal bindingi333Magnesium 1Combined sources2 Publications1
Binding sitei335L-glutamateBy similarity1

<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: UniProtKB-EC
  • glutamine binding Source: CAFA
  • metal ion binding Source: UniProtKB-KW
  • transcription factor binding Source: CAFA

GO - Biological processi

<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
BSUB:BSU17460-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
6.3.1.2, 658

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P12425

Protein family/group databases

MoonProt database of moonlighting proteins

More...
MoonProti
P12425

<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%5Fand%5Ftaxonomy%5Fsection">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 synthetase1 Publication (EC:6.3.1.22 Publications)
Short name:
GS1 Publication
Alternative name(s):
Glutamate--ammonia ligaseCurated
Glutamine synthetase I alphaCurated
Short name:
GSI alphaCurated
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:glnA1 Publication
Ordered Locus Names:BSU17460
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiBacillus subtilis (strain 168)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri224308 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000001570 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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

<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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

In cells lacking this gene, expression of glnR, tnrA, nasB, nrgAB, gabP and ure genes is derepressed.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi59G → R: Unable to form stable complex with TnrA. In the presence of glutamine, this mutant derepresses amtB-lacZ fusion and glnRA-lacZ fusion. 1 Publication1
Mutagenesisi62R → A: Highly resistant to inhibition by glutamine and AMP. Regulation by TnrA and GlnR is abolished. Only small differences (less than 2-fold) in its steady-state kinetic constants compared with the wild-type. Similar sensitivity to Met-Sox that compared to the wild-ytpe. 1 Publication1
Mutagenesisi190V → A: Unable to form stable complex with TnrA. In the presence of glutamine, this mutant partially relieves expression of the glnRA-lacZ fusion, but has no effect on the TnrA-dependent regulation of amtB-lacZ fusion. Resistant to inhibition by MetSox. 2 Publications1
Mutagenesisi302G → E: Unable to form stable complex with TnrA. In the presence of glutamine, amtB-lacZ fusion is only 4-fold regulated by TnrA, whereas glnRA-lacZ fusion is derepressed. This mutant retains enzymatic specific activity with a 2-fold decrease of the affinity for glutamate and glutamine compared to the wild-type. Slightly less sensitive to inhibition by glutamine. 1 Publication1
Mutagenesisi304E → A: Highly resistant to Met-Sox inhibition. 8- and 2-fold increase of the affinity for glutamate and ATP, respectively. Strong decrease of the affinity for ammonium. 1 Publication1
Mutagenesisi306P → H: Unable to form stable complex with TnrA. In the presence of glutamine, this mutant completely derepresses glnRA-lacZ fusion, whereas amtB-lacZ fusion expression is only partially derepresses. 1 Publication1
Mutagenesisi424E → K: Unable to form stable complex with TnrA. In the presence of glutamine, this mutant derepresses amtB-lacZ fusion and glnRA-lacZ fusion. Although it is defective in regulation, this mutant retains enzymatic specific activity and similar affinity for ATP, glutamate and glutamine compared to the wild-type. Slightly less sensitive to inhibition by glutamine. 2 Publications1

<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%5Fprocessing%5Fsection">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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001532332 – 444Glutamine synthetaseAdd BLAST443

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P12425

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

More...
PaxDbi
P12425

PRoteomics IDEntifications database

More...
PRIDEi
P12425

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Repressed by GlnR under conditions of nitrogen excess (PubMed:2573733). Repressed by TnrA under conditions of nitrogen limitation.2 Publications

<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%5Fsection">'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%5Fsection">'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 hexagons. In its feedback-inhibited form, interacts with TnrA in order to block its DNA-binding activity. This inhibitory effect is the highest when both glutamine and AMP are present.

3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

Database of interacting proteins

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DIPi
DIP-29670N

Protein interaction database and analysis system

More...
IntActi
P12425, 4 interactors

Molecular INTeraction database

More...
MINTi
P12425

STRING: functional protein association networks

More...
STRINGi
224308.BSU17460

<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

Secondary structure

1444
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
P12425

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
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>Regioni240 – 241L-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

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eggNOGi
COG0174, Bacteria

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P12425

KEGG Orthology (KO)

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KOi
K01915

Identification of Orthologs from Complete Genome Data

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OMAi
PHPHEFE

Database for complete collections of gene phylogenies

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PhylomeDBi
P12425

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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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

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

Superfamily database of structural and functional annotation

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SUPFAMi
SSF54368, SSF54368, 1 hit
SSF55931, SSF55931, 1 hit

TIGRFAMs; a protein family database

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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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P12425-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAKYTREDIE KLVKEENVKY IRLQFTDILG TIKNVEIPVS QLGKALDNKV
60 70 80 90 100
MFDGSSIEGF VRIEESDMYL YPDLNTFVIF PWTAEKGKVA RFICDIYNPD
110 120 130 140 150
GTPFEGDPRN NLKRILKEME DLGFSDFNLG PEPEFFLFKL DEKGEPTLEL
160 170 180 190 200
NDKGGYFDLA PTDLGENCRR DIVLELEEMG FEIEASHHEV APGQHEIDFK
210 220 230 240 250
YAGAVRSCDD IQTFKLVVKT IARKHGLHAT FMPKPLFGVN GSGMHCNLSL
260 270 280 290 300
FKNGVNAFFD ENADLQLSET AKHFIAGIVK HATSFTAVTN PTVNSYKRLV
310 320 330 340 350
PGYEAPCYVA WSAQNRSPLI RIPASRGIST RVEVRSVDPA ANPYLALSVL
360 370 380 390 400
LAAGLDGIKN KLEAPAPIDR NIYVMSKEER MENGIVDLPA TLAEALEEFK
410 420 430 440
SNEVMVKALG EHLFEHFIEA KEIEWDMFRT QVHPWEREQY MSQY
Length:444
Mass (Da):50,278
Last modified:January 23, 2007 - v3
<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:i83A5657CE1388AB0
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti10E → V in strain: PCI 219. 1
Natural varianti43G → E in strain: PCI 219. 1
Natural varianti253N → D in strain: PCI 219. 1
Natural varianti259F → Y in strain: PCI 219. 1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M22811 Genomic DNA Translation: AAA83376.1
D00854 Genomic DNA Translation: BAA00730.1
U66480 Genomic DNA Translation: AAB41080.1
AL009126 Genomic DNA Translation: CAB13630.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JT0392, AJBSQS

NCBI Reference Sequences

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RefSeqi
NP_389628.1, NC_000964.3
WP_003231737.1, NZ_JNCM01000035.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CAB13630; CAB13630; BSU17460

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
51991359
940020

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bsu:BSU17460

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|224308.179.peg.1894

<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
M22811 Genomic DNA Translation: AAA83376.1
D00854 Genomic DNA Translation: BAA00730.1
U66480 Genomic DNA Translation: AAB41080.1
AL009126 Genomic DNA Translation: CAB13630.1
PIRiJT0392, AJBSQS
RefSeqiNP_389628.1, NC_000964.3
WP_003231737.1, NZ_JNCM01000035.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FWXmodel-A/B/C/D1-444[»]
4LNFX-ray2.95A/B/C/D/E/F/G/H/I/J/K/L2-444[»]
4LNIX-ray2.58A/B/C/D/E/F/G/H/I/J/K/L2-444[»]
4LNKX-ray2.87A/B/C/D/E/F2-444[»]
4LNNX-ray3.10A/B/C/D/E/F/G/H/I/J/K/L2-444[»]
4LNOX-ray2.90A/B/C/D/E/F2-444[»]
4S0RX-ray3.50A/B/C/D/E/F/G/H/I/J/K/L/M/N1-444[»]
SMRiP12425
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

DIPiDIP-29670N
IntActiP12425, 4 interactors
MINTiP12425
STRINGi224308.BSU17460

Protein family/group databases

MoonProtiP12425

Proteomic databases

jPOSTiP12425
PaxDbiP12425
PRIDEiP12425

Genome annotation databases

EnsemblBacteriaiCAB13630; CAB13630; BSU17460
GeneIDi51991359
940020
KEGGibsu:BSU17460
PATRICifig|224308.179.peg.1894

Phylogenomic databases

eggNOGiCOG0174, Bacteria
InParanoidiP12425
KOiK01915
OMAiPHPHEFE
PhylomeDBiP12425

Enzyme and pathway databases

BioCyciBSUB:BSU17460-MONOMER
BRENDAi6.3.1.2, 658
SABIO-RKiP12425

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

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiGLN1A_BACSU
<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: P12425
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: August 12, 2020
This is version 161 of the entry and version 3 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

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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