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Protein

Glutamine synthetase

Gene

glnA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 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: CACAO
  2. nitrogen fixation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBSUB:BSU17460-MONOMER.
SABIO-RKP12425.

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:BSU17460
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU17460. [Micado]

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 444443Glutamine synthetasePRO_0000153233Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei373 – 3731O-AMP-tyrosineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP12425.

Expressioni

Inductioni

Repressed by GlnR under conditions of nitrogen excess. Repressed by TnrA under conditions of nitrogen limitation.

Interactioni

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.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
tnrAQ456668EBI-6402863,EBI-8507041

Protein-protein interaction databases

DIPiDIP-29670N.
IntActiP12425. 4 interactions.
MINTiMINT-224371.
STRINGi224308.BSU17460.

Structurei

Secondary structure

1
444
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 1611Combined sources
Beta strandi20 – 267Combined sources
Beta strandi32 – 387Combined sources
Helixi39 – 413Combined sources
Helixi42 – 465Combined sources
Beta strandi51 – 533Combined sources
Helixi54 – 563Combined sources
Helixi63 – 653Combined sources
Beta strandi67 – 8014Combined sources
Helixi81 – 833Combined sources
Helixi84 – 874Combined sources
Beta strandi89 – 979Combined sources
Beta strandi99 – 1035Combined sources
Helixi108 – 12114Combined sources
Beta strandi125 – 1339Combined sources
Beta strandi135 – 1406Combined sources
Beta strandi142 – 1443Combined sources
Beta strandi146 – 1516Combined sources
Turni160 – 1623Combined sources
Beta strandi163 – 1653Combined sources
Helixi166 – 17813Combined sources
Beta strandi183 – 1886Combined sources
Beta strandi194 – 1996Combined sources
Helixi204 – 22421Combined sources
Beta strandi227 – 2304Combined sources
Beta strandi244 – 2529Combined sources
Beta strandi261 – 2633Combined sources
Helixi264 – 2663Combined sources
Helixi269 – 28921Combined sources
Helixi295 – 2984Combined sources
Beta strandi311 – 3133Combined sources
Beta strandi316 – 3227Combined sources
Helixi327 – 3293Combined sources
Beta strandi332 – 3343Combined sources
Helixi343 – 35917Combined sources
Helixi372 – 3743Combined sources
Helixi377 – 3837Combined sources
Helixi392 – 4009Combined sources
Helixi403 – 4097Combined sources
Helixi411 – 43020Combined sources
Helixi434 – 4407Combined sources
Turni441 – 4433Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FWXmodel-A/B/C/D1-444[»]
3QAJX-ray3.05A/B/C/D/E/F/G/H/I/J/K/L1-444[»]
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[»]
ProteinModelPortaliP12425.
SMRiP12425. Positions 5-443.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glutamine synthetase family.Curated

Phylogenomic databases

eggNOGiCOG0174.
HOGENOMiHOG000005156.
InParanoidiP12425.
KOiK01915.
OMAiKVLNQVG.
OrthoDBiEOG6B360N.
PhylomeDBiP12425.

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.

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
Checksum:i83A5657CE1388AB0
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti10 – 101E → V in strain: PCI 219.
Natural varianti43 – 431G → E in strain: PCI 219.
Natural varianti253 – 2531N → D in strain: PCI 219.
Natural varianti259 – 2591F → Y in strain: PCI 219.

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.

Genome annotation databases

EnsemblBacteriaiCAB13630; CAB13630; BSU17460.
GeneIDi940020.
KEGGibsu:BSU17460.
PATRICi18975307. VBIBacSub10457_1845.

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:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FWXmodel-A/B/C/D1-444[»]
3QAJX-ray3.05A/B/C/D/E/F/G/H/I/J/K/L1-444[»]
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[»]
ProteinModelPortaliP12425.
SMRiP12425. Positions 5-443.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29670N.
IntActiP12425. 4 interactions.
MINTiMINT-224371.
STRINGi224308.BSU17460.

Proteomic databases

PaxDbiP12425.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13630; CAB13630; BSU17460.
GeneIDi940020.
KEGGibsu:BSU17460.
PATRICi18975307. VBIBacSub10457_1845.

Organism-specific databases

GenoListiBSU17460. [Micado]

Phylogenomic databases

eggNOGiCOG0174.
HOGENOMiHOG000005156.
InParanoidiP12425.
KOiK01915.
OMAiKVLNQVG.
OrthoDBiEOG6B360N.
PhylomeDBiP12425.

Enzyme and pathway databases

BioCyciBSUB:BSU17460-MONOMER.
SABIO-RKP12425.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of the Bacillus subtilis glutamine synthetase gene region."
    Strauch M.A., Aronson A.I., Brown S.W., Schreier H.J., Sonenshein A.L.
    Gene 71:257-265(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The complete nucleotide sequence of the glutamine synthetase gene (glnA) of Bacillus subtilis."
    Nakano Y., Tanaka E., Kato C., Kimura K., Horikoshi K.
    FEMS Microbiol. Lett. 48:81-86(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-21.
    Strain: ATCC 6633 / PCI 219 / NRS 231.
  3. "Sequencing of a 26 kb region of the Bacillus subtilis genome downstream of spoVJ."
    Borchert S., Klein C., Piksa B., Hammelmann M., Entian K.-D.
    Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  5. "Bacillus subtilis glutamine synthetase controls gene expression through a protein-protein interaction with transcription factor TnrA."
    Wray L.V. Jr., Zalieckas J.M., Fisher S.H.
    Cell 107:427-435(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TNRA.

Entry informationi

Entry nameiGLNA_BACSU
AccessioniPrimary (citable) accession number: P12425
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 128 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Elevated Mn2+ concentration reduces sensitivity of GlnA to feedback inhibitors Gln and AMP.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.