Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P19064

- GLNA_BACCE

UniProt

P19064 - GLNA_BACCE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Glutamine synthetase

Gene

glnA

Organism
Bacillus cereus
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine.

Enzyme regulationi

Not regulated by post-translational modification and not subject to feedback inhibition.

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
OrganismiBacillus cereus
Taxonomic identifieri1396 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

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 – 11Removed1 Publication
Chaini2 – 444443Glutamine synthetasePRO_0000153232Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP19064.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glutamine synthetase family.Curated

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.

P19064-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MARYTKEDIF RLAKEENVKY IRLQFTDLLG VIKNVEIPVS QLTKALDNKM
60 70 80 90 100
MFDGSSIEGF VRIEESDMYL YPDLDTWVIF PWTAEKGKVA RLICDIYNAD
110 120 130 140 150
GTPFEGDPRN NLKRVLKEME ALGFSDFNLG PEPEFFLFKV DEKGNPTLEL
160 170 180 190 200
NDNGGYFDLA PMDLGENCRR DIVLELEEMG FEIEASHHEV APGQHEIDFK
210 220 230 240 250
YANAIRSCDD IQTFKLVVKT IARKHGLHAT FMPKPLYGVN GSGMHCNLSL
260 270 280 290 300
FKNGENVFYD QNGDLQLSDD ARHFIAGILK HAPAFTAVAN PTVNSYKRLV
310 320 330 340 350
PGYEAPCYVA WSAQNRSPLV RIPASRGIST RVEVRSVDPA ANPYLVMATL
360 370 380 390 400
LAAGLDGIKN KLTPPAAVDR NIYVMTKEER EEAGIVDLPA TLAQALVTLQ
410 420 430 440
SNEVISNALG DHLLEHFIEA KEFEWDIFRT QVHQWERDQY MSLY
Length:444
Mass (Da):50,195
Last modified:January 23, 2007 - v3
Checksum:i75A4A2525A445FF7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00513 Genomic DNA. Translation: BAA00403.1.
PIRiJU0075. AJBSQU.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00513 Genomic DNA. Translation: BAA00403.1 .
PIRi JU0075. AJBSQU.

3D structure databases

ProteinModelPortali P19064.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

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. "Nucleotide sequence of the glutamine synthetase gene (glnA) and its upstream region from Bacillus cereus."
    Nakano Y., Kato C., Tanaka E., Kimura K., Horikoshi K.
    J. Biochem. 106:209-215(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-19.
    Strain: IFO 3131.

Entry informationi

Entry nameiGLNA_BACCE
AccessioniPrimary (citable) accession number: P19064
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 79 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3