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P15106

- GLNA_STRCO

UniProt

P15106 - GLNA_STRCO

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Protein

Glutamine synthetase

Gene

glnA

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript 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: CACAO

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:SCO2198
ORF Names:SC3H12.06
OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Taxonomic identifieri100226 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
ProteomesiUP000001973: Chromosome

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
Chaini1 – 469469Glutamine synthetasePRO_0000153266Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei397 – 3971O-AMP-tyrosineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP15106.

PTM databases

PhosSiteiP12011306.

Expressioni

Inductioni

Regulated in response to the available nitrogen source.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi100226.SCO2198.

Structurei

3D structure databases

ProteinModelPortaliP15106.
SMRiP15106. Positions 3-469.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glutamine synthetase family.Curated

Phylogenomic databases

eggNOGiCOG0174.
HOGENOMiHOG000005157.
InParanoidiP15106.
KOiK01915.
OMAiDMLLMPI.
OrthoDBiEOG6B360N.
PhylomeDBiP15106.

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.

P15106-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFQNADDVKK FIADEDVKFV DVRFCDLPGV MQHFTLPATA FDPDAEQAFD
60 70 80 90 100
GSSIRGFQAI HESDMSLRPD LSTARVDPFR RDKTLNINFF IHDPITGEQY
110 120 130 140 150
SRDPRNVAKK AEAYLASTGI ADTAFFGPEA EFYVFDSVRF ATRENESFYH
160 170 180 190 200
IDSEAGAWNT GALEDNRGYK VRYKGGYFPV PPVDHFADLR AEISLELERS
210 220 230 240 250
GLQVERQHHE VGTAGQAEIN YKFNTLLAAA DDLQLFKYIV KNVAWKNGKT
260 270 280 290 300
ATFMPKPIFG DNGSGMHVHQ SLWSGGEPLF YDEQGYAGLS DTARYYIGGI
310 320 330 340 350
LKHAPSLLAF TNPTVNSYHR LVPGFEAPVN LVYSQRNRSA AMRIPITGSN
360 370 380 390 400
PKAKRVEFRA PDASGNPYLA FSALLLAGLD GIKNKIEPAE PIDKDLYELA
410 420 430 440 450
PEEHANVAQV PTSLGAVLDR LEADHEFLLQ GDVFTPDLIE TWIDFKRANE
460
IAPLQLRPHP HEFEMYFDV
Length:469
Mass (Da):52,568
Last modified:April 1, 1990 - v1
Checksum:i7C141D49C70FC437
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23172 Genomic DNA. Translation: AAA72717.1.
AL939111 Genomic DNA. Translation: CAB90845.1.
PIRiJT0389. AJSMQC.
RefSeqiNP_626450.1. NC_003888.3.

Genome annotation databases

EnsemblBacteriaiCAB90845; CAB90845; CAB90845.
GeneIDi1097631.
KEGGisco:SCO2198.
PATRICi23734052. VBIStrCoe124346_2235.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23172 Genomic DNA. Translation: AAA72717.1 .
AL939111 Genomic DNA. Translation: CAB90845.1 .
PIRi JT0389. AJSMQC.
RefSeqi NP_626450.1. NC_003888.3.

3D structure databases

ProteinModelPortali P15106.
SMRi P15106. Positions 3-469.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 100226.SCO2198.

PTM databases

PhosSitei P12011306.

Proteomic databases

PRIDEi P15106.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB90845 ; CAB90845 ; CAB90845 .
GeneIDi 1097631.
KEGGi sco:SCO2198.
PATRICi 23734052. VBIStrCoe124346_2235.

Phylogenomic databases

eggNOGi COG0174.
HOGENOMi HOG000005157.
InParanoidi P15106.
KOi K01915.
OMAi DMLLMPI.
OrthoDBi EOG6B360N.
PhylomeDBi P15106.

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

« Hide 'large scale' publications
  1. "Cloning and nucleotide sequence of the Streptomyces coelicolor gene encoding glutamine synthetase."
    Wray L.V. Jr., Fisher S.H.
    Gene 71:247-256(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-471 / A3(2) / M145.

Entry informationi

Entry nameiGLNA_STRCO
AccessioniPrimary (citable) accession number: P15106
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: October 29, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3