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Protein

Glutamine synthetase 1, mitochondrial

Gene

Gs1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. glutamate-ammonia ligase activity Source: FlyBase

GO - Biological processi

  1. glutamine biosynthetic process Source: InterPro
  2. glutamine metabolic process Source: FlyBase
  3. mitochondrion organization Source: FlyBase
  4. phagocytosis Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_202933. Astrocytic Glutamate-Glutamine Uptake And Metabolism.
REACT_216833. Amino acid synthesis and interconversion (transamination).

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamine synthetase 1, mitochondrial (EC:6.3.1.2)
Alternative name(s):
Glutamate--ammonia ligase 1
Gene namesi
Name:Gs1
ORF Names:CG2718
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0001142. Gs1.

Subcellular locationi

GO - Cellular componenti

  1. lipid particle Source: FlyBase
  2. mitochondrion Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2727MitochondrionSequence AnalysisAdd
BLAST
Chaini28 – 399372Glutamine synthetase 1, mitochondrialPRO_0000011173Add
BLAST

Proteomic databases

PaxDbiP20477.

Expressioni

Gene expression databases

BgeeiP20477.
ExpressionAtlasiP20477. differential.

Interactioni

Subunit structurei

Homooctamer.

Protein-protein interaction databases

BioGridi59433. 20 interactions.
MINTiMINT-297766.

Structurei

3D structure databases

ProteinModelPortaliP20477.
SMRiP20477. Positions 45-399.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glutamine synthetase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0174.
GeneTreeiENSGT00390000010047.
HOGENOMiHOG000246596.
InParanoidiP20477.
KOiK01915.
OMAiKSFGRDV.
OrthoDBiEOG7CZK5G.
PhylomeDBiP20477.

Family and domain databases

Gene3Di3.30.590.10. 1 hit.
InterProiIPR008147. Gln_synt_beta.
IPR014746. Gln_synth/guanido_kin_cat_dom.
IPR008146. Gln_synth_cat_dom.
IPR027303. Gln_synth_gly_rich_site.
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.
PROSITEiPS00180. GLNA_1. 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.

P20477-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALRVAGLFL KKELVAPATQ QLRLLRTGNT TRSQFLANSP NTALDKSILQ
60 70 80 90 100
RYRNLETPAN RVQATYLWID GTGENIRLKD RVLDKVPSSV EDLPDWQYDG
110 120 130 140 150
SSTYQAHGEN SDTTLKPRAI YRDPFKPGKN DVIVLCDTYS ADGKPTASNK
160 170 180 190 200
RAAFQAAIDL ISDQEPWFGI EQEYTLLDVD GRPFGWPENG FPAPQGPYYC
210 220 230 240 250
GVGADRVYAR DLVEAHVVAC LYAGIDFAGT NAEVMPAQWE FQIGPAGIKA
260 270 280 290 300
CDDLWVSRYI LQRIAEEYGV VVTFDPKPME GQWNGAGAHT NFSTKEMRAD
310 320 330 340 350
GGIKAIEEAI EKLSKRHERH IKAYDPKEGK DNERRLVGRL ETSSIDKFSW
360 370 380 390
GVANRAVSVR VPRGVATAGK GYLEDRRPSS NCDPYAVCNA IVRTCLLNE
Length:399
Mass (Da):44,396
Last modified:June 21, 2005 - v3
Checksum:i935E8D1D9927ACCC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21A → R in CAA10031 (Ref. 2) Curated
Sequence conflicti178 – 1836DVDGRP → RRGRTS in CAA36971 (PubMed:1969491).Curated
Sequence conflicti288 – 2881A → R in CAA36971 (PubMed:1969491).Curated
Sequence conflicti309 – 3091A → P in CAA36971 (PubMed:1969491).Curated
Sequence conflicti325 – 3251D → Y in CAA36971 (PubMed:1969491).Curated
Sequence conflicti393 – 3931R → Q in CAA36971 (PubMed:1969491).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52760 mRNA. Translation: CAA36971.1.
AJ012460 mRNA. Translation: CAA10031.1.
AE014134 Genomic DNA. Translation: AAF51546.1.
AE014134 Genomic DNA. Translation: AAF51547.1.
AY058730 mRNA. Translation: AAL13959.1.
PIRiS09109. AJFF1M.
RefSeqiNP_001162839.1. NM_001169368.3.
NP_476570.1. NM_057222.4.
NP_722606.1. NM_164367.2.
UniGeneiDm.6999.

Genome annotation databases

EnsemblMetazoaiFBtr0078114; FBpp0077773; FBgn0001142.
FBtr0078115; FBpp0077774; FBgn0001142.
FBtr0300568; FBpp0289795; FBgn0001142.
GeneIDi33172.
KEGGidme:Dmel_CG2718.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52760 mRNA. Translation: CAA36971.1.
AJ012460 mRNA. Translation: CAA10031.1.
AE014134 Genomic DNA. Translation: AAF51546.1.
AE014134 Genomic DNA. Translation: AAF51547.1.
AY058730 mRNA. Translation: AAL13959.1.
PIRiS09109. AJFF1M.
RefSeqiNP_001162839.1. NM_001169368.3.
NP_476570.1. NM_057222.4.
NP_722606.1. NM_164367.2.
UniGeneiDm.6999.

3D structure databases

ProteinModelPortaliP20477.
SMRiP20477. Positions 45-399.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi59433. 20 interactions.
MINTiMINT-297766.

Proteomic databases

PaxDbiP20477.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0078114; FBpp0077773; FBgn0001142.
FBtr0078115; FBpp0077774; FBgn0001142.
FBtr0300568; FBpp0289795; FBgn0001142.
GeneIDi33172.
KEGGidme:Dmel_CG2718.

Organism-specific databases

CTDi33172.
FlyBaseiFBgn0001142. Gs1.

Phylogenomic databases

eggNOGiCOG0174.
GeneTreeiENSGT00390000010047.
HOGENOMiHOG000246596.
InParanoidiP20477.
KOiK01915.
OMAiKSFGRDV.
OrthoDBiEOG7CZK5G.
PhylomeDBiP20477.

Enzyme and pathway databases

ReactomeiREACT_202933. Astrocytic Glutamate-Glutamine Uptake And Metabolism.
REACT_216833. Amino acid synthesis and interconversion (transamination).

Miscellaneous databases

GenomeRNAii33172.
NextBioi782262.

Gene expression databases

BgeeiP20477.
ExpressionAtlasiP20477. differential.

Family and domain databases

Gene3Di3.30.590.10. 1 hit.
InterProiIPR008147. Gln_synt_beta.
IPR014746. Gln_synth/guanido_kin_cat_dom.
IPR008146. Gln_synth_cat_dom.
IPR027303. Gln_synth_gly_rich_site.
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.
PROSITEiPS00180. GLNA_1. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Homologous nuclear genes encode cytoplasmic and mitochondrial glutamine synthetase in Drosophila melanogaster."
    Caizzi R., Bozzetti M.P., Caggese C., Ritossa F.
    J. Mol. Biol. 212:17-26(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Glover D.M.
    Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.

Entry informationi

Entry nameiGLNA1_DROME
AccessioniPrimary (citable) accession number: P20477
Secondary accession number(s): A4UZX3, O96770, Q9VPK0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: June 21, 2005
Last modified: January 7, 2015
This is version 113 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. 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.