GLNA1_DROME
ID GLNA1_DROME Reviewed; 399 AA.
AC P20477; A4UZX3; O96770; Q9VPK0;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Glutamine synthetase 1, mitochondrial;
DE EC=6.3.1.2;
DE AltName: Full=Glutamate--ammonia ligase 1;
DE Flags: Precursor;
GN Name=Gs1; ORFNames=CG2718;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1969491; DOI=10.1016/0022-2836(90)90301-2;
RA Caizzi R., Bozzetti M.P., Caggese C., Ritossa F.;
RT "Homologous nuclear genes encode cytoplasmic and mitochondrial glutamine
RT synthetase in Drosophila melanogaster.";
RL J. Mol. Biol. 212:17-26(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Glover D.M.;
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine +
CC phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2;
CC -!- SUBUNIT: Homooctamer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X52760; CAA36971.1; -; mRNA.
DR EMBL; AJ012460; CAA10031.1; -; mRNA.
DR EMBL; AE014134; AAF51546.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF51547.1; -; Genomic_DNA.
DR EMBL; AY058730; AAL13959.1; -; mRNA.
DR PIR; S09109; AJFF1M.
DR RefSeq; NP_001162839.1; NM_001169368.3.
DR RefSeq; NP_476570.1; NM_057222.4.
DR RefSeq; NP_722606.1; NM_164367.2.
DR AlphaFoldDB; P20477; -.
DR SMR; P20477; -.
DR BioGRID; 59433; 21.
DR STRING; 7227.FBpp0077773; -.
DR PaxDb; P20477; -.
DR PRIDE; P20477; -.
DR DNASU; 33172; -.
DR EnsemblMetazoa; FBtr0078114; FBpp0077773; FBgn0001142.
DR EnsemblMetazoa; FBtr0078115; FBpp0077774; FBgn0001142.
DR EnsemblMetazoa; FBtr0300568; FBpp0289795; FBgn0001142.
DR GeneID; 33172; -.
DR KEGG; dme:Dmel_CG2718; -.
DR CTD; 33172; -.
DR FlyBase; FBgn0001142; Gs1.
DR VEuPathDB; VectorBase:FBgn0001142; -.
DR eggNOG; KOG0683; Eukaryota.
DR HOGENOM; CLU_036762_1_1_1; -.
DR InParanoid; P20477; -.
DR OMA; HAVACLY; -.
DR OrthoDB; 784869at2759; -.
DR PhylomeDB; P20477; -.
DR Reactome; R-DME-210455; Astrocytic Glutamate-Glutamine Uptake And Metabolism.
DR Reactome; R-DME-8964539; Glutamate and glutamine metabolism.
DR BioGRID-ORCS; 33172; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 33172; -.
DR PRO; PR:P20477; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0001142; Expressed in embryonic/larval hemocyte (Drosophila) and 42 other tissues.
DR ExpressionAtlas; P20477; baseline and differential.
DR Genevisible; P20477; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004356; F:glutamate-ammonia ligase activity; IDA:FlyBase.
DR GO; GO:0006542; P:glutamine biosynthetic process; IBA:GO_Central.
DR GO; GO:1901704; P:L-glutamine biosynthetic process; IMP:FlyBase.
DR GO; GO:0006909; P:phagocytosis; IMP:FlyBase.
DR GO; GO:0010636; P:positive regulation of mitochondrial fusion; IMP:FlyBase.
DR Gene3D; 3.10.20.70; -; 1.
DR InterPro; IPR008147; Gln_synt_b-grasp.
DR InterPro; IPR036651; Gln_synt_N.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR008146; Gln_synth_cat_dom.
DR InterPro; IPR027303; Gln_synth_gly_rich_site.
DR InterPro; IPR027302; Gln_synth_N_conserv_site.
DR Pfam; PF00120; Gln-synt_C; 1.
DR Pfam; PF03951; Gln-synt_N; 1.
DR SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF54368; SSF54368; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR PROSITE; PS00180; GLNA_1; 1.
DR PROSITE; PS00181; GLNA_ATP; 1.
DR PROSITE; PS51986; GS_BETA_GRASP; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Ligase; Mitochondrion; Nucleotide-binding; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 28..399
FT /note="Glutamine synthetase 1, mitochondrial"
FT /id="PRO_0000011173"
FT DOMAIN 62..143
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 150..399
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT CONFLICT 2
FT /note="A -> R (in Ref. 2; CAA10031)"
FT /evidence="ECO:0000305"
FT CONFLICT 178..183
FT /note="DVDGRP -> RRGRTS (in Ref. 1; CAA36971)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="A -> R (in Ref. 1; CAA36971)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="A -> P (in Ref. 1; CAA36971)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="D -> Y (in Ref. 1; CAA36971)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="R -> Q (in Ref. 1; CAA36971)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 399 AA; 44396 MW; 935E8D1D9927ACCC CRC64;
MALRVAGLFL KKELVAPATQ QLRLLRTGNT TRSQFLANSP NTALDKSILQ RYRNLETPAN
RVQATYLWID GTGENIRLKD RVLDKVPSSV EDLPDWQYDG SSTYQAHGEN SDTTLKPRAI
YRDPFKPGKN DVIVLCDTYS ADGKPTASNK RAAFQAAIDL ISDQEPWFGI EQEYTLLDVD
GRPFGWPENG FPAPQGPYYC GVGADRVYAR DLVEAHVVAC LYAGIDFAGT NAEVMPAQWE
FQIGPAGIKA CDDLWVSRYI LQRIAEEYGV VVTFDPKPME GQWNGAGAHT NFSTKEMRAD
GGIKAIEEAI EKLSKRHERH IKAYDPKEGK DNERRLVGRL ETSSIDKFSW GVANRAVSVR
VPRGVATAGK GYLEDRRPSS NCDPYAVCNA IVRTCLLNE
