ID GLNA_SCHPO Reviewed; 359 AA. AC Q09179; O13949; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 24-JAN-2024, entry version 144. DE RecName: Full=Glutamine synthetase; DE Short=GS; DE EC=6.3.1.2; DE AltName: Full=Glutamate--ammonia ligase; GN Name=gln1; ORFNames=SPAC23H4.06; OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; OC Schizosaccharomyces. OX NCBI_TaxID=284812; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=972 / ATCC 24843; RX PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M., RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., RA Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). RN [2] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273; THR-303 AND SER-305, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=18257517; DOI=10.1021/pr7006335; RA Wilson-Grady J.T., Villen J., Gygi S.P.; RT "Phosphoproteome analysis of fission yeast."; RL J. Proteome Res. 7:1088-1097(2008). 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. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. 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; CU329670; CAB11660.1; -; Genomic_DNA. DR PIR; T38322; T38322. DR RefSeq; NP_593400.1; NM_001018832.2. DR AlphaFoldDB; Q09179; -. DR SMR; Q09179; -. DR BioGRID; 278246; 3. DR STRING; 284812.Q09179; -. DR iPTMnet; Q09179; -. DR SwissPalm; Q09179; -. DR MaxQB; Q09179; -. DR PaxDb; 4896-SPAC23H4-06-1; -. DR EnsemblFungi; SPAC23H4.06.1; SPAC23H4.06.1:pep; SPAC23H4.06. DR GeneID; 2541752; -. DR KEGG; spo:SPAC23H4.06; -. DR PomBase; SPAC23H4.06; gln1. DR VEuPathDB; FungiDB:SPAC23H4.06; -. DR eggNOG; KOG0683; Eukaryota. DR HOGENOM; CLU_036762_1_1_1; -. DR InParanoid; Q09179; -. DR OMA; DRRPNAN; -. DR PhylomeDB; Q09179; -. DR Reactome; R-SPO-210455; Astrocytic Glutamate-Glutamine Uptake And Metabolism. DR Reactome; R-SPO-8964539; Glutamate and glutamine metabolism. DR PRO; PR:Q09179; -. DR Proteomes; UP000002485; Chromosome I. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; HDA:PomBase. DR GO; GO:0005634; C:nucleus; HDA:PomBase. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004356; F:glutamine synthetase activity; IDA:PomBase. DR GO; GO:0019676; P:ammonia assimilation cycle; IMP:PomBase. DR GO; GO:0006542; P:glutamine biosynthetic process; IDA:PomBase. DR Gene3D; 3.10.20.70; Glutamine synthetase, N-terminal domain; 1. DR Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1. DR InterPro; IPR008147; Gln_synt_N. DR InterPro; IPR036651; Gln_synt_N_sf. 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 PANTHER; PTHR20852; GLUTAMINE SYNTHETASE; 1. DR PANTHER; PTHR20852:SF57; GLUTAMINE SYNTHETASE 2 CYTOPLASMIC; 1. DR Pfam; PF00120; Gln-synt_C; 1. DR Pfam; PF03951; Gln-synt_N; 1. DR SMART; SM01230; Gln-synt_C; 1. DR SUPFAM; SSF54368; Glutamine synthetase, N-terminal domain; 1. DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 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 1: Evidence at protein level; KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Phosphoprotein; KW Reference proteome. FT CHAIN 1..359 FT /note="Glutamine synthetase" FT /id="PRO_0000153162" FT DOMAIN 28..107 FT /note="GS beta-grasp" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330" FT DOMAIN 114..359 FT /note="GS catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331" FT MOD_RES 273 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18257517" FT MOD_RES 303 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:18257517" FT MOD_RES 305 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18257517" SQ SEQUENCE 359 AA; 40018 MW; 96AACB6A912B3D0E CRC64; MSQYDVEPLL SKAAILNKYA DLPQNGKVMA EYIWIDGFNH LRSKTMTLDA KPSSIDQLRV WNFDGSSTGQ APGNNSDTLL KPVAMYNDPF RRGDNILVLA ACYTADGSPN GFNHRDACAK LLEKHADKET WFGIEQEYTM LDYYDRPFGW PKGGFPGPQG PFYCGVGTGR VFARDIVEAH YKACLYAGIN ISGINAEVMP SQWEYQVGPC AGIEMGDQLW MSRFLLHRIA EDFGVKISFH PKPILGDWNG AGCHTNVSTK DTRAEGGIKA IESYLEKFAK RHKEHIAVYG DDNDLRLTGR HETGSIDKFT YGVADRGASV RIPRSVAMNG CGYFEDRRPA SSIDPYLVTG IITETMFEH //