ID A0A0D6KE22_9CYAN Unreviewed; 471 AA. AC A0A0D6KE22; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 29-MAY-2024, entry version 35. DE RecName: Full=Glutamine synthetase {ECO:0000256|ARBA:ARBA00021364, ECO:0000256|RuleBase:RU004356}; DE EC=6.3.1.2 {ECO:0000256|ARBA:ARBA00012937, ECO:0000256|RuleBase:RU004356}; GN ORFNames=FDUTEX481_05015 {ECO:0000313|EMBL:EKE97637.1}; OS Tolypothrix sp. PCC 7601. OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae; OC Tolypothrix. OX NCBI_TaxID=1188 {ECO:0000313|EMBL:EKE97637.1, ECO:0000313|Proteomes:UP000032761}; RN [1] {ECO:0000313|EMBL:EKE97637.1, ECO:0000313|Proteomes:UP000032761} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7601 / UTEX B 481 {ECO:0000313|Proteomes:UP000032761}; RX PubMed=25953173; RA Yerrapragada S., Shukla A., Hallsworth-Pepin K., Choi K., Wollam A., RA Clifton S., Qin X., Muzny D., Raghuraman S., Ashki H., Uzman A., RA Highlander S.K., Fryszczyn B.G., Fox G.E., Tirumalai M.R., Liu Y., Kim S., RA Kehoe D.M., Weinstock G.M.; RT "Extreme Sensory Complexity Encoded in the 10-Megabase Draft Genome RT Sequence of the Chromatically Acclimating Cyanobacterium Tolypothrix sp. RT PCC 7601."; RL Genome Announc. 3:0-0(2015). 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 Evidence={ECO:0000256|RuleBase:RU004356}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two hexagons. CC {ECO:0000256|ARBA:ARBA00011354, ECO:0000256|RuleBase:RU000387}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|RuleBase:RU000387}. CC -!- SIMILARITY: Belongs to the glutamine synthetase family. CC {ECO:0000256|ARBA:ARBA00009897, ECO:0000256|PROSITE-ProRule:PRU01330, CC ECO:0000256|RuleBase:RU000384}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EKE97637.1}. 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; AGCR01000113; EKE97637.1; -; Genomic_DNA. DR RefSeq; WP_045874111.1; NZ_JH930373.1. DR AlphaFoldDB; A0A0D6KE22; -. DR SMR; A0A0D6KE22; -. DR STRING; 1188.FDUTEX481_05015; -. DR PATRIC; fig|1188.3.peg.8994; -. DR HOGENOM; CLU_017290_1_2_3; -. DR OrthoDB; 9807095at2; -. DR Proteomes; UP000032761; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004356; F:glutamine synthetase activity; IEA:UniProtKB-EC. DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro. DR GO; GO:0019740; P:nitrogen utilization; IEA:TreeGrafter. 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; IPR004809; Gln_synth_I. DR InterPro; IPR001637; Gln_synth_I_adenylation_site. DR InterPro; IPR027302; Gln_synth_N_conserv_site. DR NCBIfam; TIGR00653; GlnA; 1. DR PANTHER; PTHR43407; GLUTAMINE SYNTHETASE; 1. DR PANTHER; PTHR43407:SF1; LENGSIN; 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; PS00182; GLNA_ADENYLATION; 1. DR PROSITE; PS00181; GLNA_ATP; 1. DR PROSITE; PS51986; GS_BETA_GRASP; 1. DR PROSITE; PS51987; GS_CATALYTIC; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|PIRSR:PIRSR604809-2, KW ECO:0000256|RuleBase:RU004356}; Cytoplasm {ECO:0000256|RuleBase:RU000387}; KW Ligase {ECO:0000256|RuleBase:RU004356}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR604809-2, KW ECO:0000256|RuleBase:RU004356}; KW Phosphoprotein {ECO:0000256|PIRSR:PIRSR604809-50}. FT DOMAIN 14..99 FT /note="GS beta-grasp" FT /evidence="ECO:0000259|PROSITE:PS51986" FT DOMAIN 106..471 FT /note="GS catalytic" FT /evidence="ECO:0000259|PROSITE:PS51987" FT BINDING 208 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2" FT BINDING 224..226 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2" FT BINDING 265..266 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1" FT BINDING 272..274 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2" FT BINDING 322 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1" FT BINDING 328 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1" FT BINDING 340 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2" FT BINDING 340 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1" FT BINDING 354 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2" FT BINDING 361 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1" FT MOD_RES 399 FT /note="O-AMP-tyrosine" FT /evidence="ECO:0000256|PIRSR:PIRSR604809-50" SQ SEQUENCE 471 AA; 53050 MW; 4216D115B6EC7310 CRC64; MTTPQEVLKL IQDQKIQMID LKFIDTPGTW QHLTVYYNQI DESSFTDGVP FDGSSIRGWK GIEESDMTMV LDPNTAWIDP FMKEPTLSII CSIKEPRTGE WYNRCPRVIA QKAIDYLVST GLGDTAFFGP EAEFFIFDDA RFDQTANSGY YYVDSVEGRW NSGKDEGPNL AYKPRFKEGY FPVAPTDTFQ DMRTEMLLTM AACGVPIEKQ HHEVATGGQC ELGFRFGKLI EAADWLMTYK YVIKNVAKKY GRTVTFMPKP IFGDNGSGMH CHQSIWKDGK PLFGGDKYAG LSDMALYYIG GILKHAPALL GITNPTTNSY KRLVPGYEAP VNLAYSQGNR SASVRIPLSG TNPKAKRLEF RCPDATSNPY LAFAAMLCAG IDGIKNKIHP GEPLDRNIYE LSPEELAKVP STPGSLELAL EALENDHAFL TESGVFTEDF IQNWIEYKLV NEVKQLQLRP HPYEFYLYYD C //