ID A0A0D6KE22_9CYAN Unreviewed; 471 AA. AC A0A0D6KE22; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 24-JUN-2015, entry version 2. DE RecName: Full=Glutamine synthetase {ECO:0000256|RuleBase:RU004356}; DE EC=6.3.1.2 {ECO:0000256|RuleBase:RU004356}; GN ORFNames=FDUTEX481_05015 {ECO:0000313|EMBL:EKE97637.1}; OS Tolypothrix sp. PCC 7601. OC Bacteria; Cyanobacteria; Nostocales; Microchaetaceae; Tolypothrix. OX NCBI_TaxID=1188 {ECO:0000313|EMBL:EKE97637.1}; RN [1] {ECO:0000313|EMBL:EKE97637.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UTEX B 481 {ECO:0000313|EMBL:EKE97637.1}; RA Weinstock G., Sodergren E., Clifton S., Shukla A., Yerrapragada S., RA Ashki H., Raghuraman S., Kim S., Choi K., Fulton L., Fulton B., RA Wollam A., Wang C., Lobos E., Fronick C., Harrison M., Strong C., RA Farmer C., Lek S., Tomlinson C., Hou S., Chen J., Bhonagiri V., RA Zhang X., Suruliraj S., Pepin K.H., Mitreva M., Warren W., RA Mardis E.R., Wilson R.K., Kehoe D.M.; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + L-glutamate + NH(3) = ADP + phosphate + CC L-glutamine. {ECO:0000256|RuleBase:RU004356}. CC -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two CC hexagons. {ECO:0000256|RuleBase:RU000387}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU000387}. CC -!- SIMILARITY: Belongs to the glutamine synthetase family. CC {ECO:0000256|RuleBase:RU000384}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 Gene3D; 3.10.20.70; -; 1. DR Gene3D; 3.30.590.10; -; 1. DR InterPro; IPR008147; Gln_synt_beta. 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 Pfam; PF00120; Gln-synt_C; 1. DR Pfam; PF03951; Gln-synt_N; 1. DR SUPFAM; SSF54368; SSF54368; 1. DR TIGRFAMs; TIGR00653; GlnA; 1. DR PROSITE; PS00180; GLNA_1; 1. DR PROSITE; PS00182; GLNA_ADENYLATION; 1. DR PROSITE; PS00181; GLNA_ATP; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU004356}; KW Ligase {ECO:0000256|RuleBase:RU004356}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU004356}. 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 //