ID A0A096ELL8_9BURK Unreviewed; 471 AA. AC A0A096ELL8; A0A176TQW3; D0J2P4; D8D3L3; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 24-JAN-2024, entry version 44. DE RecName: Full=Glutamine synthetase {ECO:0000256|RuleBase:RU004356}; DE EC=6.3.1.2 {ECO:0000256|RuleBase:RU004356}; GN Name=glnA {ECO:0000313|EMBL:KGG94405.1}; GN ORFNames=N5D63_22585 {ECO:0000313|EMBL:MDH1336939.1}, P245_07500 GN {ECO:0000313|EMBL:KGG94405.1}, P608_04680 GN {ECO:0000313|EMBL:KGH18454.1}; OS Comamonas thiooxydans. OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Comamonas. OX NCBI_TaxID=363952 {ECO:0000313|EMBL:KGG94405.1, ECO:0000313|Proteomes:UP000029567}; RN [1] {ECO:0000313|Proteomes:UP000029549, ECO:0000313|Proteomes:UP000029567} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DF2 {ECO:0000313|EMBL:KGH18454.1, RC ECO:0000313|Proteomes:UP000029549}, and JL14 RC {ECO:0000313|EMBL:KGG94405.1, ECO:0000313|Proteomes:UP000029567}; RA Liu L., Zhu W., Xia X., Xu B., Luo M., Wang G.; RT "High correlation between genotypes and phenotypes of environmental RT bacteria Comamonas testosteroni strains."; RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:MDH1336939.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=GD03832 {ECO:0000313|EMBL:MDH1336939.1}; RA Diorio-Toth L.; RT "Intensive care unit water sources are persistently colonized with multi- RT drug resistant bacteria and are the site of extensive horizontal gene RT transfer of antibiotic resistance genes."; RL Submitted (SEP-2022) to the EMBL/GenBank/DDBJ databases. 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 -!- 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:KGG94405.1}. 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; AWTN01000071; KGG94405.1; -; Genomic_DNA. DR EMBL; AWTP01000046; KGH18454.1; -; Genomic_DNA. DR EMBL; JAOCEK010000028; MDH1336939.1; -; Genomic_DNA. DR RefSeq; WP_003063782.1; NZ_VTRK01000005.1. DR GeneID; 69561060; -. DR PATRIC; fig|285.48.peg.3312; -. DR OrthoDB; 9807095at2; -. DR Proteomes; UP000029549; Unassembled WGS sequence. DR Proteomes; UP000029567; Unassembled WGS sequence. DR Proteomes; UP001161065; Unassembled WGS sequence. 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 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; IPR027302; Gln_synth_N_conserv_site. DR NCBIfam; TIGR00653; GlnA; 1. DR PANTHER; PTHR43407; GLUTAMINE SYNTHETASE; 1. DR PANTHER; PTHR43407:SF2; GLUTAMINE SYNTHETASE; 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 3: Inferred from homology; KW ATP-binding {ECO:0000256|PIRSR:PIRSR604809-2, KW ECO:0000256|RuleBase:RU004356}; KW Ligase {ECO:0000256|RuleBase:RU004356, ECO:0000313|EMBL:KGG94405.1}; KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR604809-2, KW ECO:0000256|RuleBase:RU004356}; KW Phosphoprotein {ECO:0000256|PIRSR:PIRSR604809-50}. FT DOMAIN 15..100 FT /note="GS beta-grasp" FT /evidence="ECO:0000259|PROSITE:PS51986" FT DOMAIN 107..471 FT /note="GS catalytic" FT /evidence="ECO:0000259|PROSITE:PS51987" FT BINDING 210 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2" FT BINDING 267..268 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1" FT BINDING 274..276 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2" FT BINDING 324 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1" FT BINDING 330 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1" FT BINDING 342 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2" FT BINDING 342 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1" FT BINDING 355 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2" FT BINDING 362 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1" FT MOD_RES 400 FT /note="O-AMP-tyrosine" FT /evidence="ECO:0000256|PIRSR:PIRSR604809-50" SQ SEQUENCE 471 AA; 52311 MW; 573476E30E2C068D CRC64; MAKTVADVMQ MVQDNEVKFV DLRFTDTRGK EQHVTVPVSH FDEDKFASGH AFDGSSVAGW KGIEASDMQL VPDPNTANID PFFEETTLIL QCDVIEPGDG KAYDRDPRSI AKRAEAYLKA SGLGDTAYFG PEPEFFIFDG VRWGTEPHNP FFEIEEYEAP WNTGTKFETG NRGHRPRVKG GYFPVPPVDS TQDMRAEMSL LLEAVGIPVE VFHHEVAGAG QNEIGTRFST LVERADWTQL QKYIIWNVAN TYGKTATFMP KPYAGDNGSG MHVHQSVWKD GKNLFAGDGY AGLSDFALYY IGGIIKHARA LNAITNPGTN SYKRLVPGFE APVKLAYSAK NRSASIRIPY VSNPKARRVE ARFPDPLMNP YLGFAALLMA GLDGVENKIH PGEAATKDLY HLPPEEDKLV PTVCHSLDQA LEALDADRAF LTKGGVFSDS MLDAYIELKM GEVTRYRQSV HPVEYDMYFS L //