GLN1B_SALTY
ID GLN1B_SALTY Reviewed; 469 AA.
AC P0A1P6; P06201; Q60007;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Glutamine synthetase {ECO:0000303|PubMed:2879772};
DE Short=GS {ECO:0000303|PubMed:2879772};
DE EC=6.3.1.2 {ECO:0000305|PubMed:7727369};
DE AltName: Full=Glutamate--ammonia ligase {ECO:0000305};
DE AltName: Full=Glutamine synthetase I beta {ECO:0000305};
DE Short=GSI beta {ECO:0000305};
GN Name=glnA {ECO:0000303|PubMed:2879772}; OrderedLocusNames=STM4007;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2879772; DOI=10.1016/0378-1119(86)90415-4;
RA Janson C.A., Kayne P.S., Almassy R.J., Grunstein M., Eisenberg D.;
RT "Sequence of glutamine synthetase from Salmonella typhimurium and
RT implications for the protein structure.";
RL Gene 46:297-300(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 133-469.
RC STRAIN=LT2;
RA Kustu S.G.;
RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) IN COMPLEX WITH MANGANESE ION,
RP COFACTOR, AND SUBUNIT.
RX PubMed=2572586; DOI=10.2210/pdb2gls/pdb;
RA Yamashita M.M., Almassy R.J., Janson C.A., Cascio D., Eisenberg D.;
RT "Refined atomic model of glutamine synthetase at 3.5 A resolution.";
RL J. Biol. Chem. 264:17681-17690(1989).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 2-469 IN COMPLEX WITH L-GLUTAMATE
RP AND 2 MANGANESE IONS, ACTIVITY REGULATION, COFACTOR, AND SUBUNIT.
RX PubMed=8099447; DOI=10.1073/pnas.90.11.4996;
RA Liaw S.H., Pan C., Eisenberg D.;
RT "Feedback inhibition of fully unadenylylated glutamine synthetase from
RT Salmonella typhimurium by glycine, alanine, and serine.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:4996-5000(1993).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) OF 2-469 IN COMPLEX WITH AMP AND 2
RP MANGANESE IONS, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND SUBUNIT.
RX PubMed=7727369; DOI=10.1021/bi00203a014;
RA Liaw S.H., Jun G., Eisenberg D.;
RT "Interactions of nucleotides with fully unadenylylated glutamine synthetase
RT from Salmonella typhimurium.";
RL Biochemistry 33:11184-11188(1994).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 2-469 IN COMPLEX WITH ADP;
RP SUBSTRATE ANALOG AND 2 MANGANESE IONS, ACTIVITY REGULATION, COFACTOR, AND
RP SUBUNIT.
RX PubMed=11329256; DOI=10.1021/bi002438h;
RA Gill H.S., Eisenberg D.;
RT "The crystal structure of phosphinothricin in the active site of glutamine
RT synthetase illuminates the mechanism of enzymatic inhibition.";
RL Biochemistry 40:1903-1912(2001).
CC -!- FUNCTION: Catalyzes the ATP-dependent biosynthesis of glutamine from
CC glutamate and ammonia. {ECO:0000269|PubMed:7727369}.
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:0000305|PubMed:7727369};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:11329256, ECO:0000269|PubMed:2572586,
CC ECO:0000269|PubMed:7727369, ECO:0000269|PubMed:8099447};
CC Note=Binds 2 Mn(2+) ions per subunit. {ECO:0000269|PubMed:11329256,
CC ECO:0000269|PubMed:2572586, ECO:0000269|PubMed:7727369,
CC ECO:0000269|PubMed:8099447};
CC -!- ACTIVITY REGULATION: When cellular nitrogen levels are high, the C-
CC terminal adenylyl transferase (AT) of GlnE inhibits GlnA by covalent
CC transfer of an adenylyl group from ATP to Tyr-398. Conversely, when
CC nitrogen levels are low, the N-terminal adenylyl removase (AR) of GlnE
CC activates GlnA by removing the adenylyl group by phosphorolysis. The
CC fully adenylated enzyme complex is inactive.
CC {ECO:0000250|UniProtKB:Q3V5W6}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.58 mM for ATP {ECO:0000269|PubMed:7727369};
CC -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two hexameric
CC ring. {ECO:0000269|PubMed:11329256, ECO:0000269|PubMed:2572586,
CC ECO:0000269|PubMed:7727369, ECO:0000269|PubMed:8099447}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P9WN39}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR EMBL; M14536; AAA27134.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL22846.1; -; Genomic_DNA.
DR EMBL; X85104; CAA59423.1; -; Genomic_DNA.
DR PIR; A25818; AJEBQT.
DR RefSeq; NP_462887.1; NC_003197.2.
DR RefSeq; WP_001271699.1; NC_003197.2.
DR PDB; 1F1H; X-ray; 2.67 A; A/B/C/D/E/F/G/H/I/J/K/L=2-469.
DR PDB; 1F52; X-ray; 2.49 A; A/B/C/D/E/F/G/H/I/J/K/L=2-469.
DR PDB; 1FPY; X-ray; 2.89 A; A/B/C/D/E/F/G/H/I/J/K/L=2-469.
DR PDB; 1LGR; X-ray; 2.79 A; A/B/C/D/E/F/G/H/I/J/K/L=2-469.
DR PDB; 2GLS; X-ray; 3.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-469.
DR PDB; 2LGS; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L=2-469.
DR PDBsum; 1F1H; -.
DR PDBsum; 1F52; -.
DR PDBsum; 1FPY; -.
DR PDBsum; 1LGR; -.
DR PDBsum; 2GLS; -.
DR PDBsum; 2LGS; -.
DR AlphaFoldDB; P0A1P6; -.
DR SMR; P0A1P6; -.
DR DIP; DIP-61253N; -.
DR STRING; 99287.STM4007; -.
DR BindingDB; P0A1P6; -.
DR ChEMBL; CHEMBL5089; -.
DR DrugBank; DB02663; 2-Amino-4-(Hydroxymethyl-Phosphinyl)Butanoic Acid.
DR PaxDb; P0A1P6; -.
DR PRIDE; P0A1P6; -.
DR EnsemblBacteria; AAL22846; AAL22846; STM4007.
DR GeneID; 1255533; -.
DR KEGG; stm:STM4007; -.
DR PATRIC; fig|99287.12.peg.4223; -.
DR HOGENOM; CLU_017290_1_2_6; -.
DR OMA; PHPHEFE; -.
DR PhylomeDB; P0A1P6; -.
DR BioCyc; SENT99287:STM4007-MON; -.
DR BRENDA; 6.3.1.2; 5542.
DR EvolutionaryTrace; P0A1P6; -.
DR PHI-base; PHI:7742; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004356; F:glutamate-ammonia ligase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006542; P:glutamine biosynthetic process; IBA:GO_Central.
DR GO; GO:0019740; P:nitrogen utilization; IBA:GO_Central.
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; 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 SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF54368; SSF54368; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR TIGRFAMs; TIGR00653; GlnA; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Ligase; Magnesium; Manganese;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..469
FT /note="Glutamine synthetase"
FT /id="PRO_0000153253"
FT DOMAIN 13..97
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 105..469
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT BINDING 130
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11329256,
FT ECO:0000269|PubMed:2572586, ECO:0000269|PubMed:8099447,
FT ECO:0007744|PDB:1F1H, ECO:0007744|PDB:1F52,
FT ECO:0007744|PDB:1FPY, ECO:0007744|PDB:2GLS,
FT ECO:0007744|PDB:2LGS"
FT BINDING 132
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11329256,
FT ECO:0000269|PubMed:7727369, ECO:0000269|PubMed:8099447,
FT ECO:0007744|PDB:1F1H, ECO:0007744|PDB:1F52,
FT ECO:0007744|PDB:1FPY, ECO:0007744|PDB:1LGR,
FT ECO:0007744|PDB:2LGS"
FT BINDING 208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:7727369,
FT ECO:0007744|PDB:1LGR"
FT BINDING 213
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11329256,
FT ECO:0000269|PubMed:7727369, ECO:0000269|PubMed:8099447,
FT ECO:0007744|PDB:1F1H, ECO:0007744|PDB:1F52,
FT ECO:0007744|PDB:1FPY, ECO:0007744|PDB:1LGR,
FT ECO:0007744|PDB:2LGS"
FT BINDING 221
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11329256,
FT ECO:0000269|PubMed:7727369, ECO:0000269|PubMed:8099447,
FT ECO:0007744|PDB:1F1H, ECO:0007744|PDB:1F52,
FT ECO:0007744|PDB:1FPY, ECO:0007744|PDB:1LGR,
FT ECO:0007744|PDB:2LGS"
FT BINDING 265..266
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:7727369,
FT ECO:0000269|PubMed:8099447, ECO:0000305|PubMed:11329256,
FT ECO:0007744|PDB:1F1H, ECO:0007744|PDB:1FPY,
FT ECO:0007744|PDB:1LGR, ECO:0007744|PDB:2LGS"
FT BINDING 266
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 270
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11329256,
FT ECO:0000269|PubMed:2572586, ECO:0000269|PubMed:8099447,
FT ECO:0007744|PDB:1F1H, ECO:0007744|PDB:1F52,
FT ECO:0007744|PDB:1FPY, ECO:0007744|PDB:2GLS,
FT ECO:0007744|PDB:2LGS"
FT BINDING 272..274
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:11329256,
FT ECO:0007744|PDB:1F1H, ECO:0007744|PDB:1F52,
FT ECO:0007744|PDB:1FPY"
FT BINDING 274
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P77961"
FT BINDING 322
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:8099447,
FT ECO:0000305|PubMed:11329256, ECO:0007744|PDB:1FPY,
FT ECO:0007744|PDB:2LGS"
FT BINDING 328
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000305|PubMed:11329256,
FT ECO:0007744|PDB:1FPY"
FT BINDING 340
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 340
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 345
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 353
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P77961"
FT BINDING 358
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11329256,
FT ECO:0000269|PubMed:2572586, ECO:0000269|PubMed:7727369,
FT ECO:0000269|PubMed:8099447, ECO:0007744|PDB:1F1H,
FT ECO:0007744|PDB:1F52, ECO:0007744|PDB:1FPY,
FT ECO:0007744|PDB:1LGR, ECO:0007744|PDB:2GLS,
FT ECO:0007744|PDB:2LGS"
FT BINDING 360
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:8099447,
FT ECO:0007744|PDB:2LGS"
FT MOD_RES 398
FT /note="O-AMP-tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT CONFLICT 223
FT /note="A -> R (in Ref. 3; CAA59423)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="A -> P (in Ref. 1; AAA27134 and 3; CAA59423)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="R -> P (in Ref. 1; AAA27134)"
FT /evidence="ECO:0000305"
FT HELIX 3..12
FT /evidence="ECO:0007829|PDB:1F52"
FT STRAND 17..23
FT /evidence="ECO:0007829|PDB:1F52"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:1FPY"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:1F52"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:1F52"
FT HELIX 41..46
FT /evidence="ECO:0007829|PDB:1F52"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:1F52"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:1F52"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:1F1H"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:1FPY"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:1F52"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:1F52"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:2GLS"
FT STRAND 85..93
FT /evidence="ECO:0007829|PDB:1F52"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:1F52"
FT HELIX 105..118
FT /evidence="ECO:0007829|PDB:1F52"
FT STRAND 123..144
FT /evidence="ECO:0007829|PDB:1F52"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:1F52"
FT HELIX 158..162
FT /evidence="ECO:0007829|PDB:1F52"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:1FPY"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:1F52"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:1LGR"
FT HELIX 190..202
FT /evidence="ECO:0007829|PDB:1F52"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:1F52"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:1F52"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:1F52"
FT HELIX 229..249
FT /evidence="ECO:0007829|PDB:1F52"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:1F52"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:1FPY"
FT STRAND 269..277
FT /evidence="ECO:0007829|PDB:1F52"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:1F1H"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:1F52"
FT HELIX 293..304
FT /evidence="ECO:0007829|PDB:1F52"
FT HELIX 306..313
FT /evidence="ECO:0007829|PDB:1F52"
FT HELIX 317..321
FT /evidence="ECO:0007829|PDB:1F52"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:1F52"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:1F1H"
FT STRAND 332..338
FT /evidence="ECO:0007829|PDB:1F52"
FT STRAND 342..345
FT /evidence="ECO:0007829|PDB:1F52"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:1F52"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:1F52"
FT HELIX 368..384
FT /evidence="ECO:0007829|PDB:1F52"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:1F52"
FT TURN 403..407
FT /evidence="ECO:0007829|PDB:2GLS"
FT HELIX 415..424
FT /evidence="ECO:0007829|PDB:1F52"
FT HELIX 427..430
FT /evidence="ECO:0007829|PDB:1F52"
FT HELIX 431..433
FT /evidence="ECO:0007829|PDB:1F52"
FT HELIX 437..456
FT /evidence="ECO:0007829|PDB:1F52"
FT HELIX 460..466
FT /evidence="ECO:0007829|PDB:1F52"
SQ SEQUENCE 469 AA; 51786 MW; CD4303E758871E10 CRC64;
MSAEHVLTML NEHEVKFVDL RFTDTKGKEQ HVTIPAHQVN AEFFEEGKMF DGSSIGGWKG
INESDMVLMP DASTAVIDPF FADSTLIIRC DILEPGTLQG YDRDPRSIAK RAEDYLRATG
IADTVLFGPE PEFFLFDDIR FGASISGSHV AIDDIEGAWN SSTKYEGGNK GHRPGVKGGY
FPVPPVDSAQ DIRSEMCLVM EQMGLVVEAH HHEVATAGQN EVATRFNTMT KKADEIQIYK
YVVHNVAHRF GKTATFMPKP MFGDNGSGMH CHMSLAKNGT NLFSGDKYAG LSEQALYYIG
GVIKHAKAIN ALANPTTNSY KRLVPGYEAP VMLAYSARNR SASIRIPVVA SPKARRIEVR
FPDPAANPYL CFAALLMAGL DGIKNKIHPG EAMDKNLYDL PPEEAKEIPQ VAGSLEEALN
ALDLDREFLK AGGVFTDEAI DAYIALRREE DDRVRMTPHP VEFELYYSV
