GLN1B_SYNY3
ID GLN1B_SYNY3 Reviewed; 473 AA.
AC P77961; Q59981;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Glutamine synthetase {ECO:0000303|PubMed:1973929};
DE Short=GS {ECO:0000303|PubMed:1973929};
DE EC=6.3.1.2 {ECO:0000305|PubMed:1973929};
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:1973929}; OrderedLocusNames=slr1756;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=7727755; DOI=10.1007/bf00020231;
RA Reyes J.C., Florencio F.J.;
RT "Electron transport controls transcription of the glutamine synthetase gene
RT (glnA) from the cyanobacterium Synechocystis sp. PCC 6803.";
RL Plant Mol. Biol. 27:789-799(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=1973929; DOI=10.1128/jb.172.8.4732-4735.1990;
RA Merida A., Leurentop L., Candau P., Florencio F.J.;
RT "Purification and properties of glutamine synthetases from the
RT cyanobacteria Synechocystis sp. strain PCC 6803 and Calothrix sp. strain
RT PCC 7601.";
RL J. Bacteriol. 172:4732-4735(1990).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8002575; DOI=10.1128/jb.176.24.7516-7523.1994;
RA Reyes J.C., Florencio F.J.;
RT "A mutant lacking the glutamine synthetase gene (glnA) is impaired in the
RT regulation of the nitrate assimilation system in the cyanobacterium
RT Synechocystis sp. strain PCC 6803.";
RL J. Bacteriol. 176:7516-7523(1994).
RN [5]
RP INDUCTION.
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=9098067; DOI=10.1128/jb.179.8.2678-2689.1997;
RA Reyes J.C., Muro-Pastor M.I., Florencio F.J.;
RT "Transcription of glutamine synthetase genes (glnA and glnN) from the
RT cyanobacterium Synechocystis sp. strain PCC 6803 is differently regulated
RT in response to nitrogen availability.";
RL J. Bacteriol. 179:2678-2689(1997).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH ATP ANALOG AND 2
RP MANGANESE IONS, AND COFACTOR.
RA Saelices L., Cascio D., Florencio F.J., Muro-Pastor M.I.;
RT "Crystal structure of glutamine synthetase from Synechocystis sp. PCC
RT 6803.";
RL Submitted (JUN-2010) to the PDB data bank.
CC -!- FUNCTION: Involved in nitrogen metabolism via ammonium assimilation
CC (PubMed:8002575). Catalyzes the ATP-dependent biosynthesis of glutamine
CC from glutamate and ammonia (PubMed:1973929, PubMed:8002575).
CC {ECO:0000269|PubMed:1973929, ECO:0000269|PubMed:8002575}.
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:1973929};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:1973929, ECO:0000269|Ref.6};
CC Note=Binds 2 Mg(2+) ions per subunit (Ref.6). Also able to bind Co(2+),
CC Mn(2+) and Ca(2+) ion (PubMed:1973929). {ECO:0000269|PubMed:1973929,
CC ECO:0000269|Ref.6};
CC -!- ACTIVITY REGULATION: Inhibited by ADP (90%), AMP (80%), alanine (52%)
CC and aspartate (41%) (PubMed:1973929). The activity of this enzyme could
CC be controlled by adenylation under conditions of abundant glutamine (By
CC similarity). {ECO:0000250|UniProtKB:Q3V5W6,
CC ECO:0000269|PubMed:1973929}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.17 mM for ammonium {ECO:0000269|PubMed:1973929};
CC KM=0.55 mM for ATP {ECO:0000269|PubMed:1973929};
CC KM=1.2 mM for L-glutamate {ECO:0000269|PubMed:1973929};
CC KM=14.3 mM for L-glutamine {ECO:0000269|PubMed:1973929};
CC KM=14.5 mM for hydroxylamine {ECO:0000269|PubMed:1973929};
CC pH dependence:
CC Optimum pH is 7.2. {ECO:0000269|PubMed:1973929};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius.
CC {ECO:0000269|PubMed:1973929};
CC -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two hexagons.
CC {ECO:0000269|PubMed:1973929}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P9WN39}.
CC -!- INDUCTION: Highly expressed in nitrate- or ammonium-grown cells and
CC exhibits two- to fourfold-higher expression in nitrogen-starved cells.
CC {ECO:0000269|PubMed:9098067}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are able to grow with
CC nitrate as the sole nitrogen source, but it are unable to grow in
CC ammonium-containing medium. This mutant is impaired in the regulation
CC of the nitrate assimilation system. {ECO:0000269|PubMed:8002575}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR EMBL; X69199; CAA49139.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA17055.1; -; Genomic_DNA.
DR PIR; S75141; S75141.
DR PDB; 3NG0; X-ray; 2.80 A; A=1-473.
DR PDBsum; 3NG0; -.
DR AlphaFoldDB; P77961; -.
DR SMR; P77961; -.
DR DIP; DIP-48822N; -.
DR IntAct; P77961; 5.
DR STRING; 1148.1652131; -.
DR PaxDb; P77961; -.
DR EnsemblBacteria; BAA17055; BAA17055; BAA17055.
DR KEGG; syn:slr1756; -.
DR eggNOG; COG0174; Bacteria.
DR InParanoid; P77961; -.
DR PhylomeDB; P77961; -.
DR BRENDA; 6.3.1.2; 382.
DR Proteomes; UP000001425; 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; 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; 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..473
FT /note="Glutamine synthetase"
FT /id="PRO_0000153272"
FT DOMAIN 15..100
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 107..473
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT BINDING 132
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000305|Ref.6, ECO:0007744|PDB:3NG0"
FT BINDING 134
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PDB:3NG0"
FT BINDING 210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|Ref.6, ECO:0007744|PDB:3NG0"
FT BINDING 215
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PDB:3NG0"
FT BINDING 223
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PDB:3NG0"
FT BINDING 267..268
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 268
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 272
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 274..276
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 276
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|Ref.6, ECO:0007744|PDB:3NG0"
FT BINDING 324
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT BINDING 330
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT BINDING 342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|Ref.6, ECO:0007744|PDB:3NG0"
FT BINDING 342
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 347
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|Ref.6, ECO:0007744|PDB:3NG0"
FT BINDING 356
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|Ref.6, ECO:0007744|PDB:3NG0"
FT BINDING 361
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PDB:3NG0"
FT BINDING 363
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT MOD_RES 401
FT /note="O-AMP-tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT CONFLICT 115
FT /note="V -> A (in Ref. 2; BAA17055)"
FT /evidence="ECO:0000305"
FT CONFLICT 145..147
FT /note="QTE -> PNG (in Ref. 1; CAA49139)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="Q -> E (in Ref. 1; CAA49139)"
FT /evidence="ECO:0000305"
FT CONFLICT 204..206
FT /note="GLC -> AFG (in Ref. 2; BAA17055)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="K -> KFDK (in Ref. 1; CAA49139)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="M -> I (in Ref. 1; CAA49139)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="K -> N (in Ref. 1; CAA49139)"
FT /evidence="ECO:0000305"
FT CONFLICT 378..379
FT /note="ML -> IV (in Ref. 1; CAA49139)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="E -> Q (in Ref. 1; CAA49139)"
FT /evidence="ECO:0000305"
FT HELIX 5..14
FT /evidence="ECO:0007829|PDB:3NG0"
FT STRAND 19..25
FT /evidence="ECO:0007829|PDB:3NG0"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:3NG0"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:3NG0"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:3NG0"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:3NG0"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:3NG0"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:3NG0"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:3NG0"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:3NG0"
FT STRAND 87..95
FT /evidence="ECO:0007829|PDB:3NG0"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:3NG0"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:3NG0"
FT HELIX 107..120
FT /evidence="ECO:0007829|PDB:3NG0"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:3NG0"
FT STRAND 125..133
FT /evidence="ECO:0007829|PDB:3NG0"
FT STRAND 135..145
FT /evidence="ECO:0007829|PDB:3NG0"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:3NG0"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:3NG0"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:3NG0"
FT HELIX 192..204
FT /evidence="ECO:0007829|PDB:3NG0"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:3NG0"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:3NG0"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:3NG0"
FT HELIX 231..251
FT /evidence="ECO:0007829|PDB:3NG0"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:3NG0"
FT STRAND 271..279
FT /evidence="ECO:0007829|PDB:3NG0"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:3NG0"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:3NG0"
FT HELIX 295..315
FT /evidence="ECO:0007829|PDB:3NG0"
FT HELIX 321..324
FT /evidence="ECO:0007829|PDB:3NG0"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:3NG0"
FT STRAND 337..340
FT /evidence="ECO:0007829|PDB:3NG0"
FT STRAND 344..348
FT /evidence="ECO:0007829|PDB:3NG0"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:3NG0"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:3NG0"
FT HELIX 371..388
FT /evidence="ECO:0007829|PDB:3NG0"
FT HELIX 418..427
FT /evidence="ECO:0007829|PDB:3NG0"
FT HELIX 430..433
FT /evidence="ECO:0007829|PDB:3NG0"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:3NG0"
FT HELIX 440..453
FT /evidence="ECO:0007829|PDB:3NG0"
FT HELIX 455..460
FT /evidence="ECO:0007829|PDB:3NG0"
FT HELIX 465..470
FT /evidence="ECO:0007829|PDB:3NG0"
SQ SEQUENCE 473 AA; 53026 MW; 75F8E28EB5EA9515 CRC64;
MARTPQEVLK WIQDENIKII DLKFIDTPGI WQHCSFYYDQ LDENSFTEGI PFDGSSIRGW
KAINESDMCM VPDPNTATID PFCKEPTLSM ICSIKEPRTG EWYNRDPRTI AAKAVEYLRG
TGIADTVYFG PEAEFFLFDD IRFGQTENSS YYFADSVEGR WNTGREEEGG NLGYKPGYKQ
GYFPVAPTDT AQDIRTEMLL TMAGLCVPIE KHHHEVASGG QNELGIKFDK LVNSADNLMI
YKYVIKNVAK KYGKTVTFMP KPIFNDNGSG MHVHQSLWKD GQPLFAGDKY AGFSQMGLWY
IGGILKHAPA LLAFTNPTTN SYKRLVPGFE APVNLAYSQG NRSASVRIPL SGGNPKAKRL
EFRCPDATSN PYLAFAAMLC AGIDGIKNQI DPGEPLDVDI YDLSPEELAK IPSTPGSLEA
ALEALEKDHE FLTGTGVFSP DFVESWIEYK LDNEVNPMRL RPHPYEFSLY YDC
