GLN1B_NOSS1
ID GLN1B_NOSS1 Reviewed; 474 AA.
AC P00964;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Glutamine synthetase {ECO:0000250|UniProtKB:P77961};
DE Short=GS {ECO:0000250|UniProtKB:P77961};
DE EC=6.3.1.2 {ECO:0000250|UniProtKB:P77961};
DE AltName: Full=Glutamate--ammonia ligase {ECO:0000250|UniProtKB:P77961};
DE AltName: Full=Glutamine synthetase I beta {ECO:0000250|UniProtKB:P77961};
DE Short=GSI beta {ECO:0000250|UniProtKB:P77961};
GN Name=glnA {ECO:0000250|UniProtKB:P77961}; OrderedLocusNames=alr2328;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Tumer N.E., Robinson S.J., Haselkorn R.;
RT "Different promoters for the Anabaena glutamine synthetase gene during
RT growth usine molecular or fixed nitrogen.";
RL Nature 306:337-342(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
RN [3]
RP PROTEIN SEQUENCE OF 23-57; 98-104; 142-196; 213-243; 326-343 AND 391-411,
RP AND MASS SPECTROMETRY.
RA Singh H., Rajaram H., Apte S.K.;
RL Submitted (DEC-2008) to UniProtKB.
CC -!- FUNCTION: Involved in nitrogen metabolism via ammonium assimilation.
CC Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate
CC and ammonia. {ECO:0000250|UniProtKB:P77961}.
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:0000250|UniProtKB:P77961};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P77961};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P77961};
CC -!- ACTIVITY REGULATION: The activity of this enzyme could be controlled by
CC adenylation under conditions of abundant glutamine.
CC {ECO:0000250|UniProtKB:Q3V5W6}.
CC -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two hexagons.
CC {ECO:0000250|UniProtKB:P77961}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P9WN39}.
CC -!- MASS SPECTROMETRY: Mass=53314; Method=MALDI;
CC Evidence={ECO:0000269|Ref.3};
CC -!- MISCELLANEOUS: In Anabaena, it is present in ammonia-grown vegetative
CC cells as well as in heterocysts (for nitrogen fixation).
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000250|UniProtKB:P77961}.
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DR EMBL; X00147; CAA24982.1; -; Genomic_DNA.
DR EMBL; BA000019; BAB74027.1; -; Genomic_DNA.
DR PIR; A01192; AJAIQ.
DR PIR; AI2096; AI2096.
DR RefSeq; WP_010996484.1; NZ_RSCN01000004.1.
DR AlphaFoldDB; P00964; -.
DR SMR; P00964; -.
DR STRING; 103690.17131420; -.
DR EnsemblBacteria; BAB74027; BAB74027; BAB74027.
DR KEGG; ana:alr2328; -.
DR eggNOG; COG0174; Bacteria.
DR OMA; PHPHEFE; -.
DR OrthoDB; 416474at2; -.
DR Proteomes; UP000002483; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004356; F:glutamate-ammonia ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR GO; GO:0043158; P:heterocyst differentiation; IEA:UniProtKB-KW.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
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 ATP-binding; Cytoplasm; Direct protein sequencing; Heterocyst; Ligase;
KW Magnesium; Metal-binding; Nitrogen fixation; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..474
FT /note="Glutamine synthetase"
FT /id="PRO_0000153215"
FT DOMAIN 14..99
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 106..474
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT BINDING 131
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P77961"
FT BINDING 133
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P77961"
FT BINDING 211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P77961"
FT BINDING 216
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P77961"
FT BINDING 224
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P77961"
FT BINDING 268..269
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 269
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 273
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 275..277
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 277
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P77961"
FT BINDING 325
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT BINDING 331
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT BINDING 343
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P77961"
FT BINDING 343
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 348
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P77961"
FT BINDING 357
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P77961"
FT BINDING 362
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P77961"
FT BINDING 364
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT MOD_RES 402
FT /note="O-AMP-tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT CONFLICT 107
FT /note="R -> P (in Ref. 1; CAA24982)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="Missing (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 474 AA; 53136 MW; 6A801A1B55262B28 CRC64;
MTTPQEVLKR IQDEKIELID LKFIDTVGTW QHLTLYQNQI DESSFSDGVP FDGSSIRGWK
AINESDMTMV LDPNTAWIDP FMEVPTLSIV CSIKEPRTGE WYNRCPRVIA QKAIDYLVST
GIGDTAFFGP EAEFFIFDSA RFAQNANEGY YFLDSVEGAW NSGKEGTADK PNLAYKPRFK
EGYFPVSPTD SFQDIRTEML LTMAKLGVPI EKHHHEVATG GQCELGFRFG KLIEAADWLM
IYKYVIKNVA KKYGKTVTFM PKPIFGDNGS GMHCHQSIWK DGKPLFAGDQ YAGLSEMGLY
YIGGLLKHAP ALLAITNPST NSYKRLVPGY EAPVNLAYSQ GNRSASIRIP LSGTNPKAKR
LEFRCPDATS NPYLAFAAML CAGIDGIKNK IHPGEPLDKN IYELSPEELA KVPSTPGSLE
LALEALENDH AFLTDTGVFT EDFIQNWIDY KLANEVKQMQ LRPHPYEFSI YYDV
