GLN1B_FRAAL
ID GLN1B_FRAAL Reviewed; 474 AA.
AC P46033;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Glutamine synthetase {ECO:0000250|UniProtKB:P9WN39};
DE Short=GS {ECO:0000250|UniProtKB:P9WN39};
DE EC=6.3.1.2 {ECO:0000250|UniProtKB:P9WN39};
DE AltName: Full=Glutamate--ammonia ligase {ECO:0000250|UniProtKB:P9WN39};
DE AltName: Full=Glutamine synthetase I beta {ECO:0000250|UniProtKB:P9WN39};
DE Short=GSI beta {ECO:0000250|UniProtKB:P9WN39};
GN Name=glnA {ECO:0000250|UniProtKB:P9WN39};
OS Frankia alni.
OC Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=1859;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CpI1;
RX PubMed=8099074; DOI=10.1128/jb.175.11.3679-3684.1993;
RA Hosted T.J., Rochefort D.A., Benson D.R.;
RT "Close linkage of genes encoding glutamine synthetases I and II in Frankia
RT alni CpI1.";
RL J. Bacteriol. 175:3679-3684(1993).
CC -!- FUNCTION: Catalyzes the ATP-dependent biosynthesis of glutamine from
CC glutamate and ammonia. {ECO:0000250|UniProtKB:P9WN39}.
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:P9WN39};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P9WN39};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P9WN39};
CC -!- ACTIVITY REGULATION: The activity of this enzyme could be controlled by
CC adenylation under conditions of abundant glutamine.
CC {ECO:0000250|UniProtKB:P9WN39}.
CC -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two hexagons.
CC {ECO:0000250|UniProtKB:P9WN39}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P9WN39}.
CC -!- MISCELLANEOUS: Two forms of glutamine synthetase (GSI and GSII) can be
CC found in this nitrogen fixing bacteria, GSI is a typical prokaryotic
CC glutamine synthetase whereas GSII is similar to the eukaryotic enzyme.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000250|UniProtKB:P9WN39}.
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DR EMBL; L10631; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A40598; A40598.
DR AlphaFoldDB; P46033; -.
DR SMR; P46033; -.
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: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 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Ligase; Magnesium; Metal-binding;
KW Nitrogen fixation; Nucleotide-binding; Phosphoprotein.
FT CHAIN 1..474
FT /note="Glutamine synthetase"
FT /id="PRO_0000153221"
FT DOMAIN 15..99
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 107..474
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT BINDING 132
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 134
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 215
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 223
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
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:0000250|UniProtKB:P77961"
FT BINDING 325
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
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:P9WN39"
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:P9WN39"
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:P9WN39"
FT BINDING 364
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT MOD_RES 402
FT /note="O-AMP-tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
SQ SEQUENCE 474 AA; 53952 MW; FE1DB19AC1735652 CRC64;
MFTKAEDVLR YIRDEDVQFI DVRFCDLPGI MQHFTIPTQV FAESVFTDGL MFDGSSIRGF
QAIHESDMLL LPDPQTAFVD PFREHKTLAM TFFIHDPITK EQYSRDPRNI AKKAETYLRG
TSIADTAYFG PEAEFYIFDD VRYDYNPYGS MHHVDSVEAA WNTSRKEEGG NLGYKPRFKG
GYFPVPPTDH FTDLRSEMTR VLYETGITVE MQHHEVGTAG QAEIDIRYDT LLKTADNLML
YKYVIRNVAR SRGKTVTFMP KPLFEDNGSG MHVHSSLWKD GEPLFYSPNG YGGLSDTARY
YIGGLLHHAP ALLAFTNPTT NSYRRLVPGY EAPVNLVYSA RNRSACCRIP LGGDSPKAKR
VEFRVPDPSC NPYLAFAAML MAGLDGIRNK IDPPDPIDKD LYELPPDELA AVPQVPGSLE
KVLDALEADN DFLREGDVFT TDLIETWLEY KRLNEVDAIR LRPHPYEFTL YYDI
