GLNA2_FRAAL
ID GLNA2_FRAAL Reviewed; 352 AA.
AC P20805;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Glutamine synthetase {ECO:0000303|PubMed:1975584};
DE Short=GS {ECO:0000303|PubMed:1975584};
DE EC=6.3.1.2 {ECO:0000250|UniProtKB:P16580};
DE AltName: Full=Glutamate--ammonia ligase {ECO:0000305};
DE AltName: Full=Glutamine synthetase II {ECO:0000303|PubMed:1975584};
DE Short=GSII {ECO:0000303|PubMed:1975584};
GN Name=glnII {ECO:0000303|PubMed:1975584};
OS Frankia alni.
OC Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=1859;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=CpI1;
RX PubMed=1975584; DOI=10.1128/jb.172.9.5335-5342.1990;
RA Rochefort D.A., Benson D.R.;
RT "Molecular cloning, sequencing, and expression of the glutamine synthetase
RT II (glnII) gene from the actinomycete root nodule symbiont Frankia sp.
RT strain CpI1.";
RL J. Bacteriol. 172:5335-5342(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
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:Q02154}.
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:P16580};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P16580};
CC -!- SUBUNIT: Homooctamer and homotetramer. {ECO:0000250|UniProtKB:Q02154}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P16580}.
CC -!- INDUCTION: By nitrogen starvation. {ECO:0000305|PubMed:1975584}.
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|PubMed:1975584}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR EMBL; M58415; AAA62803.1; -; Genomic_DNA.
DR EMBL; L10632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P20805; -.
DR SMR; P20805; -.
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; IPR027302; Gln_synth_N_conserv_site.
DR Pfam; PF00120; Gln-synt_C; 2.
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 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 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Ligase; Magnesium; Metal-binding;
KW Nitrogen fixation; Nucleotide-binding; Stress response.
FT CHAIN 1..352
FT /note="Glutamine synthetase"
FT /id="PRO_0000153222"
FT DOMAIN 3..82
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 87..352
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT BINDING 108
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 110
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 169
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 176
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 272
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
SQ SEQUENCE 352 AA; 38666 MW; 2BFCC8B8A87C3340 CRC64;
MSYQAEYIWI DGTEPEPLMR SKTRIIKDGK EPEIWGFDGS STNQAPGSNS DCVLRPVFET
PDPIRGGDNR LVLCEVQLTD FTPPTNTRAA ALGVAERYAD MSPMFGIEQE YTFFKDGRPY
GWPEVGYPAP QGPYYCGVGG SKMPGRQIVE RHTQACLDAG LAIEGTNAEV MMGQWEFQIG
VLPAPAIGDQ IWLGRWLLHR IAEDYGVEVS FAAKPIPGDW NGAGAHTNFS TKQTMEGWDA
IVTCCEALGT RVTEHVTHYG KGIEDRLTGK HETAPWNKYS WGASDRGASV RIPWAVEKAK
KGWLEDRRPN ANMDPYLVTA LMIDTCCSAL AGDKPTLFVP SQTTPAPAEA SV
