GLNA_HALVD
ID GLNA_HALVD Reviewed; 456 AA.
AC P43386; D4GZI4;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Glutamine synthetase {ECO:0000250|UniProtKB:P12425};
DE Short=GS {ECO:0000250|UniProtKB:P12425};
DE EC=6.3.1.2 {ECO:0000250|UniProtKB:P12425};
DE AltName: Full=Glutamate--ammonia ligase {ECO:0000250|UniProtKB:P12425};
DE AltName: Full=Glutamine synthetase I alpha {ECO:0000250|UniProtKB:P12425};
DE Short=GSI alpha {ECO:0000250|UniProtKB:P12425};
GN Name=glnA {ECO:0000250|UniProtKB:P12425}; OrderedLocusNames=HVO_0239;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7916055; DOI=10.1007/bf00175876;
RA Brown J.R., Masuchi Y., Robb F.T., Doolittle W.F.;
RT "Evolutionary relationships of bacterial and archaeal glutamine synthetase
RT genes.";
RL J. Mol. Evol. 38:566-576(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
CC -!- FUNCTION: Glutamine synthetase (GS) is an unusual multitasking protein
CC that functions as an enzyme, a transcription coregulator, and a
CC chaperone in ammonium assimilation and in the regulation of genes
CC involved in nitrogen metabolism. It catalyzes the ATP-dependent
CC biosynthesis of glutamine from glutamate and ammonia. Feedback-
CC inhibited GlnA also interacts with and regulates the activity of the
CC transcriptional regulator TnrA. During nitrogen limitation, TnrA is in
CC its DNA-binding active state and turns on the transcription of genes
CC required for nitrogen assimilation. Under conditions of nitrogen
CC excess, feedback-inhibited GlnA forms a stable complex with TnrA, which
CC inhibits its DNA-binding activity. In contrast, feedback-inhibited GlnA
CC acts as a chaperone to stabilize the DNA-binding activity of GlnR,
CC which represses the transcription of nitrogen assimilation genes.
CC {ECO:0000250|UniProtKB:P12425}.
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:P12425};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P12425};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P12425};
CC -!- ACTIVITY REGULATION: Inhibited by glutamine.
CC {ECO:0000250|UniProtKB:P12425}.
CC -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two hexagons.
CC In its feedback-inhibited form, interacts with TnrA in order to block
CC its DNA-binding activity. {ECO:0000250|UniProtKB:P12425}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P12425}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR EMBL; U03029; AAC43489.1; -; Genomic_DNA.
DR EMBL; CP001956; ADE03696.1; -; Genomic_DNA.
DR PIR; T47127; T47127.
DR RefSeq; WP_004045354.1; NZ_AOHU01000107.1.
DR AlphaFoldDB; P43386; -.
DR SMR; P43386; -.
DR STRING; 309800.C498_19454; -.
DR EnsemblBacteria; ADE03696; ADE03696; HVO_0239.
DR GeneID; 8924457; -.
DR KEGG; hvo:HVO_0239; -.
DR eggNOG; arCOG01909; Archaea.
DR HOGENOM; CLU_017290_1_3_2; -.
DR OMA; PHPHEFE; -.
DR OrthoDB; 47310at2157; -.
DR Proteomes; UP000008243; 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 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 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..456
FT /note="Glutamine synthetase"
FT /id="PRO_0000153203"
FT DOMAIN 26..113
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 120..456
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT BINDING 143
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 145
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 195
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 200
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 207
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 251..252
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 252
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 256
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 258..260
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 260
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P77961"
FT BINDING 309
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT BINDING 315
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT BINDING 327
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 327
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 332
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 345
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 347
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT SITE 72
FT /note="Important for inhibition by glutamine"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT CONFLICT 130..131
FT /note="RA -> P (in Ref. 1; AAC43489)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="A -> R (in Ref. 1; AAC43489)"
FT /evidence="ECO:0000305"
FT CONFLICT 299..308
FT /note="VADPTVNSYK -> SLTRRSTPTR (in Ref. 1; AAC43489)"
FT /evidence="ECO:0000305"
FT CONFLICT 403..413
FT /note="DLGGAVDALEE -> TSAARRRPRR (in Ref. 1; AAC43489)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 456 AA; 50522 MW; 7A3905E9706174EA CRC64;
MTEDNALTDG GLSDEAQAVI DEIEEKNVDF LRLQFTDILG TVKNVSIPAS QAEKAFTEGI
YFDGSSIDGF VRIQESDMRL EPDPSTFAVL PWRKKENSAA GRLICDVFNT STGEPFSGDP
RGVLKRAIER AEELGYDVNV APEPEFFLFE EDEDGRATTV TNDAGGYFDL APKDLASDVR
RDIIYGLESM GFDIEASHHE VAEGQHEINF TYDDALSTAD NVATFRSVVR AIAAEHDLHA
TFMPKPIPRI NGSGMHTHIS LFKDGENAFH DGDDEFDLSD TAKSFVAGIL DHAPAITAVA
DPTVNSYKRL VPGYEAPVYI AWSDRNRSAL IRKPAARTPA ASRIEARFPD PSCNPYLAFA
ALIHAGLDGV EKGLDCPDPV RENIYEFDEA KREEYGIETL PKDLGGAVDA LEEDEVIQEA
LGDHVFEKFV EAKRSEFKDY LVDVSQWELD RYLETF
