GLNA_PYRFU
ID GLNA_PYRFU Reviewed; 439 AA.
AC Q05907;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2002, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Glutamine synthetase {ECO:0000250|UniProtKB:Q9HH09};
DE Short=GS {ECO:0000250|UniProtKB:Q9HH09};
DE EC=6.3.1.2 {ECO:0000250|UniProtKB:Q9HH09};
DE AltName: Full=Glutamate--ammonia ligase {ECO:0000250|UniProtKB:Q9HH09};
DE AltName: Full=Glutamine synthetase I alpha {ECO:0000250|UniProtKB:Q9HH09};
DE Short=GSI alpha {ECO:0000250|UniProtKB:Q9HH09};
GN Name=glnA {ECO:0000250|UniProtKB:Q9HH09}; OrderedLocusNames=PF0450;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
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 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
CC -!- FUNCTION: Probably involved in nitrogen metabolism via ammonium
CC assimilation. Catalyzes the ATP-dependent biosynthesis of glutamine
CC from glutamate and ammonia. {ECO:0000250|UniProtKB:Q9HH09}.
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:Q9HH09};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9HH09};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P9WN39};
CC -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two hexagons.
CC {ECO:0000250|UniProtKB:Q9HH09}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9HH09}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000250|UniProtKB:Q9HH09}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L12410; AAA71968.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL80574.1; -; Genomic_DNA.
DR RefSeq; WP_011011567.1; NZ_CP023154.1.
DR AlphaFoldDB; Q05907; -.
DR SMR; Q05907; -.
DR STRING; 186497.PF0450; -.
DR EnsemblBacteria; AAL80574; AAL80574; PF0450.
DR GeneID; 41712250; -.
DR KEGG; pfu:PF0450; -.
DR PATRIC; fig|186497.12.peg.474; -.
DR eggNOG; arCOG01909; Archaea.
DR HOGENOM; CLU_017290_1_3_2; -.
DR OMA; PHPHEFE; -.
DR OrthoDB; 47310at2157; -.
DR PhylomeDB; Q05907; -.
DR Proteomes; UP000001013; 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; Reference proteome.
FT CHAIN 1..439
FT /note="Glutamine synthetase"
FT /id="PRO_0000153209"
FT DOMAIN 12..93
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 99..439
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT BINDING 122
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 124
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 177
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 184
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 229
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 233
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 235..237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P77961"
FT BINDING 283
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 289
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT BINDING 301
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 301
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 306
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 313
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P77961"
FT BINDING 318
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 320
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT CONFLICT 203
FT /note="K -> G (in Ref. 1; AAA71968)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="M -> L (in Ref. 1; AAA71968)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="A -> S (in Ref. 1; AAA71968)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="I -> L (in Ref. 1; AAA71968)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="S -> N (in Ref. 1; AAA71968)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="E -> G (in Ref. 1; AAA71968)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="A -> S (in Ref. 1; AAA71968)"
FT /evidence="ECO:0000305"
FT CONFLICT 421..426
FT /note="MPKDTK -> IPPDTE (in Ref. 1; AAA71968)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 439 AA; 50183 MW; 96563A8E9A0E0892 CRC64;
MNISVSMNKF DSKIKFVQLV FVDINGMPKG MEIPASRLEE AVTDGISFDG SSVPGFQGIE
DSDLVFKADP DTYVEVPWDN VARVYGFIYK DNKPYGADPR GILKRALEEL EKEGYKAYIG
PEPEFYLFKK NGTWELEIPD VGGYFDILTL DKARDIRREI AEYMPSFGLI PEVLHHEVGK
AQHEIDFRYD EALKTADNIV SFKYITKAVA EMHGLYATFM PKPLFGFPGN GMHLHISLWK
DGENVFMGEE GLSEIALHFI GGILKHAKAL TAVTNPTVNS YKRLVPSYEA PVYISWGYRN
RSALIRVPAF WGKGARIEYR CPDPSANPYF AFAAVLKAGL DGIKHKIDPF AYVEENVYEM
SEEKRKELGI ETLPGSLGEA LEELEKDKVV KEALGDAYKN FINYKWKEWE SYLEYLEEKH
MPKDTKKVTE WELERYFFL
