GLNA_SULAC
ID GLNA_SULAC Reviewed; 473 AA.
AC Q9HH09; Q4J8S1;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Glutamine synthetase {ECO:0000303|PubMed:9865608};
DE Short=GS {ECO:0000303|PubMed:9865608};
DE EC=6.3.1.2 {ECO:0000305|PubMed:9865608};
DE AltName: Full=Glutamate--ammonia ligase {ECO:0000305};
DE AltName: Full=Glutamine synthetase I alpha {ECO:0000305};
DE Short=GSI alpha {ECO:0000305};
GN Name=glnA {ECO:0000303|PubMed:9865608}; OrderedLocusNames=Saci_1483;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-26, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION,
RP COFACTOR, SUBCELLULAR LOCATION, AND SUBUNIT.
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=9865608; DOI=10.1515/bchm.1998.379.11.1349;
RA Yin Z.M., Purschke W.G., Schaefer G., Schmidt C.L.;
RT "The glutamine synthetase from the hyperthermoacidophilic crenarcheon
RT Sulfolobus acidocaldarius: isolation, characterization and sequencing of
RT the gene.";
RL Biol. Chem. 379:1349-1354(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
CC -!- FUNCTION: Probably involved in nitrogen metabolism via ammonium
CC assimilation. Catalyzes the ATP-dependent biosynthesis of glutamine
CC from glutamate and ammonia. {ECO:0000269|PubMed:9865608}.
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:0000305|PubMed:9865608};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:9865608};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:9865608};
CC Note=Binds 2 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:P9WN39};
CC -!- ACTIVITY REGULATION: Strongly inhibited by glycine and L-alanine. AMP
CC at 10 mM displays a very weak inhibitory effect. The activity of this
CC enzyme is not controlled by adenylation. {ECO:0000269|PubMed:9865608}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.15 mM for ADP {ECO:0000269|PubMed:9865608};
CC KM=0.24 mM for manganese {ECO:0000269|PubMed:9865608};
CC KM=1.3 mM for L-glutamine {ECO:0000269|PubMed:9865608};
CC pH dependence:
CC Optimum pH is between 7 and 7.5. {ECO:0000269|PubMed:9865608};
CC Temperature dependence:
CC Optimum temperature is 90 degrees Celsius. In the absence of
CC magnesium or manganese ions about 50% of the activity is lost within
CC 100 minutes at 78 degrees Celsius, whereas more than 95% of the
CC activity is retained in presence of 4 mM manganese ions. Magnesium
CC ions are a less effective. {ECO:0000269|PubMed:9865608};
CC -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two hexagons.
CC {ECO:0000269|PubMed:9865608}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:9865608}.
CC -!- MISCELLANEOUS: GlnA of S.acidocaldarius is unique among the archeal
CC glutamine synthetase since the regulatory properties suggest a position
CC within the GS I-alpha subgroup. However, the sequence shows more
CC pronounced similarities to the GS I-beta subgroup.
CC {ECO:0000269|PubMed:9865608}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR EMBL; AJ224678; CAC20905.1; -; Genomic_DNA.
DR EMBL; CP000077; AAY80804.1; -; Genomic_DNA.
DR RefSeq; WP_011278306.1; NC_007181.1.
DR AlphaFoldDB; Q9HH09; -.
DR SMR; Q9HH09; -.
DR STRING; 330779.Saci_1483; -.
DR EnsemblBacteria; AAY80804; AAY80804; Saci_1483.
DR GeneID; 3474677; -.
DR KEGG; sai:Saci_1483; -.
DR PATRIC; fig|330779.12.peg.1427; -.
DR eggNOG; arCOG01909; Archaea.
DR HOGENOM; CLU_017290_1_2_2; -.
DR OMA; VFPWESK; -.
DR BRENDA; 6.3.1.2; 6160.
DR Proteomes; UP000001018; 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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Direct protein sequencing; Ligase; Magnesium;
KW Manganese; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9865608"
FT CHAIN 2..473
FT /note="Glutamine synthetase"
FT /id="PRO_0000153213"
FT DOMAIN 18..102
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 110..473
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT BINDING 133
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 135
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 212
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 220
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 264..265
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 265
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 269
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 271..273
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 273
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P77961"
FT BINDING 324
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 330
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT BINDING 342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 342
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 347
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 CONFLICT 185
FT /note="D -> V (in Ref. 1; CAC20905)"
FT /evidence="ECO:0000305"
FT CONFLICT 204..207
FT /note="FTIE -> TIEA (in Ref. 1; CAC20905)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="A -> H (in Ref. 1; CAC20905)"
FT /evidence="ECO:0000305"
FT CONFLICT 211..259
FT /note="HEVATAGQGEIDFRFSTLADTADKVQVLKYVTKNIASKRGMIATFMPKP ->
FT EVATAGQGDIDFRFSTLADTADKVQVLKYVTKNIASKRGMIATFMPKPF (in Ref.
FT 1; CAC20905)"
FT /evidence="ECO:0000305"
FT CONFLICT 261..299
FT /note="FGDNGSGMHTHFSLWTKDGKNLMYDPNDEYAELSQIGRY -> GDNGSGMHT
FT HFSLWTKDGKNLMYDPNDEYAELSQIGRYI (in Ref. 1; CAC20905)"
FT /evidence="ECO:0000305"
FT CONFLICT 301..303
FT /note="IGG -> GPL (in Ref. 1; CAC20905)"
FT /evidence="ECO:0000305"
FT CONFLICT 305..314
FT /note="LEHGRALSAI -> EHGRALSAIV (in Ref. 1; CAC20905)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="P -> G (in Ref. 1; CAC20905)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 473 AA; 53586 MW; F8EA4FD71B1CDD5D CRC64;
MPGLPKNEHE ALEFLKSNNI KWVDLQFTDL LGKLQHITIP SNEFDESSFK VGFGKLDGSS
IKGFTSIYES DMVLLPIPQT MTLIPWMQGV ARVLTKVFWG GGKGRFERDP RGIAEEAEKY
QSEQGYVSYF GPELEFFVFD KVEVDASLPQ SGTGYKIHSR EAPWSKNGGY VIRYKEGYYP
ASPVDQLMDI RLEIISTLVD YFGFTIEAAH HEVATAGQGE IDFRFSTLAD TADKVQVLKY
VTKNIASKRG MIATFMPKPF FGDNGSGMHT HFSLWTKDGK NLMYDPNDEY AELSQIGRYI
IGGLLEHGRA LSAIVAPTTN SYRRLVPGYE APVYLVWSKS NRSAAIRIPA YYKGMEKAKR
LEYRPPDPSS NPYLVFSAIL MAGLDGIRRK LDPGDPVDEN IYHMSEEKKR SLKIRELPGS
LDEALNELES DNEFLKPVFN SSILQAYLDL KKEEAKMMQL YPHPMEIYQY LDS
