GLNA3_HALMT
ID GLNA3_HALMT Reviewed; 456 AA.
AC I3R176; M0J406;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 03-SEP-2014, sequence version 2.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Glutamine synthetase 3 {ECO:0000303|PubMed:23069245};
DE Short=GS3 {ECO:0000303|PubMed:23069245};
DE EC=6.3.1.2 {ECO:0000269|PubMed:23069245};
DE AltName: Full=Glutamate--ammonia ligase {ECO:0000250|UniProtKB:P12425};
GN Name=glnA3 {ECO:0000305}; Synonyms=glnA {ECO:0000312|EMBL:AFK17986.2};
GN OrderedLocusNames=HFX_0245 {ECO:0000312|EMBL:AFK17986.2};
GN ORFNames=BM92_08030 {ECO:0000312|EMBL:AHZ22595.1},
GN C439_09150 {ECO:0000312|EMBL:EMA02739.1},
GN E6P09_04325 {ECO:0000312|EMBL:QCQ76583.1};
OS Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC
OS 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=523841;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RX PubMed=22843593; DOI=10.1128/jb.00880-12;
RA Han J., Zhang F., Hou J., Liu X., Li M., Liu H., Cai L., Zhang B., Chen Y.,
RA Zhou J., Hu S., Xiang H.;
RT "Complete genome sequence of the metabolically versatile halophilic
RT archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-
RT hydroxyvalerate) producer.";
RL J. Bacteriol. 194:4463-4464(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RA Bautista V.;
RT "Transcriptional profiles of Haloferax mediterranei on the basis of
RT nitrogen availability.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RA DasSarma S., DasSarma P., DasSarma S., Fomenkov A., Vincze T., Anton B.P.,
RA Roberts R.J.;
RT "Methylomes of two halophilic Archaea, Haloarcula marismortui and Haloferax
RT mediterranei.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, AND INTERACTION
RP WITH GLNK1 AND GLNK2.
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RX PubMed=23069245; DOI=10.1016/j.bbapap.2012.10.006;
RA Pedro-Roig L., Camacho M., Bonete M.J.;
RT "Regulation of ammonium assimilation in Haloferax mediterranei: interaction
RT between glutamine synthetase and two GlnK proteins.";
RL Biochim. Biophys. Acta 1834:16-23(2013).
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:23069245}.
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:0000269|PubMed:23069245};
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: 12-fold increase in the presence of 2-
CC oxoglutarate. Up to 18-fold increase in the presence of 2-oxoglutarate
CC and GlnK1 or GlnK2. Inhibited by AMP and glutamine.
CC {ECO:0000269|PubMed:23069245}.
CC -!- SUBUNIT: Homododecamer (PubMed:23069245). Interacts with the nitrogen
CC regulatory proteins GlnK1 and GlnK2 in the presence of 2-oxoglutarate
CC (PubMed:23069245). {ECO:0000269|PubMed:23069245}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P12425}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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; CP001868; AFK17986.2; -; Genomic_DNA.
DR EMBL; AOLO01000007; EMA02739.1; -; Genomic_DNA.
DR EMBL; CP007551; AHZ22595.1; -; Genomic_DNA.
DR EMBL; CP039139; QCQ76583.1; -; Genomic_DNA.
DR RefSeq; WP_004058344.1; NZ_CP039139.1.
DR AlphaFoldDB; I3R176; -.
DR SMR; I3R176; -.
DR STRING; 523841.HFX_0245; -.
DR EnsemblBacteria; AFK17986; AFK17986; HFX_0245.
DR EnsemblBacteria; AHZ22595; AHZ22595; BM92_08030.
DR EnsemblBacteria; EMA02739; EMA02739; C439_09150.
DR EnsemblBacteria; QCQ76583; QCQ76583; E6P09_04325.
DR GeneID; 40155616; -.
DR KEGG; hme:HFX_0245; -.
DR PATRIC; fig|523841.21.peg.1859; -.
DR eggNOG; arCOG01909; Archaea.
DR HOGENOM; CLU_017290_1_3_2; -.
DR OrthoDB; 47310at2157; -.
DR Proteomes; UP000006469; Chromosome.
DR Proteomes; UP000011603; Unassembled WGS sequence.
DR Proteomes; UP000027075; Chromosome.
DR Proteomes; UP000299011; 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; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding.
FT CHAIN 1..456
FT /note="Glutamine synthetase 3"
FT /id="PRO_0000453010"
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 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"
SQ SEQUENCE 456 AA; 50449 MW; 7BAC516394FC0E60 CRC64;
MTEDNVLTDG GLSAEAQAVI DEIEEKNVDF LRLQFTDILG TVKNVSIPAS QAEKAFTEGI
YFDGSSIDGF VRIQESDMRL EPDPSTFAIL PWRKKENSAA ARLICDVFNT STGEPFSGDP
RGVLKRAIER AEDMGYDINA APEPEFFLFE EDEDGSATTI TNDAGGYFDL APKDLASDVR
RDIIYGLESM GFDIEASHHE VAEGQHEINF TYDDALSTAD NVATFRSVVR AIAAEHDLHA
TFMPKPIAKV NGSGMHTHIS LFKDGENAFH DGADEFDLSE TAKQFTAGIL EHAPAVTAVA
NPTVNSYKRL VPGYEAPVYI AWSDRNRSAL IRKPAARTPA ASRIEARFPD PSCNPYLALA
ALIHAGLDGI ERELDCADPV RENIYEFDEE KREEYGIETL PKDLGAAVDA LEEDEVIQNA
LGEHVTEKFV EAKRSEFKDY LVAVSEWEID RYLETF
