GLNA1_METMA
ID GLNA1_METMA Reviewed; 447 AA.
AC Q8PY99;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Glutamine synthetase {ECO:0000303|PubMed:15752204};
DE Short=GS {ECO:0000250|UniProtKB:P12425};
DE EC=6.3.1.2 {ECO:0000269|PubMed:15752204};
DE AltName: Full=Glutamate--ammonia ligase {ECO:0000250|UniProtKB:P12425};
GN Name=glnA1 {ECO:0000303|PubMed:15752204};
GN OrderedLocusNames=MM_0964 {ECO:0000312|EMBL:AAM30660.1};
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, AND INTERACTION
RP WITH GLNK1.
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=15752204; DOI=10.1111/j.1365-2958.2005.04511.x;
RA Ehlers C., Weidenbach K., Veit K., Forchhammer K., Schmitz R.A.;
RT "Unique mechanistic features of post-translational regulation of glutamine
RT synthetase activity in Methanosarcina mazei strain Goe1 in response to
RT nitrogen availability.";
RL Mol. Microbiol. 55:1841-1854(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:15752204}.
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:15752204};
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: Directly stimulated by the effector molecule 2-
CC oxoglutarate. Inhibited by GlnK1. 2-oxoglutarate antagonizes the
CC inhibitory effects of GlnK1, but does not prevent GlnK1/GlnA1 complex
CC formation. {ECO:0000269|PubMed:15752204}.
CC -!- SUBUNIT: Homohexamer. Interacts and forms stable complexes with the
CC regulatory protein GlnK1. {ECO:0000269|PubMed:15752204}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P12425}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR EMBL; AE008384; AAM30660.1; -; Genomic_DNA.
DR RefSeq; WP_011032914.1; NC_003901.1.
DR AlphaFoldDB; Q8PY99; -.
DR SMR; Q8PY99; -.
DR STRING; 192952.MM_0964; -.
DR EnsemblBacteria; AAM30660; AAM30660; MM_0964.
DR GeneID; 44085795; -.
DR GeneID; 66137635; -.
DR KEGG; mma:MM_0964; -.
DR PATRIC; fig|192952.21.peg.1140; -.
DR eggNOG; arCOG01909; Archaea.
DR HOGENOM; CLU_017290_1_3_2; -.
DR OMA; TFYTHPE; -.
DR BRENDA; 6.3.1.2; 3270.
DR Proteomes; UP000000595; 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; Reference proteome.
FT CHAIN 1..447
FT /note="Glutamine synthetase"
FT /id="PRO_0000453011"
FT DOMAIN 20..105
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 112..447
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT BINDING 135
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 137
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 199
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 243..244
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 244
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 248
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 252
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P77961"
FT BINDING 301
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT BINDING 307
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT BINDING 319
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 319
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 324
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 336
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 338
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
SQ SEQUENCE 447 AA; 50593 MW; CB7C2A9960150F92 CRC64;
MVQMKKCTTK EDVLEAVKER DVKFIRTQFT DTLGIIKSWA IPAEQLEEAF ENGVMFDGSS
IQGFTRIEES DMKLALDPST FRILPWRPAT GAVARILGDV YLPDGNPFKG DPRYVLKTAI
KEAEKMGFSM NVGPELEFFL FKLDANGNPT TELTDQGGYF DFAPLDRAQD VRRDIDYALE
HMGFQIEASH HEVAPSQHEI DFRFGDVLCT ADNVVTFKYV VKSIAYHKGY YASFMPKPLF
GVNGSGMHSN QSLFKDGKNV FYDPDTPTKL SQDAMYYIGG LLKHIREFTA VTNPVVNSYK
RLVPGYEAPV YISWSAQNRS SLIRIPATRG NGTRIELRCP DPACNPYLAF ALMLRAGLEG
IKNKIDPGEP TNVNIFHLSD KEREERGIRS LPADLKEAID EMKGSKFVKE ALGEHVFSHY
LCAKEMEWDE YKAVVHPWEL SRYLSML
