ID A0A5P9QDQ9_9MICO Unreviewed; 447 AA.
AC A0A5P9QDQ9;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Glutamine synthetase {ECO:0000313|EMBL:QFU98605.1};
DE EC=6.3.1.2 {ECO:0000313|EMBL:QFU98605.1};
GN ORFNames=KDY119_02121 {ECO:0000313|EMBL:QFU98605.1};
OS Luteimicrobium xylanilyticum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Luteimicrobium.
OX NCBI_TaxID=1133546 {ECO:0000313|EMBL:QFU98605.1, ECO:0000313|Proteomes:UP000326702};
RN [1] {ECO:0000313|EMBL:QFU98605.1, ECO:0000313|Proteomes:UP000326702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HY-24 {ECO:0000313|EMBL:QFU98605.1,
RC ECO:0000313|Proteomes:UP000326702};
RA Kim D.Y., Park H.-Y.;
RT "Genome sequence of Luteimicrobium xylanilyticum HY-24.";
RL Submitted (OCT-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|ARBA:ARBA00009897, ECO:0000256|PROSITE-ProRule:PRU01330,
CC ECO:0000256|RuleBase:RU000384}.
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DR EMBL; CP045529; QFU98605.1; -; Genomic_DNA.
DR RefSeq; WP_036949782.1; NZ_CP045529.1.
DR AlphaFoldDB; A0A5P9QDQ9; -.
DR KEGG; lxl:KDY119_02121; -.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000326702; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004356; F:glutamine synthetase 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; Glutamine synthetase, N-terminal domain; 1.
DR Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR InterPro; IPR008147; Gln_synt_N.
DR InterPro; IPR036651; Gln_synt_N_sf.
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 NCBIfam; TIGR00653; GlnA; 1.
DR PANTHER; PTHR43785; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE; 1.
DR PANTHER; PTHR43785:SF11; GLUTAMINE SYNTHETASE; 1.
DR Pfam; PF00120; Gln-synt_C; 1.
DR Pfam; PF03951; Gln-synt_N; 1.
DR SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF54368; Glutamine synthetase, N-terminal domain; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 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 {ECO:0000256|PIRSR:PIRSR604809-2};
KW Ligase {ECO:0000313|EMBL:QFU98605.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR604809-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000326702}.
FT DOMAIN 15..100
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 107..447
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
FT BINDING 184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 247..249
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 298
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 304
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 316
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 316
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 338
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
SQ SEQUENCE 447 AA; 50363 MW; 69EB47B313CF5A9B CRC64;
MDRQQEFVLR TVEERDIRFI RLWFTDVLGM LKSVAVAPAE LESAFSEGIG FDGSSIEGFT
RVYEADMIAK PDPTTFQVLP WRGEQQGTAR MFCDILTPDG EPSLADSRYV LKRALAKASD
KGFTFYTHPE VEFYLFQALD LDAPVPRLVP VDRGGYFDHV PRGSAHDFRR AAISMLESMG
ISVEFSHHEA GPGQNEIDLR YADALTTADN LMTFRTVVKE VALEQGVYAS FMPKPLAEHP
GSGMHTHMSL FEGDRNAFHE PGSEYELSKV ARQFIAGLLH HAAEITAVTN QYVNSYKRLW
GGSEAPSFVS WGHNNRSALV RVPMYKPGKG NSSRVEYRAL DSAANPYLSF ALLLAAGLKG
IEEGYELPEE TSDDVWELTP TERRALDIRP LPQDLDEAVG IMERSELVAE TLGEHVFDYV
LRNKREEWTA YRTQVTPFEL ERFFSIL
//
