ID A0A0Q7AWB5_9ACTN Unreviewed; 446 AA.
AC A0A0Q7AWB5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Glutamine synthetase {ECO:0000313|EMBL:KQW43973.1};
GN ORFNames=ASC77_21505 {ECO:0000313|EMBL:KQW43973.1};
OS Nocardioides sp. Root1257.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736439 {ECO:0000313|EMBL:KQW43973.1, ECO:0000313|Proteomes:UP000051939};
RN [1] {ECO:0000313|EMBL:KQW43973.1, ECO:0000313|Proteomes:UP000051939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1257 {ECO:0000313|EMBL:KQW43973.1,
RC ECO:0000313|Proteomes:UP000051939};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW43973.1, ECO:0000313|Proteomes:UP000051939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1257 {ECO:0000313|EMBL:KQW43973.1,
RC ECO:0000313|Proteomes:UP000051939};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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|PROSITE-ProRule:PRU01330, ECO:0000256|RuleBase:RU000384}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQW43973.1}.
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DR EMBL; LMDV01000013; KQW43973.1; -; Genomic_DNA.
DR RefSeq; WP_056158953.1; NZ_LMDV01000013.1.
DR AlphaFoldDB; A0A0Q7AWB5; -.
DR STRING; 1736439.ASC77_21505; -.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000051939; Unassembled WGS sequence.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
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 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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Reference proteome {ECO:0000313|Proteomes:UP000051939}.
FT DOMAIN 15..101
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 108..446
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 446 AA; 50157 MW; 0FACE6950BFFBF77 CRC64;
MGKQEDFVLR ALEERDVRFV RLWFTDVLGF LKSVAVAPAE LEQAFSEGIG FDGSSIEGFA
RVYESDMLAK PDPSTFQILP WRSGEGPSTA RMFCDIVMPD GSPSYADPRH VLKRTLSKAA
DKGFTFYTHP EIEFYLFKDV PEDGGPPVPA DRSGFFDHTA QSMGADFRRE AIGMLEQMGI
SVEFSHHEGG PGQQEIDLRY ADALSTADNI MTFRTVVREV ALTQGLWASF MPKPYTEHPG
SGMHTHVSLF EGDNNAFFAA GAEYQLSETG RRFIAGILKH ANEISCITNQ WVNSYKRMLW
GAEAPSYICW GHNNRSAMIR VPMYKPLKGQ STRVELRSLD AACNPYLAYA VVLAAGMKGI
EEGYELPREA EDDVWSLSER ERKSLGIDPL PRSLYDAINI AESSELLAET LGEQVFEFFL
RNKRAEWDDY RGQVSAFERE RMLPVI
//
