ID A0A2A3HT81_9ACTN Unreviewed; 452 AA.
AC A0A2A3HT81;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Glutamine synthetase {ECO:0000313|EMBL:PBC70991.1};
GN ORFNames=BX265_5556 {ECO:0000313|EMBL:PBC70991.1};
OS Streptomyces sp. TLI_235.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1938860 {ECO:0000313|EMBL:PBC70991.1, ECO:0000313|Proteomes:UP000218662};
RN [1] {ECO:0000313|EMBL:PBC70991.1, ECO:0000313|Proteomes:UP000218662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TLI_235 {ECO:0000313|EMBL:PBC70991.1,
RC ECO:0000313|Proteomes:UP000218662};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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:PBC70991.1}.
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DR EMBL; NSGV01000002; PBC70991.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3HT81; -.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000218662; Unassembled WGS sequence.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
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 PANTHER; PTHR43785; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE; 1.
DR PANTHER; PTHR43785:SF16; GLUTAMINE SYNTHETASE GLNA4 (GLUTAMINE SYNTHASE) (GS-II)-RELATED; 1.
DR Pfam; PF00120; Gln-synt_C; 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; PS51986; GS_BETA_GRASP; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000218662}.
FT DOMAIN 18..114
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 121..452
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 452 AA; 49535 MW; 921CFA0C99B683E7 CRC64;
MSSPRLTLDR LRELVADGSV DTVVLAMTDM QGRLQGKRLA AEYFLSDVVP GAAEGCGYLL
AVDTDMNTVD GYAISSWESG YGDLVLTPDL ATLRTVPWHP ATAMVQCDVH HHDGRPVTVS
PRQVLRRQLE RLAGYGWQAY AGTELEFILF RDTYEQAWER AYHGLTPANQ YNVDYSILGT
SRVEPLLRRL RNEMAGAGLT VESAKGECNL GQHEIAFKYA DALTTCDNHA VYKTGAKEIA
AQEGCSLTFM AKYDEREGNS CHIHLSLRDA AGAPVMAGDG PHGFSRTMEH FLAGQLACLS
EFALLLAPTV NSYKRYVPGS FAPTAIAWGR DNRTCALRVV GHGPSLRFEN RVPGGDVNPY
LAVAALIAAG LYGIEHQLEL EPEFTGNAYA SDAPRVPSTL RDAVDAFEAS EAATEAFGKD
VVRHYAHAGR TELAAYDRAV TDWERRRGFE RL
//
