ID A0A0U3Q300_9ACTN Unreviewed; 501 AA.
AC A0A0U3Q300;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Glutamine synthetase {ECO:0000313|EMBL:ALV30884.1};
GN ORFNames=AS200_01365 {ECO:0000313|EMBL:ALV30884.1};
OS Streptomyces sp. CdTB01.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1725411 {ECO:0000313|EMBL:ALV30884.1, ECO:0000313|Proteomes:UP000068029};
RN [1] {ECO:0000313|EMBL:ALV30884.1, ECO:0000313|Proteomes:UP000068029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CdTB01 {ECO:0000313|EMBL:ALV30884.1,
RC ECO:0000313|Proteomes:UP000068029};
RA Tian Y., Zhou G., Yang H., Lu X.;
RT "Complete genome sequence of the Streptomyces sp. strain CdTB01, a
RT bacterium tolerant to cadmium.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|PROSITE-ProRule:PRU01330, ECO:0000256|RuleBase:RU000384}.
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DR EMBL; CP013743; ALV30884.1; -; Genomic_DNA.
DR RefSeq; WP_058920572.1; NZ_CP013743.1.
DR AlphaFoldDB; A0A0U3Q300; -.
DR STRING; 1725411.AS200_01365; -.
DR KEGG; scx:AS200_01365; -.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000068029; Chromosome.
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:SF12; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE PUUA; 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:UP000068029}.
FT DOMAIN 43..144
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 151..501
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 501 AA; 53617 MW; F202B088F750E9A2 CRC64;
MYVRSWSSPA AQGSVGRPSF VADHALWDDA RTAAAERIEA SLADIDLVRL VFGDPHGLAR
SKTLTAEAFR SVLRNGMNFS PGPFVFDTGH AVAVDFLGEH GIGVDEIAGA GNFILVPDPL
TFQLLPGGDA RTAWVIGDEY LRDGTPHPLS SRAVLRRVAA SYTARRLAPV VGLEVEWYLT
RRLDDEPGNT GNGFGLQGQA PRVQAVNAGY QFNLDAHYDI LAPLTDPLAL HLLALGLPLR
SMEHESGPGQ VETTFSPMSA LDAADAMLLF RTTVKNWCAR RGHHASFMSK PLLDAADPSG
WHLNQSVTDL TAHTNLFAAE GPSGGLSPQG KAYAEGLLSH ARELCLLSVP TVNGYRRLAA
EHTLAPTRLG VSQEDRSALL RLVGHGTGAH IENRIGEPCA NPYLTIAAQL FAGLEGLTAP
AAPADTTAEA GGPGLVPQHL REALTAFRAG RAARLLGEPL AACLAKLKDS ELRRYEAWSL
QTAPAPGQVT DWEQREYFGA Y
//
