ID A0A4R4PXQ7_9ACTN Unreviewed; 447 AA.
AC A0A4R4PXQ7;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Glutamine synthetase {ECO:0000313|EMBL:TDC27307.1};
GN ORFNames=E1265_02115 {ECO:0000313|EMBL:TDC27307.1};
OS Streptomyces sp. 8K308.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2530388 {ECO:0000313|EMBL:TDC27307.1, ECO:0000313|Proteomes:UP000294502};
RN [1] {ECO:0000313|EMBL:TDC27307.1, ECO:0000313|Proteomes:UP000294502}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8K308 {ECO:0000313|EMBL:TDC27307.1,
RC ECO:0000313|Proteomes:UP000294502};
RA Sahin N., Ay H., Saygin H.;
RT "Draft genome sequences of novel Actinobacteria.";
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|PROSITE-ProRule:PRU01331, 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:TDC27307.1}.
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DR EMBL; SMKC01000006; TDC27307.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R4PXQ7; -.
DR OrthoDB; 3277468at2; -.
DR Proteomes; UP000294502; 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:SF12; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE PUUA; 1.
DR Pfam; PF00120; Gln-synt_C; 1.
DR Pfam; PF16952; Gln-synt_N_2; 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; 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:UP000294502}.
FT DOMAIN 113..447
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 447 AA; 47411 MW; 7905FF70BFC5E184 CRC64;
MEPEQQLMQR LNAAKVSAVA LTWVDNAGLT RVKAVPVSRL AEAVRRGVGM SPVFDVFLVD
DSITSSPRIG GPDGDLRLVP DLDRLTVLAA QPGWAWAPAD RYEQTRAPYA ACQRRFVRRQ
AERALAEHGL ELRMGFETEW VVTRPGDLGD ARVPAGGAGP AYGMSRLVES SDYLRDLAEA
FAAQGLPLLQ LHPEYSPGQF EISARPAAPV TAADDAVLVR ETVRAVSQRH GLAASFAPVV
DTAGLGNGRH LHLSLWRGGK NACRDGDGPF GMSAVCEAFL AGVLRELPAL LAIGAPSPAS
YLRLRPSVWA GAFQCWGLEN REAAVRFVTG APDDQDAANA EIKCFDGAAN PYLVTGAVIA
AGLAGVADGL TLPQPVAGDP AERRVAPPPR LPESLPAALD HLESATVLRT ALGEELYGAI
LAVRQGEVAL FATATPEEIA AATRERY
//