ID E2Q1S4_STRCL Unreviewed; 455 AA.
AC E2Q1S4;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Glutamine synthetase {ECO:0000313|EMBL:EFG06550.1};
DE EC=6.3.1.2 {ECO:0000313|EMBL:EFG06550.1};
GN ORFNames=SCLAV_1473 {ECO:0000313|EMBL:EFG06550.1};
OS Streptomyces clavuligerus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1901 {ECO:0000313|EMBL:EFG06550.1, ECO:0000313|Proteomes:UP000002357};
RN [1] {ECO:0000313|EMBL:EFG06550.1, ECO:0000313|Proteomes:UP000002357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 /
RC NRRL 3585 / VKM Ac-602 {ECO:0000313|Proteomes:UP000002357};
RX PubMed=20624727; DOI=10.1093/gbe/evq013;
RA Medema M.H., Trefzer A., Kovalchuk A., van den Berg M., Mueller U.,
RA Heijne W., Wu L., Alam M.T., Ronning C.M., Nierman W.C., Bovenberg R.A.L.,
RA Breitling R., Takano E.;
RT "The sequence of a 1.8-mb bacterial linear plasmid reveals a rich
RT evolutionary reservoir of secondary metabolic pathways.";
RL Genome Biol. Evol. 2:212-224(2010).
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}.
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DR EMBL; CM000913; EFG06550.1; -; Genomic_DNA.
DR AlphaFoldDB; E2Q1S4; -.
DR STRING; 1901.BB341_20815; -.
DR eggNOG; COG0174; Bacteria.
DR Proteomes; UP000002357; 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 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 Ligase {ECO:0000313|EMBL:EFG06550.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002357}.
FT DOMAIN 17..102
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 109..455
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 455 AA; 50763 MW; D78974CC3AAD0AB7 CRC64;
MEMDKQQEFV LRTLEERDIR FVRLWFTDVL GFLKSVAVAP AELEQAFDEG IGFDGSAIEG
FARVYESDMI AKPDPGTFQI LPWRAEAPGT ARMFCDILMP DGSPSFADPR YVLKRGLAKA
SDLGFTFYTH PEIEFFLLKD KPLDGSRPVP ADNSGYFDHT PQNVGMDFRR QAITMLESMG
ISVEFSHHEG APGQQEIDLR YADALSTADN IMTFRLVMKQ VALEQGVQAT FMPKPFSEYP
GSGMHTHLSL FEGDRNAFYE SGAEYQLSKV GRSFIAGLLR HAAEISAVTN QWVNSYKRIW
GGSARSAGAG GEAPSYICWG HNNRSALIRV PMYKPGKTGS SRVEMRSIDS GANPYLTYAV
LLAAGLKGIE QGYELPAGAD DDVWALSDAE RRAMGIEPLP QNLGEAISLM ERSELVAETL
GEHVFDFFLR NKKQEWEEYR SEVTAFELRK NLPVL
//
