ID A0A3D9SIS7_9ACTN Unreviewed; 337 AA.
AC A0A3D9SIS7;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=glutamine synthetase {ECO:0000256|ARBA:ARBA00012937};
DE EC=6.3.1.2 {ECO:0000256|ARBA:ARBA00012937};
DE AltName: Full=Glutamine synthetase II {ECO:0000256|ARBA:ARBA00043026};
GN ORFNames=DFJ69_1004 {ECO:0000313|EMBL:REE95607.1};
OS Thermomonospora umbrina.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Thermomonospora.
OX NCBI_TaxID=111806 {ECO:0000313|EMBL:REE95607.1, ECO:0000313|Proteomes:UP000256661};
RN [1] {ECO:0000313|EMBL:REE95607.1, ECO:0000313|Proteomes:UP000256661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43927 {ECO:0000313|EMBL:REE95607.1,
RC ECO:0000313|Proteomes:UP000256661};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the ATP-dependent biosynthesis of glutamine from
CC glutamate and ammonia. {ECO:0000256|ARBA:ARBA00003117}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine +
CC phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000777};
CC -!- SUBUNIT: Homooctamer and homotetramer. {ECO:0000256|ARBA:ARBA00038740}.
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:REE95607.1}.
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DR EMBL; QTTT01000001; REE95607.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D9SIS7; -.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000256661; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IPR048091; Gln_syn_GlnII.
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 NCBIfam; NF041605; gln_syn_GlnII; 1.
DR PANTHER; PTHR20852; GLUTAMINE SYNTHETASE; 1.
DR PANTHER; PTHR20852:SF57; GLUTAMINE SYNTHETASE 2 CYTOPLASMIC; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000256661}.
FT DOMAIN 3..81
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 88..337
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 337 AA; 36823 MW; E847EDABE69A09DD CRC64;
MSYKAEYIWI DGTEPTAMLR SKTRILADGA DLPTWGFDGS STNQAPGEHS DCVLKPVFSC
PDPIRGGDHK LVLCEVYLPD GTPHPTNTRA KLVPIAESFA EQESLFGIEQ EYTFFQAGRP
LGFPETGFPA PQGPYYCGVG ADEVFGREIV EQHLDACLAA GLPISGINAE VMPGQWEFQV
GPAGPLEVSD ALWVARWLLY RIAEEHNVAA TLDPKPAKGD WNGAGAHTNF STKAMRESYA
PIITAAESLG GRIKEHIAVY GYGIEERLTG LHETAPWTEF SYGVGDRGAS VRIPWQVEVD
QKGYMEDRRP NANCDPYEVT RLLVDTCCTA LKNAGQV
//
