ID A0A1S2PYP1_9ACTN Unreviewed; 342 AA.
AC A0A1S2PYP1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=BIV24_06470 {ECO:0000313|EMBL:OIJ98014.1};
OS Streptomyces colonosanans.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1428652 {ECO:0000313|EMBL:OIJ98014.1, ECO:0000313|Proteomes:UP000179935};
RN [1] {ECO:0000313|EMBL:OIJ98014.1, ECO:0000313|Proteomes:UP000179935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC 93 {ECO:0000313|EMBL:OIJ98014.1,
RC ECO:0000313|Proteomes:UP000179935};
RA Lee L.-H., Ser H.-L., Law J.W.-F.;
RT "Genome sequence of Streptomyces sp. MUSC 93.";
RL Submitted (OCT-2016) 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:OIJ98014.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MLYP01000014; OIJ98014.1; -; Genomic_DNA.
DR RefSeq; WP_071365188.1; NZ_MLYP01000014.1.
DR AlphaFoldDB; A0A1S2PYP1; -.
DR STRING; 1428652.BIV24_06470; -.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000179935; 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: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; 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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000179935}.
FT DOMAIN 3..84
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 91..342
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 342 AA; 37229 MW; C19AC7F1F561BFFE CRC64;
MTFKAEYIWI DGTAPTAKLR SKTKILAGDA QGAQLPLWGF DGSSTNQAEG HFSDLVLKPV
FSCPDPIRGG GDILVMCEVL NTDMTPHRSN TRAALAEVAE KFAAQEPIFG IEQEYTFFDG
MRPLGFPEGG FPAPQGGYYC GVGADEIFGR DVVEAHLDNC LKAGLGISGI NAEVMPGQWE
FQVGPLSPLE VSDQLWVARW LLYRTAEDFN VSATLDPKPV KGDWNGAGAH TNFSTKAMRE
GYDAIITACE SLGEGSKPLD HVKNYGAGID DRLTGAHETA PWDEYSYGVA DRGASVRIPW
QVERDRKGYI EDRRPNANVD PYVVTRLLTD TCCAALEKAG QV
//
