ID A0A2V4MSY7_9ACTN Unreviewed; 452 AA.
AC A0A2V4MSY7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Glutamine synthetase {ECO:0000313|EMBL:PYC66287.1};
GN ORFNames=C7C46_31560 {ECO:0000313|EMBL:PYC66287.1};
OS Streptomyces tateyamensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=565073 {ECO:0000313|EMBL:PYC66287.1, ECO:0000313|Proteomes:UP000248039};
RN [1] {ECO:0000313|EMBL:PYC66287.1, ECO:0000313|Proteomes:UP000248039}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 21389 {ECO:0000313|EMBL:PYC66287.1,
RC ECO:0000313|Proteomes:UP000248039};
RA Schwalen C.J., Hudson G.A., Mitchell D.A.;
RT "Bioinformatic expansion and discovery of thiopeptide antibiotics.";
RL Submitted (MAR-2018) 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:PYC66287.1}.
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DR EMBL; PYBW01000181; PYC66287.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V4MSY7; -.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000248039; 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; 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:SF16; GLUTAMINE SYNTHETASE GLNA4 (GLUTAMINE SYNTHASE) (GS-II)-RELATED; 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; 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:UP000248039}.
FT DOMAIN 121..452
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 452 AA; 49482 MW; 889B6B4C0DAE32AD CRC64;
MSGSRLTLDQ LRAQVAEGTI DTVVLAVTDM QGRLQGKRLA ADYFLTDVVE NAAEGCGYLL
AVDVEMNTVE GYQVSSWESG YGDLVMVPDL ATLRRVPWHP ATAMVQCDLA RHDGAPVAVS
PRQVLRRQLD RLAEHGWQAY VGTELEFIVF KDSYEQAWDK DYRGLTPVNQ YNVDYSILGT
GRIEPLLRRL RNEMAGAGLT VESAKGECNL GQHEIAFKYA EALVSCDDHV VYKTGAKEIA
AQDGVSLTFM AKYNEREGNS CHIHLSLRAA DGAPVFAGDL QHGFSRTMEH FLAGQLACLR
EFSLLLAPTV NSYKRYVAGS FAPTAVAWGR DNRTCALRVV GHGSSLRFEN RVPGGDVNPY
LAVAALIAAG LHGIEQGLEL EPEFTGNAYT SDAPRVPSTL RDAVALFEAS EVAAAAFGKE
VVHHYTHAGR VELAAFDAAV TDWERRRGFE RL
//
