ID A0A0F2C913_9MICO Unreviewed; 451 AA.
AC A0A0F2C913;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Glutamine synthetase {ECO:0000313|EMBL:KJQ54409.1};
DE EC=6.3.1.2 {ECO:0000313|EMBL:KJQ54409.1};
GN Name=glnA_3 {ECO:0000313|EMBL:KJQ54409.1};
GN ORFNames=RS85_01561 {ECO:0000313|EMBL:KJQ54409.1};
OS Microbacterium sp. SA39.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1263625 {ECO:0000313|EMBL:KJQ54409.1, ECO:0000313|Proteomes:UP000033425};
RN [1] {ECO:0000313|EMBL:KJQ54409.1, ECO:0000313|Proteomes:UP000033425}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA39 {ECO:0000313|EMBL:KJQ54409.1,
RC ECO:0000313|Proteomes:UP000033425};
RA Corretto E., Antonielli L., Sessitsch A., Kidd P., Weyens N., Brader G.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KJQ54409.1}.
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DR EMBL; JXRU01000032; KJQ54409.1; -; Genomic_DNA.
DR RefSeq; WP_046012871.1; NZ_JXRU01000032.1.
DR AlphaFoldDB; A0A0F2C913; -.
DR STRING; 1263625.RS85_01561; -.
DR PATRIC; fig|1263625.4.peg.1568; -.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000033425; Unassembled WGS sequence.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:UniProtKB-EC.
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: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; PS51986; GS_BETA_GRASP; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:KJQ54409.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033425}.
FT DOMAIN 17..113
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 120..451
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 451 AA; 49690 MW; EDE3F7D5CDBB702A CRC64;
MSGNLSIDQL DAGIAAGEID TVIVAFADAQ GRLVGKRVSA RLFQEDILHH GAEACDYLLS
VDVDMNTVDG YAMSGWDRGY GDMVLRPDVE TLRRIPWLDG TALVIADLIW ANGEPVGPSP
RAILDRQRDR LAERGLTAFA GTELEFIVFE NTYRDAWARK YEGLTPATDY NVDYNLLAST
RMEPLLRDIR NGMDGAGLYC EGVKGECNLG QQEIAFRYAE VRETADQHAL YKNGAKEIAA
QHGQALTFMA KFNEREGNSC HIHLSLRADD GTPVMAGEGE HGFSPVMEHW IAGILATLRE
FTLLYAPNIN SYKRFAKGSF APTGVAWGID NRTCALRVIG KGSGLRVENR VPGGDVNPYL
GISAIIAGGL YGIENELPLP ERFTGNAYVD AVEHLPTTLR EAAQLFRESA IARAAFGDDV
VDHYLNQARI ELEAYDAVVT DWERIRGFER L
//
