ID A0A1I2Z6F2_9MICO Unreviewed; 445 AA.
AC A0A1I2Z6F2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Glutamine synthetase {ECO:0000313|EMBL:TFB82879.1};
GN ORFNames=E3O11_13640 {ECO:0000313|EMBL:TFB82879.1};
OS Cryobacterium levicorallinum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Cryobacterium.
OX NCBI_TaxID=995038 {ECO:0000313|EMBL:TFB82879.1, ECO:0000313|Proteomes:UP000297963};
RN [1] {ECO:0000313|EMBL:TFB82879.1, ECO:0000313|Proteomes:UP000297963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hh34 {ECO:0000313|EMBL:TFB82879.1,
RC ECO:0000313|Proteomes:UP000297963};
RA Liu Q., Xin Y.-H.;
RT "Genomics of glacier-inhabiting Cryobacterium strains.";
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
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}.
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:TFB82879.1}.
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DR EMBL; SOFE01000023; TFB82879.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2Z6F2; -.
DR STRING; 995038.SAMN05216274_103184; -.
DR Proteomes; UP000297963; Unassembled WGS sequence.
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; 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 Magnesium {ECO:0000256|ARBA:ARBA00022842}.
SQ SEQUENCE 445 AA; 49807 MW; 7F3AD2296BEF0999 CRC64;
MDKQRDFVLR TIEERGIKFV RLWFTDVVGT LKSVAIAPAE VEGAFNEGLG FDGSAIEGLT
RSFEADVLAH PDPTTFQILP WRGEVDPTAR MFCDITTPDG QPAVADPRNV LKRTLAKAAD
RGFTFYTHPE VEFYLLKSSK YGKNGPIPVD SAGYFDNVPG GTAHDFRRRS VRMLEDLGIS
VEFSHHEAGP GQNEIDLRYA DALTTADNIM TFRTVVKEVA IEQGVYATFM PKPMSEHPGS
GMHTHMSLFE GDANAFYEAG AKYQLSKIGR QFIAGLLKHA PEITAVTNQF VNSYKRLWGG
DEAPSFVCWG HNNRSALVRV PLYKPNKGQS ARVEYRAIDS AANPYLAYSL MLAAGLKGIE
EGYELPPEAE DNVWSLSDTE RRALGYTQLP ASLDHAIQFM EESELVAETL GEQVFNYVLL
NKRQEWRDYR SQVTPFELQK NLEML
//
