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Database: UniProt
Entry: A0A5C8IAN4_9MICO
LinkDB: A0A5C8IAN4_9MICO
Original site: A0A5C8IAN4_9MICO 
ID   A0A5C8IAN4_9MICO        Unreviewed;       445 AA.
AC   A0A5C8IAN4;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Glutamine synthetase {ECO:0000313|EMBL:TXK17465.1};
GN   ORFNames=FVQ89_11600 {ECO:0000313|EMBL:TXK17465.1};
OS   Homoserinibacter sp. GY 40078.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Homoserinibacter.
OX   NCBI_TaxID=2603275 {ECO:0000313|EMBL:TXK17465.1, ECO:0000313|Proteomes:UP000321701};
RN   [1] {ECO:0000313|EMBL:TXK17465.1, ECO:0000313|Proteomes:UP000321701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GY 40078 {ECO:0000313|EMBL:TXK17465.1,
RC   ECO:0000313|Proteomes:UP000321701};
RA   Shi S.;
RL   Submitted (AUG-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:TXK17465.1}.
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DR   EMBL; VRTZ01000002; TXK17465.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5C8IAN4; -.
DR   OrthoDB; 9807095at2; -.
DR   Proteomes; UP000321701; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000321701}.
FT   DOMAIN          15..100
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS51986"
FT   DOMAIN          107..445
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51987"
SQ   SEQUENCE   445 AA;  49119 MW;  EC39FEED57DA967C CRC64;
     MDKQRDFVLR TIEERGVKFV RLWFTDVVGT LKSVALAPAE VEGAFSEGVG IDGSAIEGLT
     RASEADVLAH PDPTTFQILP WRGEVDPTAR MFCDITTPDG QPAVADPRNV LKRTLAKAAD
     RGFTFYTHPE IEFYLLQSSK LKNGRPVPVD SAGYFDNVPG GTAHDFRRRS VRMLEDLGIS
     VEFSHHEAGP GQNEIDLRYA DALTTADNIM TFRTVVKEVA IEQGSYATFM PKPFSEHPGS
     GMHTHVSLFE GDANAFFDAG NEYQLSQIGR QFVAGLLRHA PEITAVTNQF VNSYKRLWGG
     DEAPSYVTWG HNNRSALVRV PLYKPGKGQS ARVEYRAIDS AANPYLSFSL ILAAGLKGIE
     EGYELPAEAD ADVFDMSGAE RRALGYGALP SSLDRALLIM EESELVAETL GEQVFNYVLL
     NKRREWAGYR SQVTPFELEA NLEAL
//
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