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Database: UniProt
Entry: A0A1H5T5F8_9ACTN
LinkDB: A0A1H5T5F8_9ACTN
Original site: A0A1H5T5F8_9ACTN 
ID   A0A1H5T5F8_9ACTN        Unreviewed;       453 AA.
AC   A0A1H5T5F8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=L-glutamine synthetase {ECO:0000313|EMBL:SEF58053.1};
GN   ORFNames=SAMN05216223_101399 {ECO:0000313|EMBL:SEF58053.1};
OS   Actinacidiphila yanglinensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Actinacidiphila.
OX   NCBI_TaxID=310779 {ECO:0000313|EMBL:SEF58053.1, ECO:0000313|Proteomes:UP000236754};
RN   [1] {ECO:0000313|EMBL:SEF58053.1, ECO:0000313|Proteomes:UP000236754}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.2023 {ECO:0000313|EMBL:SEF58053.1,
RC   ECO:0000313|Proteomes:UP000236754};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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|ARBA:ARBA00009897, ECO:0000256|PROSITE-ProRule:PRU01330,
CC       ECO:0000256|RuleBase:RU000384}.
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DR   EMBL; FNVU01000001; SEF58053.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H5T5F8; -.
DR   OrthoDB; 9807095at2; -.
DR   Proteomes; UP000236754; 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; 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   InterPro; IPR004809; Gln_synth_I.
DR   NCBIfam; TIGR00653; GlnA; 1.
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   ATP-binding {ECO:0000256|PIRSR:PIRSR604809-2};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR604809-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000236754}.
FT   DOMAIN          15..100
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS51986"
FT   DOMAIN          107..453
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51987"
FT   BINDING         182
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT   BINDING         245..247
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT   BINDING         296
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT   BINDING         310
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT   BINDING         322
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT   BINDING         322
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT   BINDING         344
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
SQ   SEQUENCE   453 AA;  50592 MW;  CAAE034517D5CA88 CRC64;
     MDKQQEFVLR TLEERDIRFV RLWFTDVLGY LKSVAVAPAE LEQAFDEGMG FDGSAIEGFA
     RVYESDMIAK PDPSTFQVLP WRAEAPGTAR MFCDILMPDG SPSYADPRYV LKRALAKTSD
     LGFTFYTHPE IEFFLLKDRP LDGSRPTPAD NSGYFDHTPQ NVGMDFRRQA ITMLESMGIS
     VEFSHHEGAP GQQEIDLRYA DALSTADNVM TFRLVMKQVA LEQGVQATFM PKPFSEYPGS
     GMHTHLSLFE GDRNAFYESG AEFQLSKVGR SFIAGLLRHA GETAAVTNQW VNSYKRIWGG
     SQRTAGAGGE APSYICWGHN NRSALIRVPM YKPGKTGSTR VEVRSLDAGA NPYLSYAVLL
     AAGMKGIQEG YELPAGADDD VWALSDSERR ALGIEPLPQN LGEAISLMER SELVAETLGE
     HVFDFFLRNK KQEWEEYRSQ VTPFELIKNL PVL
//
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