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Database: UniProt
Entry: A0A3M2L084_9NOCA
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ID   A0A3M2L084_9NOCA        Unreviewed;       478 AA.
AC   A0A3M2L084;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Glutamine synthetase {ECO:0000256|ARBA:ARBA00021364, ECO:0000256|RuleBase:RU004356};
DE            EC=6.3.1.2 {ECO:0000256|ARBA:ARBA00012937, ECO:0000256|RuleBase:RU004356};
GN   Name=glnA {ECO:0000313|EMBL:RMI27968.1};
GN   ORFNames=EBN03_31960 {ECO:0000313|EMBL:RMI27968.1};
OS   Nocardia stercoris.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=2483361 {ECO:0000313|EMBL:RMI27968.1, ECO:0000313|Proteomes:UP000279275};
RN   [1] {ECO:0000313|EMBL:RMI27968.1, ECO:0000313|Proteomes:UP000279275}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEAU-LL90 {ECO:0000313|EMBL:RMI27968.1,
RC   ECO:0000313|Proteomes:UP000279275};
RA   Ling L.;
RT   "Isolation from cow dung.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine +
CC         phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000777,
CC         ECO:0000256|RuleBase:RU004356};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two hexagons.
CC       {ECO:0000256|ARBA:ARBA00011354, ECO:0000256|RuleBase:RU000387}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|RuleBase:RU000387}.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC       {ECO:0000256|ARBA:ARBA00009897, ECO:0000256|PROSITE-ProRule:PRU01330,
CC       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:RMI27968.1}.
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DR   EMBL; RFFH01000027; RMI27968.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M2L084; -.
DR   OrthoDB; 9807095at2; -.
DR   Proteomes; UP000279275; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   InterPro; IPR027303; Gln_synth_gly_rich_site.
DR   InterPro; IPR004809; Gln_synth_I.
DR   InterPro; IPR001637; Gln_synth_I_adenylation_site.
DR   InterPro; IPR027302; Gln_synth_N_conserv_site.
DR   NCBIfam; TIGR00653; GlnA; 1.
DR   PANTHER; PTHR43407; GLUTAMINE SYNTHETASE; 1.
DR   PANTHER; PTHR43407:SF1; LENGSIN; 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; PS00180; GLNA_1; 1.
DR   PROSITE; PS00182; GLNA_ADENYLATION; 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   ECO:0000256|RuleBase:RU004356}; Cytoplasm {ECO:0000256|RuleBase:RU000387};
KW   Ligase {ECO:0000256|RuleBase:RU004356, ECO:0000313|EMBL:RMI27968.1};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR604809-2,
KW   ECO:0000256|RuleBase:RU004356};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553,
KW   ECO:0000256|PIRSR:PIRSR604809-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000279275}.
FT   DOMAIN          16..100
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS51986"
FT   DOMAIN          108..478
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51987"
FT   BINDING         214
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT   BINDING         230..232
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT   BINDING         271..272
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT   BINDING         278..280
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT   BINDING         329
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT   BINDING         335
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT   BINDING         347
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT   BINDING         347
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT   BINDING         361
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT   BINDING         368
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT   MOD_RES         406
FT                   /note="O-AMP-tyrosine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-50"
SQ   SEQUENCE   478 AA;  53566 MW;  1CE69CE144779EBA CRC64;
     MAFSTADEVI KYIKEEELEY VDVRFTDLPG VQQHFSIPAK AFTADLAEEG LAFDGSSVRG
     FQSIDESDML LLPDFSTARI DPFRAAKTLN LNFFVHDPFT REAYSRDPRN IARKAEEYLR
     STGIADTAYF GPEAEFYIFD SVRYDSQMNG AFYEVDSISG SWNTGVEFNA DGTPNRGYKV
     RPKGGYFPVA PYDHYVDLRD KMSTNLQNAG FELERGHHEV GTAGQAEINY RFNTLLSAAD
     DLQLFKYIIK NTAWAEGKSV TFMPKPLFGD NGSGMHVHQS LWKDGVPLFH DEAGYGGLSD
     LARWYIGGIL HHAPSLLAFT NPTVNSYHRL VPGYEAPINL VYSQRNRSAA VRIPVTGSNP
     KAKRIEFRAP DSSGNPYLAF SAMLMAGLDG IKKKIEPAAP VDKDLYELPP EEAKNIQQAP
     TSLASVIDRL EADHDYLTEG GVFTPDLIET WISIKREQEI APINLRPHPY EFSLYYDV
//
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