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Database: UniProt
Entry: A0A1V4H7T9_9BACL
LinkDB: A0A1V4H7T9_9BACL
Original site: A0A1V4H7T9_9BACL 
ID   A0A1V4H7T9_9BACL        Unreviewed;       446 AA.
AC   A0A1V4H7T9;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Glutamine synthetase {ECO:0000256|ARBA:ARBA00021364, ECO:0000256|RuleBase:RU004356};
DE            EC=6.3.1.2 {ECO:0000256|RuleBase:RU004356};
GN   ORFNames=BC351_11955 {ECO:0000313|EMBL:OPH47211.1};
OS   Paenibacillus ferrarius.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1469647 {ECO:0000313|EMBL:OPH47211.1, ECO:0000313|Proteomes:UP000190626};
RN   [1] {ECO:0000313|Proteomes:UP000190626}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CY1 {ECO:0000313|Proteomes:UP000190626};
RA   Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL   Submitted (JUL-2016) 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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:OPH47211.1}.
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DR   EMBL; MBTG01000066; OPH47211.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V4H7T9; -.
DR   STRING; 1469647.BC351_11955; -.
DR   OrthoDB; 9807095at2; -.
DR   Proteomes; UP000190626; Unassembled WGS sequence.
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; IPR027302; Gln_synth_N_conserv_site.
DR   NCBIfam; TIGR00653; GlnA; 1.
DR   PANTHER; PTHR43785; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE; 1.
DR   PANTHER; PTHR43785:SF12; TYPE-1 GLUTAMINE SYNTHETASE 2; 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; 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|ARBA:ARBA00022490};
KW   Ligase {ECO:0000256|RuleBase:RU004356, ECO:0000313|EMBL:OPH47211.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR604809-2,
KW   ECO:0000256|RuleBase:RU004356};
KW   Phosphoprotein {ECO:0000256|PIRSR:PIRSR604809-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190626}.
FT   DOMAIN          19..103
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS51986"
FT   DOMAIN          110..446
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51987"
FT   BINDING         186
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT   BINDING         201..203
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT   BINDING         242..243
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT   BINDING         249..251
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT   BINDING         300
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT   BINDING         306
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT   BINDING         318
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT   BINDING         318
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT   BINDING         337
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT   MOD_RES         375
FT                   /note="O-AMP-tyrosine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-50"
SQ   SEQUENCE   446 AA;  50756 MW;  BC5F299B5275C7E7 CRC64;
     MSYNDNYTKE DILRIAKEEN VRFIRLQFTD LMGSIKNVEI PFSQLEKALD NKMMFDGSSI
     EGYVRIEESD MYLYPDLDTW VIFPWVTESK VARLICDIYM PDGSPFAGDP RAILKNALKQ
     AEEMGYTAMN VGPEPEFFLF KTDEKGNPTT ELNDQGGYFD LAPMDLGENC RRDIVLTLEE
     MGFEIEASHH EVAPGQHEID FKYADAIKAA DQIQTFKLVV KTVARQHGLH ATFMPKPLFG
     MNGSGMHCHQ SLFKDDVNAF YDENDKLGLS TVARQYMAGV LRHARSFAAI TNPTVNSYKR
     LVPGYEAPCY VAWSASNRSP MIRIPASRGL STRVEVRNPD PAANPYLALA VMLAAGLDGI
     KNKMQLPPPT DRNIYVMSEE ERESQGIPSL PLDLKQALDE LLRDDVICDT LGEHALAHFY
     ELKEIEWDMY RTQVHQWERD QYLSLY
//
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