ID A0A1B1U3W6_9HELI Unreviewed; 478 AA.
AC A0A1B1U3W6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Glutamine synthetase {ECO:0000256|ARBA:ARBA00021364};
DE EC=6.3.1.2 {ECO:0000256|ARBA:ARBA00012937};
DE AltName: Full=Glutamine synthetase I beta {ECO:0000256|ARBA:ARBA00033230};
GN ORFNames=BBW65_00840 {ECO:0000313|EMBL:ANV97448.1};
OS Helicobacter enhydrae.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=222136 {ECO:0000313|EMBL:ANV97448.1, ECO:0000313|Proteomes:UP000092884};
RN [1] {ECO:0000313|Proteomes:UP000092884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 01-6242 {ECO:0000313|Proteomes:UP000092884};
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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; CP016503; ANV97448.1; -; Genomic_DNA.
DR RefSeq; WP_066338463.1; NZ_CP016503.1.
DR AlphaFoldDB; A0A1B1U3W6; -.
DR STRING; 222136.BBW65_00840; -.
DR KEGG; het:BBW65_00840; -.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000092884; Chromosome.
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: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 InterPro; IPR004809; Gln_synth_I.
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; 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 Ligase {ECO:0000313|EMBL:ANV97448.1};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR604809-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000092884}.
FT DOMAIN 20..104
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 112..478
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
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 328
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 334
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 346
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 346
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 366
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
SQ SEQUENCE 478 AA; 54334 MW; A02A679B500CBBA9 CRC64;
MQGVVMQDQI KTFFNFCREN EVEFVDFRFT DIKGTWHHIS FSLSAIDEET FTKGVPFDAS
SFHKWQPIHR SDMLLLPDLV RYFIDPFTAD VTVVVFCDVW DIYKNQPYEK CPRSIVKRAM
QYLQESGIGD VAYFGPENEF FVFDSIKITD TINSQAYSVD TQEGEWNRNT EFEGVNNGHR
PGTKGGYFPV PPIDSMVDLR AEMVKVLNLV GIETFVVHHE VGQAQGEIGI KFGDMLEAAD
NVQKLKYVVK MVAHLNGKTA TFMPKPLYGD NGSGMHTHIS IWKDSKNLFA GDEYQGLSTM
AMHFLGGVLH HARSIAAFTN ASTNSYKRLI PGFEAPSILA YSAQNRSASI RIPYSQGNSA
KRLEFRFPDS SSNPYLAFSS LLMAGLDGIT QKISAGEPMD IDLFELTLDE IREKGIKQLP
HTLRSAIEEM LLDREYLKVG NVFSEEFLQT YKAYKFEAEI WTWEARPHPF EFISTYSC
//
