ID A0A4Q7VEX3_9BURK Unreviewed; 455 AA.
AC A0A4Q7VEX3;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 10.
DE SubName: Full=L-glutamine synthetase {ECO:0000313|EMBL:RZT93822.1};
GN ORFNames=EV670_3378 {ECO:0000313|EMBL:RZT93822.1};
OS Rivibacter subsaxonicus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rivibacter.
OX NCBI_TaxID=457575 {ECO:0000313|EMBL:RZT93822.1, ECO:0000313|Proteomes:UP000293671};
RN [1] {ECO:0000313|EMBL:RZT93822.1, ECO:0000313|Proteomes:UP000293671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19570 {ECO:0000313|EMBL:RZT93822.1,
RC ECO:0000313|Proteomes:UP000293671};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (FEB-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:RZT93822.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; SHKP01000008; RZT93822.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Q7VEX3; -.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000293671; 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:SF3; GLN-SYNT_C DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00120; Gln-synt_C; 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:UP000293671}.
FT DOMAIN 19..114
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 121..455
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 455 AA; 50879 MW; 6617205719C3C800 CRC64;
MVVRDNFTFS ELENWLNENR VTEIECLVPD LTGVARGKIL PRVKFTEDRG MRLPEATVAM
GVTGEFPEEG PYYDVISPND MDMHLQADPS TVRIVPWATD PTAQVLHDCY DRNGKLVPFA
PRSVLRRICG LFDAEGWDPV VAPELEFYLV ARNTDPNQPL QPPIGRSGRA ETSRQAYSID
AVNEFDPLFE DVYEYCEKMG LNVDTLIHEI GAGQMEINFF HAAPLGLADE VFFFKRTLRE
AAMRHGMFAT FMAKPIAGEP GSAMHVHQSV VSKLTGKNIF SNPDGTPSKE FFWYIGGLQK
HIPSAMAIFA PYVNSYRRLA RNTAAPINIQ WGTDNRTVGI RSPVAGPEAR RIENRVIGAD
ANPYVALAAT LACGYLGIKN RIEPSAECKG DAYLGEYQLP RSLGEALDLL RADKELASVL
GEEFVTVYTE VKEIEYSEFM TVISPWEREH LLLHV
//
