ID A4CMG4_ROBBH Unreviewed; 752 AA.
AC A4CMG4;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Glutamine synthetase {ECO:0000313|EMBL:EAR14856.1};
GN OrderedLocusNames=RB2501_11037 {ECO:0000313|EMBL:EAR14856.1};
OS Robiginitalea biformata (strain ATCC BAA-864 / HTCC2501 / KCTC 12146).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Robiginitalea.
OX NCBI_TaxID=313596 {ECO:0000313|EMBL:EAR14856.1, ECO:0000313|Proteomes:UP000009049};
RN [1] {ECO:0000313|EMBL:EAR14856.1, ECO:0000313|Proteomes:UP000009049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-864 / HTCC2501 / KCTC 12146
RC {ECO:0000313|Proteomes:UP000009049};
RX PubMed=19767438; DOI=10.1128/JB.01191-09;
RA Oh H.M., Giovannoni S.J., Lee K., Ferriera S., Johnson J., Cho J.C.;
RT "Complete genome sequence of Robiginitalea biformata HTCC2501.";
RL J. Bacteriol. 191:7144-7145(2009).
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|PROSITE-ProRule:PRU01330, ECO:0000256|RuleBase:RU000384}.
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DR EMBL; CP001712; EAR14856.1; -; Genomic_DNA.
DR AlphaFoldDB; A4CMG4; -.
DR STRING; 313596.RB2501_11037; -.
DR KEGG; rbi:RB2501_11037; -.
DR eggNOG; COG3968; Bacteria.
DR HOGENOM; CLU_024307_0_0_10; -.
DR Proteomes; UP000009049; Chromosome.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR Gene3D; 1.20.120.1560; -; 1.
DR Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR InterPro; IPR040577; Gln-synt_C.
DR InterPro; IPR008147; Gln_synt_N.
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; IPR022147; GSIII_N.
DR PANTHER; PTHR42974; GLUTAMINE SYNTHETASE; 1.
DR PANTHER; PTHR42974:SF1; TYPE-3 GLUTAMINE SYNTHETASE; 1.
DR Pfam; PF00120; Gln-synt_C; 1.
DR Pfam; PF18318; Gln-synt_C-ter; 1.
DR Pfam; PF12437; GSIII_N; 1.
DR SMART; SM01230; Gln-synt_C; 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 Reference proteome {ECO:0000313|Proteomes:UP000009049}.
FT DOMAIN 108..197
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 202..639
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 752 AA; 84648 MW; 765FF98776843B20 CRC64;
MGDIEKNGIF NENYTNCVIL PATQKPRAMN HKNTGPRETG YHQEYRAERR SETFAKHVFN
EDRMLQYLTR EAFASVKGAI FSGSKIDRKI ADQVAEAMKA WAIAAGATHY THWFQPLTGA
TAEKHDAFFD LLPDGRAIEK FGGGQLVQQE PDASSFPSGG IRNTFEARGY TAWDPTSPAF
IYGSTLCIPT IFVSYTGEAL DNKAPLLRAL HAVDEAATGV ARYFDKNVSK VNATLGWEQE
YFLIDAELAR SRPDIILAGR TLIGQAAAKG QQLDDHYFGV IPDRAFRFMR DLEAECMVLG
IPVKTRHNEV APNQYELAPV FEEANLAVDH NLLLMDVMDK VAVRHGLRVL FHEKPFAGIN
GSGKHNNWSL STDTGTNLLS PGSTPMKNLQ FLTFFVNTIK AVDRYEELLR ASIASASNDH
RLGANEAPPA IMSIFVGKQL TDVLDELEGV SKGKLSPEEK TELKLNVVGK IPEILLDNTD
RNRTSPFAFT GNKFEMRGVG AKTNCAKPMT VLNTIVAHQL REFKSEVDKL ITKKKLKKDE
AIFNVLREYI KSSKRIRFDG DGYSEQWQKE AERRKLSNNR NTPEALQVLT APESLELFRT
MGVFTEKEVR ARKEVELETY ILQTQIEGRV LSELVYNKVI PATVAYQNSL LRNIAGLKDV
YGAAHKTMAE AQLGILEHLA EHLQAIRKKT DAMNEARKRA NGMKDIEKKA RAYCESVLPY
FDEIRYHADR LERMVSDTEW PLAKYRDLLF IK
//
