ID R9KW19_9FIRM Unreviewed; 703 AA.
AC R9KW19;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Glutamine synthetase {ECO:0000256|ARBA:ARBA00021364};
GN ORFNames=C809_01333 {ECO:0000313|EMBL:EOS50483.1};
OS Lachnospiraceae bacterium MD335.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1235793 {ECO:0000313|EMBL:EOS50483.1, ECO:0000313|Proteomes:UP000014081};
RN [1] {ECO:0000313|EMBL:EOS50483.1, ECO:0000313|Proteomes:UP000014081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COE1 {ECO:0000313|EMBL:EOS50483.1,
RC ECO:0000313|Proteomes:UP000014081};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium COE1.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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:EOS50483.1}.
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DR EMBL; ASSW01000019; EOS50483.1; -; Genomic_DNA.
DR AlphaFoldDB; R9KW19; -.
DR STRING; 1235793.C809_01333; -.
DR PATRIC; fig|1235793.3.peg.1380; -.
DR eggNOG; COG3968; Bacteria.
DR HOGENOM; CLU_024307_0_0_9; -.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000014081; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000014081}.
FT DOMAIN 65..159
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 164..595
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
FT COILED 627..657
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 703 AA; 77767 MW; 795834DB55947A5F CRC64;
MSELLNVESI FGQKVFTITK MKERLPKKVF QEVKRVMDQG GELSMATADV VAKAMKDWAV
ENGATHYTHW FQPLTGITAE KHDSFVSHPD DDGKMLMEFS GKELIKGEPD ASSFPSGGLR
ATFEARGYTA WDITSPAFLK ESGCGTILCI PTAFCSYTGE ALDKKTPLLR SMEALSEQAL
RIVRLFGDTE ATKVTASVGP EQEYFLVDKD LYMQRKDLMF AGRTLFGALP PKGQEMEDHY
FGVIKERVGA YMKDLNVELW KLGVTAKTQH NEVAPAQHEL APIYETANIA VDHNQLVMET
MKRVAYKHDL RCLLHEKPYK GVNGSGKHDN WSITTDSGVN LLEPGNTPNK NVRFLLVLAC
IMKAVDTHAD LLRQSASDVG NDHRLGANEA PPAIISIFLG DQLEDVVRQL VETGDAAKIK
KGGKLETGVS TLPDFEKDAT DRNRTSPFAF TGNKFEFRMV GSADSIASPN TTLNAIVAEA
FCEAADRIES ADDKEMAIHD LIKEYMTKHQ RIIFNGNGYS EEWVAEAKRR GLPNIKSMVE
AASTLTTKKA VDLFEKFNIF TKVELESREE IIYETYAKTI NIEALTMIDM AGKDILPAVA
SYAGDLANSI IAVKEAGATA AAQIEVLNEV DGLLAEAKKA LNTLKEVEAK ASSMEDVKAQ
AFYYKDTVRE AMDALREPVD KLEMIVDGTI WPIPTYGDLM FEV
//