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Database: UniProt
Entry: A0A4Q2K8L9_9FIRM
LinkDB: A0A4Q2K8L9_9FIRM
Original site: A0A4Q2K8L9_9FIRM 
ID   A0A4Q2K8L9_9FIRM        Unreviewed;       693 AA.
AC   A0A4Q2K8L9;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   RecName: Full=Glutamine synthetase {ECO:0000256|ARBA:ARBA00021364};
GN   ORFNames=ESZ91_09415 {ECO:0000313|EMBL:RXZ58264.1};
OS   Candidatus Borkfalkia ceftriaxoniphila.
OC   Bacteria; Bacillota; Clostridia; Candidatus Borkfalkiales;
OC   Candidatus Borkfalkiaceae; Candidatus Borkfalkia.
OX   NCBI_TaxID=2508949 {ECO:0000313|EMBL:RXZ58264.1, ECO:0000313|Proteomes:UP000291269};
RN   [1] {ECO:0000313|EMBL:RXZ58264.1, ECO:0000313|Proteomes:UP000291269}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HDS1380 {ECO:0000313|EMBL:RXZ58264.1,
RC   ECO:0000313|Proteomes:UP000291269};
RX   PubMed=30658995;
RA   Hildebrand F., Moitinho-Silva L., Blasche S., Jahn M.T., Gossmann T.I.,
RA   Heuerta-Cepas J., Hercog R., Luetge M., Bahram M., Pryszlak A., Alves R.J.,
RA   Waszak S.M., Zhu A., Ye L., Costea P.I., Aalvink S., Belzer C.,
RA   Forslund S.K., Sunagawa S., Hentschel U., Merten C., Patil K.R., Benes V.,
RA   Bork P.;
RT   "Antibiotics-induced monodominance of a novel gut bacterial order.";
RL   Gut 68:1781-1790(2019).
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:RXZ58264.1}.
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DR   EMBL; SDOZ01000003; RXZ58264.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4Q2K8L9; -.
DR   OrthoDB; 9807095at2; -.
DR   Proteomes; UP000291269; 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   Reference proteome {ECO:0000313|Proteomes:UP000291269}.
FT   DOMAIN          61..150
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS51986"
FT   DOMAIN          155..585
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51987"
SQ   SEQUENCE   693 AA;  76816 MW;  3C41ADBEF4D4A12C CRC64;
     MKVPELFASN VFNRQIMQDK LPKEIYRSLL KTIDEGAPLD MSVANVVANA MKDWAVEKGA
     THFTHWFQPM TGVTAEKHDS FISPTKDGKV IMEFSGKELV VGEPDASSFP SGGVRATFEA
     RGYTAWDPTS FAFVKDGTLY IPTAFFSYSG EVLDKKTPLL KSMAALNEQA LRILRLFGNE
     TVKRVYPTIG AEQEYFLIDR KMYDARKDLV FTGRTLFGAK APKGQELEDH YFGAIKTRVS
     EYMKDLDEEL WKLGILAKTK HNEVAPSQHE LAPVFTSTNV ASDQNQLVME TMKKVAGRHG
     LYCLLHEKPF AGINGSGKHN NWSMSTDTGM NLLDPGSTPA ENGQFMLFLT AVIKAVNEHQ
     DLLRLSVASA GNDHRLGANE APPAIVSVFL GEELEAVIDS LERGVKYSDK GRKTMKLGVD
     TLPELPKDTT DRNRTSPFAF TGNKFEFRMV GASLSLAGPN IIINTIVADA LRTFAEELEG
     AKDFNAALHD LVVRELKENG RILFNGNNYS EEWAKEAARR GLLNLKNAAE ALPLFADKKN
     IGLFERNGVF TAREVVTRTD IMLENYCKVL NIEALTMIEM AKRDIWPAVN EYIETLCNTA
     RSKKEAGAAA AADRRLIQKL SADNDAMFER AEALEGLLVE GKACGTPALL AAFFAEKVIP
     VMCELRMYAD GMELDTAAKV WPFPTYGDIL FSM
//
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