ID A0A136M178_9BACT Unreviewed; 668 AA.
AC A0A136M178;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Glutamine synthetase {ECO:0000313|EMBL:KXK27662.1};
GN ORFNames=UZ12_BCD005001256 {ECO:0000313|EMBL:KXK27662.1};
OS Bacteroidetes bacterium OLB12.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1619897 {ECO:0000313|EMBL:KXK27662.1, ECO:0000313|Proteomes:UP000070129};
RN [1] {ECO:0000313|EMBL:KXK27662.1, ECO:0000313|Proteomes:UP000070129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB12 {ECO:0000313|EMBL:KXK27662.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Genome based microbial ecology of anammox granules in a full-scale
RT wastewater treatment system.";
RL Submitted (NOV-2015) 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:KXK27662.1}.
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DR EMBL; LNFR01000050; KXK27662.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136M178; -.
DR STRING; 1619897.UZ12_BCD005001256; -.
DR PATRIC; fig|1619897.3.peg.1362; -.
DR Proteomes; UP000070129; 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;
FT DOMAIN 85..171
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 176..611
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 668 AA; 74348 MW; AEB89C0303F06B5F CRC64;
MAHLRFEALK KLNERPKVHV DATTPHISQF FGENVFGMEQ MRSTLAPAVF KKVSHAIKNH
EKIDEATADA VASAVKSWAI AKGATHFTHW FQPMTGGTAE KHDSFFDALS GIEKFKGSEL
VQQEPDASSF PSGGIRTTFE ARGYTAWDPT SPMFLYGKTL SIPTIFVSYT GETLDTKSPL
LKALKAVDVA ATKVCQLFDK DIQHVVASLG SEQEYFAVDK SLFNARPDLV MAGRTVFGHS
PARGQQLEDH YFGTIPGRVY DFMRDFEIEC WKLGIPVRTR HNEVAPSQFE VAPLFEEVNV
ANDHNQLMMD VISRVGDKHN LKILFHEKPF AGLNGSGKHN NWSLITDTGV NLYAPSSSAR
DNLLFLTFFV TTIKAVHEYA DLLRASIATA GNDFRLGANE APPAIMSVFI GSQMTAVLDE
LEKNGNVKIE KGDNMYMKLG IDQIPEIILD ATDRNRTSPF AFTGNKFEFR AVGGSDNCAT
PMAVLNLIVA EQLTQLFDTV SAEIEKGEEK RLAIVNVLRK YIKESKAIRF EGDGYSDEWV
KEAEKRGLKN IKNMPRAIEA YVSKKSLALF EKHEVMSHKE VEARNEIKLE SYIKRVQIEA
RVIGDLAMNH IIPTAIAYQN KLITNANGLK GLGVDNTAVV QTIKEISGHI ETIKGSVREM
VEERKTPQ
//
