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Database: UniProt
Entry: A0A3L8A9E8_9BACE
LinkDB: A0A3L8A9E8_9BACE
Original site: A0A3L8A9E8_9BACE 
ID   A0A3L8A9E8_9BACE        Unreviewed;       729 AA.
AC   A0A3L8A9E8;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Glutamine synthetase type III {ECO:0000313|EMBL:RLT79622.1};
GN   ORFNames=D7Y07_12755 {ECO:0000313|EMBL:RLT79622.1};
OS   Bacteroides acidifaciens.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=85831 {ECO:0000313|EMBL:RLT79622.1, ECO:0000313|Proteomes:UP000267159};
RN   [1] {ECO:0000313|EMBL:RLT79622.1, ECO:0000313|Proteomes:UP000267159}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0.1X-D8-26 {ECO:0000313|EMBL:RLT79622.1,
RC   ECO:0000313|Proteomes:UP000267159};
RA   Liu C.;
RT   "Murine metabolic-syndrome-specific gut microbial biobank.";
RL   Submitted (SEP-2018) 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:RLT79622.1}.
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DR   EMBL; RAZM01000041; RLT79622.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3L8A9E8; -.
DR   STRING; 1235814.GCA_000613385_03490; -.
DR   Proteomes; UP000267159; 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..174
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS51986"
FT   DOMAIN          182..615
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51987"
SQ   SEQUENCE   729 AA;  81929 MW;  3EBC238F0FE0CCB1 CRC64;
     MSKLRFRVVE TAFKKKAVEV ATPAERPSEY FAKYVFNKEK MFKYLPSKVY NALIDAIDNG
     APLDRSIADE VAAGMKKWAT EMGVTHYTHW FAPLTEGTAE KHDAFVEHDG KGGMMEEFTG
     KLLVQQEPDA SSFPNGGIRN TFEARGYSAW DPSSPAFIVD DTLCIPTVFI AYTGEALDYK
     APLLKALRAV DKAAVDVCHY FNPEVKKVVA YLGWEQEYFL VDEGLYAARP DLLMTGRTLM
     GHDSAKNQQL EDHYFGAIPT RVAAFMKDLE IEALKLGIPV KTRHNEVAPN QFELAPIFEE
     CNLANDHNLL IMSLMRKVSR RHGFRVLLHE KPFKGVNGSG KHNNWSLGTD TGILLMGPGK
     TPEDNLRFVT FVVNTLMAVY HHNGLLKASI SSATNAHRLG ANEAPPAIIS SFLGKQLSQV
     LDHIENSTKD DLISLSGKQG MKLDIPQIPE LLIDNTDRNR TSPFAFTGNR FEFRAVGSEA
     NCASAMIALN SAVAHQLTKF KKDVDALIEK GEPKISAILE IIRGYIKECK AIHFDGNGYS
     DEWKEEAARR GLDCETSVPV IFDNYLKPET IAMFEATGVM TKKELEARNE VKWETYTKKI
     QIEARVLGDL AMNHIIPVAT QYQTDLINNV YKMQSLFPAE KAAKLSAKNL ELIEEIADRT
     AFIKEHVDAM VEARKVANKI ESEREKAIAY HDTITPALEE IRYHIDKLEL IVDNQMWTLP
     KYRELLFVR
//
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