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
//