ID D4IQ80_9BACT Unreviewed; 718 AA.
AC D4IQ80;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 08-NOV-2023, entry version 59.
DE SubName: Full=L-glutamine synthetase {ECO:0000313|EMBL:CBK65092.1};
DE EC=6.3.1.2 {ECO:0000313|EMBL:CBK65092.1};
GN ORFNames=AL1_29910 {ECO:0000313|EMBL:CBK65092.1};
OS Alistipes shahii WAL 8301.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=717959 {ECO:0000313|EMBL:CBK65092.1, ECO:0000313|Proteomes:UP000008794};
RN [1] {ECO:0000313|EMBL:CBK65092.1, ECO:0000313|Proteomes:UP000008794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAL 8301 {ECO:0000313|EMBL:CBK65092.1,
RC ECO:0000313|Proteomes:UP000008794};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J.;
RT "The genome sequence of Alistipes shahii WAL 8301.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBK65092.1, ECO:0000313|Proteomes:UP000008794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAL 8301 {ECO:0000313|EMBL:CBK65092.1,
RC ECO:0000313|Proteomes:UP000008794};
RA Pajon A.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|PROSITE-ProRule:PRU01330, ECO:0000256|RuleBase:RU000384}.
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DR EMBL; FP929032; CBK65092.1; -; Genomic_DNA.
DR RefSeq; WP_015547896.1; NZ_CP102253.1.
DR AlphaFoldDB; D4IQ80; -.
DR STRING; 717959.AL1_29910; -.
DR KEGG; ash:AL1_29910; -.
DR PATRIC; fig|717959.3.peg.1501; -.
DR HOGENOM; CLU_024307_0_0_10; -.
DR OrthoDB; 9807095at2; -.
DR BioCyc; ASHA717959:AL1_RS14080-MONOMER; -.
DR Proteomes; UP000008794; Chromosome.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:UniProtKB-EC.
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 Ligase {ECO:0000313|EMBL:CBK65092.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008794}.
FT DOMAIN 78..167
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 172..609
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 718 AA; 80699 MW; 22CFCDE7EF01D361 CRC64;
MVDAAINHTA VEVKVPEGRP SDYFGKKVFG RAAMRKYLDK RTYAALLDTM EKRTPLTREV
ADSIAAGMRQ WALEHGADHY THWFQPLTGG TAEKHDAFAE PDGQGGVLEE FSGKLLVQQE
PDASSFPNGG IRNTFEARGY SAWDPTSPAF IVDTTLCIPT VFIAYTGEAL DYKVPLLRSL
TAIDKAATEV CRYFDKNVEK VFSYLGWEQE YFLVDESLWA VRPDLMLTGR TLMGHESAKN
QQLEDHYFGA IPTRVMAFMK DLEYECLKLG IPVKTRHNEV APNQFELAPV YEEANLANDH
NQLLMTIMDK IARRHQFRVL LHEKPFKGIN GSGKHNNWSL GTDTGVNLLG PGKTASENLQ
FITFLVNAIS AVYKHNGLLK ASIMSATNAH RLGANEAPPA IISTFLGTQV SAVLDKLAAS
KGDDAIRFDA KNVFKMSGIS HIPTLLLDNT DRNRTSPFAF TGNRFEFRAV GSSDNCAEAM
IVLNSAMAYE LTEFKKAVDA KIEAGAKKER AIYEVLKQMI KACKAIRFDG NGYSDEWKAE
AKRRGLDCET STPLIFDRYL DRESLKMFGD MGVFTKVELE ARTEVKWETY TKKIQIEGRV
LGDLAMNHIV PIASKYEAQL LDKVYKMHQI GGLNASSDIL LIKKIQDHTA SIQKLTGEMI
DARKVANRIE DPREKAIAYH DTVAVCFDEI RRHIDKLEEI VDDQIWPLPK YRELLFLR
//
