ID K4LGI5_9FIRM Unreviewed; 698 AA.
AC K4LGI5;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Glutamine synthetase {ECO:0000256|ARBA:ARBA00021364};
GN ORFNames=DCF50_p1686 {ECO:0000313|EMBL:AFV05688.1};
OS Dehalobacter sp. CF.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Dehalobacter.
OX NCBI_TaxID=1131462 {ECO:0000313|EMBL:AFV05688.1, ECO:0000313|Proteomes:UP000000482};
RN [1] {ECO:0000313|EMBL:AFV05688.1, ECO:0000313|Proteomes:UP000000482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF {ECO:0000313|EMBL:AFV05688.1};
RX PubMed=23284863; DOI=10.1371/journal.pone.0052038;
RA Tang S., Gong Y., Edwards E.A.;
RT "Semi-automatic in silico gap closure enabled de novo assembly of two
RT dehalobacter genomes from metagenomic data.";
RL PLoS ONE 7:E52038-E52038(2012).
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|PROSITE-ProRule:PRU01330, ECO:0000256|RuleBase:RU000384}.
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DR EMBL; CP003870; AFV05688.1; -; Genomic_DNA.
DR RefSeq; WP_015043735.1; NC_018867.1.
DR AlphaFoldDB; K4LGI5; -.
DR STRING; 1131462.DCF50_p1686; -.
DR KEGG; dec:DCF50_p1686; -.
DR PATRIC; fig|1131462.4.peg.1700; -.
DR eggNOG; COG3968; Bacteria.
DR HOGENOM; CLU_024307_0_0_9; -.
DR Proteomes; UP000000482; 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:AFV05688.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000482}.
FT DOMAIN 58..152
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 157..588
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 698 AA; 76924 MW; EE658EB1BF8387B3 CRC64;
MDIFAMNVFN DAVMRERLPK ATYKALKKTI EDGKALDPDV AEVVANAMKD WAIEKGATHY
THWFQPMTGL TAEKHDSFIS PTADGKVIME FSGKELIKGE PDASSFPSGG IRATFEARGY
TAWDCTSPAF AREEKNGNVT LTIPTVFYSY TGEVLDKKIP LLRSMEALSK QAVRLLRLFG
NTTATRVIST VGPEQEYFLI DKSFFDARMD LVLTGRTLFG APPAKGQEME DHYFGSIKER
IAAFMKELNE ELWKLGVLAK TQHNEVAPGQ FEIAPIFSTT NVATDHNQLI MDTLKKVALH
HDLVCLLHEK PFAGVNGSGK HNNWSMSTND GQNLLDPGNT PHDNAQFLTF LCAVIKAVDE
YSELLRVSAA NPGNDHRLGA NEAPPAIISM FLGDMLSDIV EQIQNNGGAV SSKPNGTLTV
GVSTLPEIPK DNSDRNRTSP FAFTGNKFEF RMVPSSASIA GPNMVLNTIV AESICQIADK
LEKAADFNSE LQALLKEILV KHNRIIFNGN NYSEDWVVEA EKRGLPNIKS MVEALEHFID
EKNVNAFEKH GVLSKQEVHS RYEILLEQYS KTINIEAKTM IDMANRLILP AAAKYATDLA
GSVQSVKAAV ASADTSAQEE VIKEVSSALG SFKAKTVALE KAVLGAADVE DVHANAVYYR
DIVFAAMNEL RIYGDKLETL VDAELWPLPT YVEMLFII
//
