ID A0A090JMK4_9FIRM Unreviewed; 692 AA.
AC A0A090JMK4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Glutamine synthetase {ECO:0000256|ARBA:ARBA00021364};
GN Name=glnN {ECO:0000313|EMBL:CDZ74689.1};
GN ORFNames=ING2D1G_0508 {ECO:0000313|EMBL:CDZ74689.1};
OS Peptoniphilus sp. ING2-D1G.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=1912856 {ECO:0000313|EMBL:CDZ74689.1, ECO:0000313|Proteomes:UP000032409};
RN [1] {ECO:0000313|EMBL:CDZ74689.1, ECO:0000313|Proteomes:UP000032409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Peptoniphilus sp. ING2-D1G {ECO:0000313|Proteomes:UP000032409};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) 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; LM997412; CDZ74689.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090JMK4; -.
DR STRING; 1912856.ING2D1G_0508; -.
DR KEGG; ped:ING2D1G_0508; -.
DR PATRIC; fig|875453.3.peg.494; -.
DR HOGENOM; CLU_024307_0_0_9; -.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000032409; Chromosome.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:UniProtKB-EC.
DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
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 Coiled coil {ECO:0000256|SAM:Coils}; Ligase {ECO:0000313|EMBL:CDZ74689.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000032409}.
FT DOMAIN 63..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"
FT COILED 608..642
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 692 AA; 79847 MW; 92CE120E617FD652 CRC64;
MGNRIIEEFG EMTFNKARMK ERLPYPVYLK WKEVVRTNRT LDKETADSIA HAMKEWALEK
GATHYTHWFF PLNGLTAKKH EAFLDRTSDF ETMNRFSGKE LIKGEPDASS FPSGGMRSTF
EARGYTYWDC TANSFIIDHI LYIPSIFLSY TGEVLDKRAP LMSSLNEISR EGSRVVNMIE
KSEYTYRMRP KVGLEQEFFL IDKKVYDKRS DLKNCGKTLF GARPPKGQEL EDHYFGAIPQ
RVMDFYEEVN KKLWTLGIYA KTEHNEAAPC QFEVAILFEN SNISIDDNQL CMSILQQTAL
KHDLVCLLHE KPFRGINGSG KHNNYSLMTN YGLNVFDPGE NPKENLVFLI FTAALIETVY
KYQTLFRISS SSVSNDLRLG GNEAPPAIVS VFLGKDLEDL FNSIAYEDYE PRYFDGVIKI
ASLGEIEKDR SDRNRTSSVA FTGNKFEFRM LGSSKTAADI NIVINTAMAS SLKRIADRLE
NIEEKDLKSE VYEIVKKIII NCGGILYDGD NYSDEWVEEA KKRGLKNHKT LFDALVAIKE
EKSYELFYEM NIFTENELKA IYEVNFEDIA KYHSLDLRIA EDMIIKDIVP AALKEIKDLG
ESLRYVENDC LKELMERLNN CVKELLIKRE EAMEICNNFE KKQSCFEKAE YLQENAVSLL
EEMRNYADDI EKVVSRENYK IPIYEDVFSS LI
//
