ID F8A347_CELGA Unreviewed; 448 AA.
AC F8A347;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Glutamine synthetase, type I {ECO:0000313|EMBL:AEI11902.1};
GN OrderedLocusNames=Celgi_1383 {ECO:0000313|EMBL:AEI11902.1};
OS Cellulomonas gilvus (strain ATCC 13127 / NRRL B-14078) (Cellvibrio gilvus).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=593907 {ECO:0000313|EMBL:AEI11902.1, ECO:0000313|Proteomes:UP000000485};
RN [1] {ECO:0000313|Proteomes:UP000000485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13127 / NRRL B-14078 {ECO:0000313|Proteomes:UP000000485};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Munk A., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Mead D., Brumm P.,
RA Woyke T.;
RT "Complete sequence of Cellvibrio gilvus ATCC 13127.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|PROSITE-ProRule:PRU01330, ECO:0000256|RuleBase:RU000384}.
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DR EMBL; CP002665; AEI11902.1; -; Genomic_DNA.
DR AlphaFoldDB; F8A347; -.
DR STRING; 593907.Celgi_1383; -.
DR KEGG; cga:Celgi_1383; -.
DR eggNOG; COG0174; Bacteria.
DR HOGENOM; CLU_017290_1_3_11; -.
DR Proteomes; UP000000485; Chromosome.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR Gene3D; 3.10.20.70; Glutamine synthetase, N-terminal domain; 1.
DR Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR InterPro; IPR008147; Gln_synt_N.
DR InterPro; IPR036651; Gln_synt_N_sf.
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 PANTHER; PTHR43785; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE; 1.
DR PANTHER; PTHR43785:SF11; GLUTAMINE SYNTHETASE; 1.
DR Pfam; PF00120; Gln-synt_C; 1.
DR Pfam; PF03951; Gln-synt_N; 1.
DR SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF54368; Glutamine synthetase, N-terminal domain; 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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Reference proteome {ECO:0000313|Proteomes:UP000000485}.
FT DOMAIN 18..103
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 110..448
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 448 AA; 50018 MW; D241A347B0D69E91 CRC64;
MQRMDRQQEF VLRTVEERDI RFIRLWFTDV LGILKSVAVA PAELEAAFSE GIGFDGSSIE
GLTRVYEADM IARPDPSTFQ VLPWRGERHG TARMFCDLLT PDGEPSLADS RNVLKRALSR
ASDKGFTFYT HPEVEFYLFD APADPALPLT PVDQGGYFDH VPRGTAHDFR RAAITMLESM
GISVEFSHHE AGPGQNEIDL RYADALTTAD NIMTFRTVVK EVALEQGVFA SFMPKPLADQ
PGSGMHTHLS LFEGDRNAFH EAGGHLELSK TARSFIAGLL VHAAEITAVT NQFVNSYKRL
WGGAEAPSYI CWGHNNRSAL VRVPMYKPGK GNSSRIEYRA VDSATNPYLA FAVLLAAGLK
GIEEGYELPE GAEDDVWELT DAERRALGIE PLPQSLEAAI AVMEKSELVA ETLGEHVFDF
FLRNKRQEWD EYRAQVTPYE LKRFLPVL
//
