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Database: UniProt
Entry: A0A5C5USN7_9CORY
LinkDB: A0A5C5USN7_9CORY
Original site: A0A5C5USN7_9CORY 
ID   A0A5C5USN7_9CORY        Unreviewed;       445 AA.
AC   A0A5C5USN7;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Glutamine synthetase {ECO:0000313|EMBL:TWT28580.1};
GN   ORFNames=FRX94_03155 {ECO:0000313|EMBL:TWT28580.1};
OS   Corynebacterium canis.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=679663 {ECO:0000313|EMBL:TWT28580.1, ECO:0000313|Proteomes:UP000320791};
RN   [1] {ECO:0000313|EMBL:TWT28580.1, ECO:0000313|Proteomes:UP000320791}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 58627 {ECO:0000313|EMBL:TWT28580.1,
RC   ECO:0000313|Proteomes:UP000320791};
RA   Lei W.;
RL   Submitted (AUG-2019) 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}.
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:TWT28580.1}.
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DR   EMBL; VOHM01000004; TWT28580.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5C5USN7; -.
DR   OrthoDB; 9807095at2; -.
DR   Proteomes; UP000320791; 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; 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:UP000320791}.
FT   DOMAIN          15..101
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS51986"
FT   DOMAIN          108..445
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51987"
SQ   SEQUENCE   445 AA;  50406 MW;  F2F15CE6A216C19C CRC64;
     MNSQQEFVLR TIEERDIRFV RLWFTDILGY LKSVAVVPAE LESAFEEGIG FDGSAIEGFS
     RVSEADTIAR PDPSTFQLMP FERQDTTDIA RMFCDITMPD GQPSYADPRQ VLRRQLKEAA
     NDGFTCFAHP EIEFFLVESL NTDGRPPTPT DNGGYFDQAV TDKAPHFRFD AMNALESMGI
     SVEFSHHETA PGQQEIDLRY ADVLTMADNI MTFRYIIKKT ALRNGVRSTF MPKPFAEYAG
     SAMHTHLSLF EGDTNAFHDP DDEFSLSSTA RQFIAGILHH APEFTAVTNQ WANSYKRLMF
     GNEAPTAATW GVSNSSAMVR VPTYRLGKVS SRRVEVRSPD SACNPYLAYA VLVAAGLKGI
     REGYELPDPA EDDISKLTRR ERRALGYQDL PGSLDQALRL MEQSELVAEA LGEHVFEYFL
     RNKWREWQDY QAQITSWELR TNLDY
//
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