ID A0A109W761_9FLAO Unreviewed; 725 AA.
AC A0A109W761;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Glutamine synthetase {ECO:0000313|EMBL:AMD86268.1};
GN ORFNames=AXF12_09885 {ECO:0000313|EMBL:AMD86268.1};
OS Capnocytophaga haemolytica.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=45243 {ECO:0000313|EMBL:AMD86268.1, ECO:0000313|Proteomes:UP000065822};
RN [1] {ECO:0000313|Proteomes:UP000065822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 32990 {ECO:0000313|Proteomes:UP000065822};
RA Holder M.E., Ajami N.J., Petrosino J.F.;
RL Submitted (FEB-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; CP014227; AMD86268.1; -; Genomic_DNA.
DR RefSeq; WP_066431979.1; NZ_LT906449.1.
DR AlphaFoldDB; A0A109W761; -.
DR STRING; 45243.AXF12_09885; -.
DR KEGG; chg:AXF12_09885; -.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000065822; Chromosome.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
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;
FT DOMAIN 82..171
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 176..613
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 725 AA; 81759 MW; BD66A86DEDE2DD49 CRC64;
MLRFNALKEM GKRTPVAITE NGKRSELFAQ NVFHEAAMRQ FMTPEAFNSV MGAIRYGTKI
DRRVADQVAT AMRDWAISKG ATHYTHWFQP LTGSTAEKHD AFFEPVGRDR AIERFGGGQL
VQQESDASSF PNGGIRNTFE ARGYTAWDPT SPPFVYGTTL CIPTIFISYT GEALDNKTPL
LKALTAIDEA ATEVARYFDK NVNKVTATLG WEQEYFLIDK ALARTRPDLM IAGRTLLGHQ
AAKGQQLDDH YFGAIPGRVL AYMRDLEQEC LLLGIPVKTR HNEVAPNQFE LAPIFEEANL
AVDQNSLLMD VMKKVADRHD FVVLFHEKPF AGVNGSGKHN NWSLATDTGV NLLAPSKTPM
KNLQFLTFFI CTIKAVHTYE ALLRAAVASA TNDHRLGANE APPAIMSVFI GEQLTKVLDE
LEGVPSGKLS PEEKTELKLN VVGKIPDLFL DNTDRNRTSP FAFTGNKFEF RAVGSRANCG
KPMMVLNTIV AKQLRDFKQE VDTLIEQGTL KKDEAIFNVL REYIKQSKAI RFEGDGYSKA
WEKEAAKRGL SNHKTTPEAL RENLSDQAIA LFEEMGVLSR VELEARYEIA LEEYVKTVQI
ESRIIGDIAR NHVVPTAVRY LNTLIENVKG LKEIFSSNYE AIASEQIELI KRISEHIRVI
HSKVNAMIEM RKHANALSSF EQRAEVYCHQ VLPFFEEIRY HADKLELMVD DELWTLTKYR
ELFFS
//
