ID C0DA05_9FIRM Unreviewed; 700 AA.
AC C0DA05;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Glutamine synthetase {ECO:0000256|ARBA:ARBA00021364};
GN Name=glnA {ECO:0000313|EMBL:EEG51850.1};
GN ORFNames=CLOSTASPAR_06105 {ECO:0000313|EMBL:EEG51850.1};
OS [Clostridium] asparagiforme DSM 15981.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Enterocloster.
OX NCBI_TaxID=518636 {ECO:0000313|EMBL:EEG51850.1, ECO:0000313|Proteomes:UP000004756};
RN [1] {ECO:0000313|EMBL:EEG51850.1, ECO:0000313|Proteomes:UP000004756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15981 {ECO:0000313|EMBL:EEG51850.1,
RC ECO:0000313|Proteomes:UP000004756};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEG51850.1, ECO:0000313|Proteomes:UP000004756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15981 {ECO:0000313|EMBL:EEG51850.1,
RC ECO:0000313|Proteomes:UP000004756};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Clostridium asparagiforme (DSM 15981).";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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:EEG51850.1}.
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DR EMBL; ACCJ01000515; EEG51850.1; -; Genomic_DNA.
DR AlphaFoldDB; C0DA05; -.
DR HOGENOM; CLU_024307_0_0_9; -.
DR Proteomes; UP000004756; Unassembled WGS sequence.
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:EEG51850.1}.
FT DOMAIN 64..153
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 158..590
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 700 AA; 78231 MW; F02B3ED2C3ECD772 CRC64;
MMASGIPELY GSLVFNDSVM RDKLPKDVYQ ALRKTIENHT HLELDVANSV AVAMKEWAVE
NGATHFTHWF QPMTGFTAEK HDSFISPVGG GQVVMDFSGK ELVKGEPDAS SFPSGGLRAT
FEARGYTAWD PTSPAFIKDR TLYIPTAFCS YSGEALDKKT PLLRSMETLD REAVKILHLL
GQRDVEGVSA TIGPEQEYFL VDKEIYKQRK DLIFTGRTLL GAMPPKGQEM EDHYFGALKP
RVSAFMHDLD EALWKLGIPA KTKHNEVAPA QHELAPVFDT ANVAVDHNQL TMEMMKKVAD
KHGLTCLLHE KPFEGINGSG KHNNWSLITN TGVNLLNPGR TPAANIQFLV FLMAVIKAVD
EYADLMRISV ASAGNDHRLG ANEAPPAIVS IFLGDELTAV LDSIENDTFF GKQQKVQMET
GATVLPHFFK DNTDRNRTSP FAFTGNKFEF RMPGSSLSVA GPNIVLNTAV AEALRQFYEE
LKDIPESRME EAVHALVKRA IAKHRRIIFN GNGYTDEWVR EAKKRGLYNL RSTPEALACF
TSQKNLELFT RHHIFTEQEI VSRYEILLEN YCKTIHIEAQ TMQDMVRSQF LPALRCYIDQ
ITGSIRGIKA VSEALPSAAS EKLLAALCDS YERICDAEEH LEADTKNAEG IDDMQEAAFF
YRGTLIPGME ALRAMADAVE RYLPENLLPY PSYEKLLFSV
//