ID I5AVX8_EUBCE Unreviewed; 704 AA.
AC I5AVX8;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Glutamine synthetase {ECO:0000256|ARBA:ARBA00021364};
GN ORFNames=EubceDRAFT1_2191 {ECO:0000313|EMBL:EIM57951.1};
OS [Eubacterium] cellulosolvens 6.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=633697 {ECO:0000313|EMBL:EIM57951.1, ECO:0000313|Proteomes:UP000005753};
RN [1] {ECO:0000313|EMBL:EIM57951.1, ECO:0000313|Proteomes:UP000005753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6 {ECO:0000313|EMBL:EIM57951.1,
RC ECO:0000313|Proteomes:UP000005753};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Land M.L., Hauser L., Chang Y.-J., Anderson I.J., Johnson E.,
RA Mulhopadhyay B., Kyrpides N., Woyke T.J.;
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EIM57951.1, ECO:0000313|Proteomes:UP000005753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6 {ECO:0000313|EMBL:EIM57951.1,
RC ECO:0000313|Proteomes:UP000005753};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Gu W., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Johnson E., Mukhopadhyay B.,
RA Anderson I., Woyke T.;
RT "Improved High-Quality Draft sequence of Eubacterium cellulosolvens 6.";
RL Submitted (FEB-2012) 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; CM001487; EIM57951.1; -; Genomic_DNA.
DR AlphaFoldDB; I5AVX8; -.
DR STRING; 633697.EubceDRAFT1_2191; -.
DR eggNOG; COG3968; Bacteria.
DR HOGENOM; CLU_024307_0_0_9; -.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000005753; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000005753}.
FT DOMAIN 65..159
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 164..595
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 704 AA; 78044 MW; AA8E7A11EDA73A5E CRC64;
MAEYINPADI FGELVFNDET MQERLPKKVY ATLKKIINEG GDLDLATADV IAHEMKEWAI
EKGATHYTHW FQPLNGLTAE KHDSFISAPL SSGKTLMSFS GKELIKGEPD ASSFPSGGLR
ATFEARGYTA WDCTSPAFVR QDEGGATLCI PTAFCSYTGE ALDQKTPLLR SMEVINREAL
RLIRLFGNDT SAKVIPSVGA EQEYFIVDEE KYLQRKDLIY TGRTLFGTMP AKGQEMDDHY
FGTIRPRIAA FMKDVDIELW KMGVTAKTEH NEVAPGQHEL AVIYSEANVA TDENQLIMQT
LKRVARRHGL KCLLHEKPFD GVNGSGKHDN WSLTTDDGIN LLDPGKTPHE NIQFLMILSC
IIKAVDVHAG LLRESAADPG NDHRLGANEA PPAILSIFLG EQLDDVVNQL VSTGSANRSL
KGETLNTGVA SLPELYKDAT DRNRTSPFAF TGNKFEFRMV GSQDSIAEPN VVLNTIVAEA
FAEASEIIEQ SPDFNEAVHD IIKKNFTEHQ RIIFNGNGYS DAWVEEAARR GLPNISCMVD
AIPQLVTDET VAMFEKFKVF TRSELESRAE IKYEYYAKTI NIEAKAMINI ASKRIIPAII
NYTRDLAETI IAVQAAGVGE ISVQKELLEQ TSALLREAKT ALQKLMEVDS KAGAMEVGQA
QAKYYYAEVT PAMAALRKPV DELEQIVDKS MWPMPSYGDL LFEV
//
