ID F2JNM1_CELLD Unreviewed; 695 AA.
AC F2JNM1;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Glutamine synthetase {ECO:0000256|ARBA:ARBA00021364};
GN OrderedLocusNames=Clole_4238 {ECO:0000313|EMBL:ADZ85910.1};
OS Cellulosilyticum lentocellum (strain ATCC 49066 / DSM 5427 / NCIMB 11756 /
OS RHM5) (Clostridium lentocellum).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Cellulosilyticaceae;
OC Cellulosilyticum.
OX NCBI_TaxID=642492 {ECO:0000313|EMBL:ADZ85910.1, ECO:0000313|Proteomes:UP000008467};
RN [1] {ECO:0000313|EMBL:ADZ85910.1, ECO:0000313|Proteomes:UP000008467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49066 / DSM 5427 / NCIMB 11756 / RHM5
RC {ECO:0000313|Proteomes:UP000008467};
RX PubMed=21398547; DOI=10.1128/JB.00239-11;
RG US DOE Joint Genome Institute;
RA Miller D.A., Suen G., Bruce D., Copeland A., Cheng J.F., Detter C.,
RA Goodwin L.A., Han C.S., Hauser L.J., Land M.L., Lapidus A., Lucas S.,
RA Meincke L., Pitluck S., Tapia R., Teshima H., Woyke T., Fox B.G.,
RA Angert E.R., Currie C.R.;
RT "Complete genome sequence of the cellulose-degrading bacterium
RT Cellulosilyticum lentocellum.";
RL J. Bacteriol. 193:2357-2358(2011).
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|PROSITE-ProRule:PRU01330, ECO:0000256|RuleBase:RU000384}.
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DR EMBL; CP002582; ADZ85910.1; -; Genomic_DNA.
DR RefSeq; WP_013659180.1; NC_015275.1.
DR AlphaFoldDB; F2JNM1; -.
DR STRING; 642492.Clole_4238; -.
DR KEGG; cle:Clole_4238; -.
DR eggNOG; COG3968; Bacteria.
DR HOGENOM; CLU_024307_0_0_9; -.
DR Proteomes; UP000008467; 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:UP000008467}.
FT DOMAIN 62..151
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 156..585
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 695 AA; 77671 MW; E946F445E8F8DAC9 CRC64;
MANVSEIFGC NVFNETVMQE RLPKNTFKAL KKTMAEGKEL SRDIADVVAA AMKDWAVEKG
ATHYTHWFQP MTGITAEKHD AFISPSADGK VILEFSGKEL IKGEPDASSF PSGGLRATFE
ARGYTTWDPT SYAFVKDDTL YIPTAFGSYG GEVLDKKTPL LRSMEALNKQ AIRILNKFGK
SVTRVTTTVG PEQEYFLVDK EMYAKRKDLI LTGRTLFGAK PAKGQELEDH YFGNIRTRVS
EYMKDLDNEL WKLGILAKTK HNEVAPAQHE LAPIFGTTNI ATDHNQLTME MMKKVAERHG
LVCLLHEKPF AGVNGSGKHN NWSMSTSEGE NLLEPGKSPK DNTQFLLFLA AVIKAVDEYA
DLLRVSVASA GNDHRLGANE APPAIISMFL GDELTNILEC IEKGEAVSET ARCFMETGVS
ALPRFVKDTT DRNRTSPFAF TGNKFEFRSL GSSVSISGPN IVLNTSVAEV LEEFADRLDA
ATDLEAEVMA IVKETMKDHK RVIFNGNNYS DEWVEEAERR GLLNLKTSVD AIPRFGMEKS
IKLFEKHGIF TATEVKSRCE ILLEGYAKTI NIEALTMLDM AQKEILPAVL KYNKEVFETL
KVKQELGLNV SVEKEVSYAT KLSNLTESLM SKIEELDKVL LEAKNYEDAL ESAKYYREYV
FEAMQTLRVV ADELETMVAS VAWPFPTYVD LLFYV
//
