ID B3EIQ7_CHLL2 Unreviewed; 712 AA.
AC B3EIQ7;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 24-JAN-2024, entry version 70.
DE SubName: Full=Glutamine synthetase catalytic region {ECO:0000313|EMBL:ACD89998.1};
GN OrderedLocusNames=Clim_0919 {ECO:0000313|EMBL:ACD89998.1};
OS Chlorobium limicola (strain DSM 245 / NBRC 103803 / 6330).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=290315 {ECO:0000313|EMBL:ACD89998.1, ECO:0000313|Proteomes:UP000008841};
RN [1] {ECO:0000313|EMBL:ACD89998.1, ECO:0000313|Proteomes:UP000008841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 245 / NBRC 103803 / 6330
RC {ECO:0000313|Proteomes:UP000008841};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Zhao F., Li T., Liu Z.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium limicola DSM 245.";
RL Submitted (MAY-2008) 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; CP001097; ACD89998.1; -; Genomic_DNA.
DR AlphaFoldDB; B3EIQ7; -.
DR STRING; 290315.Clim_0919; -.
DR KEGG; cli:Clim_0919; -.
DR eggNOG; COG3968; Bacteria.
DR HOGENOM; CLU_024307_0_0_10; -.
DR OMA; QFLVFCA; -.
DR Proteomes; UP000008841; 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 65..158
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 163..597
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 712 AA; 78481 MW; 4A86443CCBE1CAC3 CRC64;
MESKVPVSSY FGAMTFDQKA MRARLPKDEF KALQDTIRAG KKITGEIAGV VAHGMKEWAM
EQGATHYTHW FQPMTGSTAE KHDAFLSIDR DGTPIERFSG EQLIQGEPDA SSFPSGGMRT
TFEARGYTAW DPSSPAFLMK GGTGLTLCIP TVFISYHGEA LDSKTPLLRS MDAVSNSAIR
LLNVLGTTGI SRVKTFAGCE QEYFLIDKKF YSERPDLIMC GRTLLGALPP KGQQLEDHYF
GSIPDRVLEF MQDVEHELYL LGIPAKTRHN EVAPHQFEIA PIFEEANIAV DHNLLVMEVM
RKVADKKGFA LLLTEKPFAG INGSGKHNNW SIGTDTGINL LDPGDTPTEN INFLVFLVAV
LKGVYKRADV LRMSIASTGN DHRLGANEAP PAVVTVFLGE QLETVLDAIE SGKVDLKTEK
QVLNLGLSQV PLLNKDYTDR NRTSPFAFTG NKFEFRAVGS SQAASVPNMV LNTLMAEALD
ELTDAIEAKI AAGKDRDSAV LEAIREGITA TKDIRYPGDN YSEALQQAAK ERGLPNLKNT
PQALRTLEKS DVKAMFVKYG VLTEQEIESR LNIRLERYVK GIDIEARTLQ LMLKTLVIPD
VSEYQGDIGN SFNNLLAASE AIGLSEGAIA SQANHFKNLA ENLSSLIDLT AELDEAVEKI
ETIEGEFGKA DFCADELLPL MNAVRAVADR LELMVDRSRW QLPTYSEMLF EH
//