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Database: UniProt
Entry: B3EIQ7_CHLL2
LinkDB: B3EIQ7_CHLL2
Original site: B3EIQ7_CHLL2 
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
//
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