ID Q3AQ82_CHLCH Unreviewed; 714 AA.
AC Q3AQ82;
DT 22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Glutamine synthetase {ECO:0000313|EMBL:ABB28843.1};
DE EC=6.3.1.2 {ECO:0000313|EMBL:ABB28843.1};
GN OrderedLocusNames=Cag_1588 {ECO:0000313|EMBL:ABB28843.1};
OS Chlorobium chlorochromatii (strain CaD3).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=340177 {ECO:0000313|EMBL:ABB28843.1};
RN [1] {ECO:0000313|EMBL:ABB28843.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CaD3 {ECO:0000313|EMBL:ABB28843.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Chlorobium chlorochromatii CaD3.";
RL Submitted (AUG-2005) 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; CP000108; ABB28843.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3AQ82; -.
DR STRING; 340177.Cag_1588; -.
DR KEGG; cch:Cag_1588; -.
DR eggNOG; COG3968; Bacteria.
DR HOGENOM; CLU_024307_0_0_10; -.
DR OrthoDB; 9807095at2; -.
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:ABB28843.1}.
FT DOMAIN 67..160
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 165..599
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 714 AA; 79316 MW; A92B85CB3040F080 CRC64;
MNSDSKVPVS TYFGAFTFDH KAMRAKLPKE EFVALQETIK AGKKITAEIA GVVAHGMKEW
AMEHGATHYT HWFQPMTGST AEKHDAFLSI DRDGTPIERF SGEQLIQGEP DASSFPSGGM
RTTFEARGYT AWDPSSPAFL MKGGNGLTLC IPTVFISYHG AALDAKTPLL RSMDAASKSA
LRLLGVLGVE GVKRVKTYAG CEQEYFLVDK KFYTARPDLV MCGRTLLGAL PPKGQQLEDH
YFGSIPDRVL EFMQEVEHEL FLLGIPAKTR HNEVAPHQFE IAPIFEEANI AVDHNMLVME
VMRKIADKRG FALLLAEKPF AGINGSGKHN NWSIGTDTGI NLLDPGDTPE KSILFLIILV
SVLKAVHKRA DLLRMSIASM GNDHRLGANE APPAVVTVFL GDLLERVLDA IESGQVDLKT
EKQVLNLGLS QVPEVNKDYT DRNRTSPFAF TGNKFEFRAV GSSQAPSVAN MVLNTIMAEA
LDEMSEAIEA KIQAGSDKDV AVLETIREQI TVTKPIRYPG DNYSEALQVA AHERGLPNLK
NTPHSLRILL KKDVQDMFIK YGVLSHEEID ARLHIRLERY IKGIDIEART LLLMLKTYVI
PNVSEYQGDL GNSFNSLFAV SEAIGLSDKA LDSQAKHLKM VAENLATLLD MTNELEEAIE
QIESCKSEFD KADYCADKLL PFMEEVRVVA DRLEQVVDRS RWQLPTYLEM LFEH
//
