ID Q7NHN6_GLOVI Unreviewed; 436 AA.
AC Q7NHN6;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE SubName: Full=Glutamine synthetase III {ECO:0000313|EMBL:BAC90440.1};
GN OrderedLocusNames=gll2499 {ECO:0000313|EMBL:BAC90440.1};
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221 {ECO:0000313|EMBL:BAC90440.1, ECO:0000313|Proteomes:UP000000557};
RN [1] {ECO:0000313|EMBL:BAC90440.1, ECO:0000313|Proteomes:UP000000557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421 {ECO:0000313|Proteomes:UP000000557};
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(2003).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|PROSITE-ProRule:PRU01330, ECO:0000256|RuleBase:RU000384}.
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DR EMBL; BA000045; BAC90440.1; -; Genomic_DNA.
DR RefSeq; NP_925445.1; NC_005125.1.
DR RefSeq; WP_011142494.1; NC_005125.1.
DR AlphaFoldDB; Q7NHN6; -.
DR STRING; 251221.gene:10759998; -.
DR EnsemblBacteria; BAC90440; BAC90440; BAC90440.
DR KEGG; gvi:gll2499; -.
DR PATRIC; fig|251221.4.peg.2537; -.
DR eggNOG; COG0174; Bacteria.
DR HOGENOM; CLU_017290_1_3_3; -.
DR InParanoid; Q7NHN6; -.
DR OrthoDB; 9807095at2; -.
DR PhylomeDB; Q7NHN6; -.
DR Proteomes; UP000000557; Chromosome.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
DR GO; GO:0006542; P:glutamine biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.10.20.70; Glutamine synthetase, N-terminal domain; 1.
DR Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR InterPro; IPR008147; Gln_synt_N.
DR InterPro; IPR036651; Gln_synt_N_sf.
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; IPR017536; Glutamine_synthetase_typeIII.
DR NCBIfam; TIGR03105; gln_synth_III; 1.
DR PANTHER; PTHR43785; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE; 1.
DR PANTHER; PTHR43785:SF12; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE PUUA; 1.
DR Pfam; PF00120; Gln-synt_C; 1.
DR SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF54368; Glutamine synthetase, N-terminal domain; 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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Reference proteome {ECO:0000313|Proteomes:UP000000557}.
FT DOMAIN 12..94
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 101..436
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
FT REGION 357..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 436 AA; 48230 MW; F17937A652698EA3 CRC64;
MTVPLSELAR EKGIRYFLIS FTDLFGTQRA KLVPTQAIDA IAASGAGFAG FAAWMDMSPA
DPDMFAHPDA GSVFQLPWQP EVAWMPADLF TPEGTAIAQT PRLVLKRVLK LALELGYRVR
TGVECEYFLL AADEVQIADS RDFQSKPCYD QQALMRRYAV ISEICDAMNA LGWGAYQNDH
EDANGQFEMN WTYADALVTA DRHAFFKYMV KTVAEKHSLR ATFMPKPFMH LTGNGCHTHL
SVWDSEGKVN RFDDPRGELG LSPLAYHFIG GVQHSAEALC AFANPTVNSY KRINAPITAS
GATWSPNTIS YSGNNRTHAI RIPEPGRFEL RLADGAANPY LLPAALTAVG LDGIAHQRDA
GPRRDNNSYT NPLPPESAKP LPANLLDALR ALESDTVLSE AMGADFVASY LKLKHREWQD
YCARVTPWEL EHTLDC
//
