ID GLNA_PYRKO Reviewed; 443 AA.
AC O08467; Q5JJ67;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 29-MAY-2013, entry version 86.
DE RecName: Full=Glutamine synthetase;
DE Short=GS;
DE EC=6.3.1.2;
DE AltName: Full=Glutamate--ammonia ligase;
GN Name=glnA; OrderedLocusNames=TK1796;
OS Pyrococcus kodakaraensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Thermococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=9172372;
RA Adul Rahman R.N.Z., Jongsareejit B., Fujiwara S., Imanaka T.;
RT "Characterization of recombinant glutamine synthetase from the
RT hyperthermophilic archaeon Pyrococcus sp. strain KOD1.";
RL Appl. Environ. Microbiol. 63:2472-2476(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon
RT Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus
RT genomes.";
RL Genome Res. 15:352-363(2005).
CC -!- CATALYTIC ACTIVITY: ATP + L-glutamate + NH(3) = ADP + phosphate +
CC L-glutamine.
CC -!- ENZYME REGULATION: The activity of this enzyme is controlled by
CC adenylation under conditions of abundant glutamine. The fully
CC adenylated enzyme complex is inactive (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
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DR EMBL; D86222; BAA20530.1; -; Genomic_DNA.
DR EMBL; AP006878; BAD85985.1; -; Genomic_DNA.
DR RefSeq; YP_184209.1; NC_006624.1.
DR ProteinModelPortal; O08467; -.
DR MINT; MINT-8377176; -.
DR STRING; 69014.TK1796; -.
DR EnsemblBacteria; BAD85985; BAD85985; TK1796.
DR GeneID; 3233803; -.
DR KEGG; tko:TK1796; -.
DR eggNOG; COG0174; -.
DR HOGENOM; HOG000005156; -.
DR KO; K01915; -.
DR OMA; FAEGTMF; -.
DR ProtClustDB; CLSK491907; -.
DR BioCyc; TKOD69014:GH72-1833-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004356; F:glutamate-ammonia ligase activity; IEA:EC.
DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR GO; GO:0009399; P:nitrogen fixation; IEA:InterPro.
DR Gene3D; 3.10.20.70; -; 1.
DR Gene3D; 3.30.590.10; -; 1.
DR InterPro; IPR008147; Gln_synt_beta.
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; IPR004809; Gln_synth_I.
DR InterPro; IPR027302; Gln_synth_N_conserv_site.
DR Pfam; PF00120; Gln-synt_C; 1.
DR Pfam; PF03951; Gln-synt_N; 1.
DR SUPFAM; SSF54368; Gln_synt_beta; 1.
DR TIGRFAMs; TIGR00653; GlnA; 1.
DR PROSITE; PS00180; GLNA_1; 1.
DR PROSITE; PS00181; GLNA_ATP; 1.
PE 3: Inferred from homology;
KW ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1 443 Glutamine synthetase.
FT /FTId=PRO_0000153211.
FT MOD_RES 362 362 O-AMP-tyrosine (By similarity).
FT CONFLICT 402 402 Y -> N (in Ref. 1; BAA20530).
SQ SEQUENCE 443 AA; 50308 MW; 94357E45D5F18168 CRC64;
MNEIKGIERA VQVEVPRPRF LLLAFTDING SLKGMEIPME RYEEAVEDGV SFDGSSIPGF
EGIEDSDLIF KADPSTYAEI PWEGIGRVYG YIYKGDEPYQ ADPRGILKRV LERLEKEGLK
AHIGPEPEFY IFKKNGTWEL HIPDSGGYFD LVGLDKAREI RREIALYMPY LGLKPEVLHH
EVGKAQHEID FRYDEALRTA DNIVSFKHVV KAVAELHGYY ATFMPKPIYG FPGNGMHLHI
SLWKDGENVF IGEDGLSDTA LHFIGGILKH AKALAALTNP TVNSYKRLVP GYEAPVYISW
GYRNRSALIR VPAFKGSGAR IEYRCPDPSA NPYLALAGIL MVGLDGIKKK VEPDSYVETN
VYEMDDAERE RLGIDTLPGS LGEALEELKK DKTVREALGG AYKNFIDYKE REWEEYIEYL
SSRDIPIDTK KVTEWELERY FYV
//
