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Database: UniProt
Entry: O58097
LinkDB: O58097
Original site: O58097 
ID   GLNA_PYRHO              Reviewed;         443 AA.
AC   O58097;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   14-MAY-2014, entry version 79.
DE   RecName: Full=Glutamine synthetase;
DE            Short=GS;
DE            EC=6.3.1.2;
DE   AltName: Full=Glutamate--ammonia ligase;
GN   Name=glnA; OrderedLocusNames=PH0359; ORFNames=PHAY031;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 /
OS   NBRC 100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y.,
RA   Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y.,
RA   Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K.,
RA   Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
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; BA000001; BAA29433.1; -; Genomic_DNA.
DR   PIR; D71143; D71143.
DR   RefSeq; NP_142335.1; NC_000961.1.
DR   ProteinModelPortal; O58097; -.
DR   STRING; 70601.PH0359; -.
DR   PRIDE; O58097; -.
DR   EnsemblBacteria; BAA29433; BAA29433; BAA29433.
DR   GeneID; 1444235; -.
DR   KEGG; pho:PH0359; -.
DR   eggNOG; COG0174; -.
DR   HOGENOM; HOG000005156; -.
DR   KO; K01915; -.
DR   OMA; WSGPNRS; -.
DR   BioCyc; PHOR70601:GJWR-337-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:UniProtKB-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; SSF54368; 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.
FT   CHAIN         1    443       Glutamine synthetase.
FT                                /FTId=PRO_0000153210.
FT   MOD_RES     362    362       O-AMP-tyrosine (By similarity).
SQ   SEQUENCE   443 AA;  50587 MW;  B88005ACF23E05C0 CRC64;
     MVRKVNIIKG NEGQGKRIKF VQLIFVDING MPKGMEVPIT RLEEAIEEGI AFDGSSVPGF
     QGIEDSDLVF KADPSTYVEV PWDNVARVYG YIYKDGKPYE ADPRGVLRRT LERLEKLGIK
     VYIGPEPEFY LFKKNGSWEL EIPDVGGYFD ILTLDKAKDI KREIAEYMPY FGLTPEVLHH
     EVGKAQHEID FRHDEALKTA DNIVSFKYIV KAVAEMHGLY ATFMPKPIYG MPGNGMHLHI
     SLWKDGENIF KGEEGLSETA LYFIGGLLKH AKALAAVTNP TVNSYKRLVP GYEAPVYISW
     GYKNRSALIR VPAFWGNGAR IEYRCPDPSA NSYLAFAAIL MAGLDGIKHK IEPFAYVEEN
     VYEMDEKRRE EIGIDMLPEN LGEALDELER DKVVKEALGG AYRNFVGYKR KEWEEYLDYL
     EAKNLPKDTK NVTEWELERY FFI
//
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