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 01-MAY-2013, entry version 77.
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; FWGMNGS; -.
DR ProtClustDB; CLSK491907; -.
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: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.
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
//
