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Database: UniProt
Entry: O58097
LinkDB: O58097
Original site: O58097 
ID   GLN1A_PYRHO             Reviewed;         443 AA.
AC   O58097;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   12-APR-2017, entry version 93.
DE   RecName: Full=Glutamine synthetase {ECO:0000250|UniProtKB:Q9HH09};
DE            Short=GS {ECO:0000250|UniProtKB:Q9HH09};
DE            EC=6.3.1.2 {ECO:0000250|UniProtKB:Q9HH09};
DE   AltName: Full=Glutamate--ammonia ligase {ECO:0000250|UniProtKB:Q9HH09};
DE   AltName: Full=Glutamine synthetase I alpha {ECO:0000250|UniProtKB:Q9HH09};
DE            Short=GSI alpha {ECO:0000250|UniProtKB:Q9HH09};
GN   Name=glnA {ECO:0000250|UniProtKB:Q9HH09}; OrderedLocusNames=PH0359;
GN   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   -!- FUNCTION: Probably involved in nitrogen metabolism via ammonium
CC       assimilation. Catalyzes the ATP-dependent biosynthesis of
CC       glutamine from glutamate and ammonia.
CC       {ECO:0000250|UniProtKB:Q9HH09}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamate + NH(3) = ADP + phosphate +
CC       L-glutamine. {ECO:0000250|UniProtKB:Q9HH09}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q9HH09};
CC       Note=Binds 2 Mg(2+) ions per subunit.
CC       {ECO:0000250|UniProtKB:P9WN39};
CC   -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two
CC       hexagons. {ECO:0000250|UniProtKB:Q9HH09}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9HH09}.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC       {ECO:0000250|UniProtKB:Q9HH09}.
DR   EMBL; BA000001; BAA29433.1; -; Genomic_DNA.
DR   PIR; D71143; D71143.
DR   ProteinModelPortal; O58097; -.
DR   SMR; O58097; -.
DR   STRING; 70601.PH0359; -.
DR   PRIDE; O58097; -.
DR   EnsemblBacteria; BAA29433; BAA29433; BAA29433.
DR   KEGG; pho:PH0359; -.
DR   eggNOG; arCOG01909; Archaea.
DR   eggNOG; COG0174; LUCA.
DR   HOGENOM; HOG000005156; -.
DR   KO; K01915; -.
DR   OMA; MGFTCYT; -.
DR   OrthoDB; POG093Z00GE; -.
DR   Proteomes; UP000000752; Chromosome.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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_b-grasp.
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   SMART; SM01230; Gln-synt_C; 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; Magnesium;
KW   Metal-binding; Nucleotide-binding.
FT   CHAIN         1    443       Glutamine synthetase.
FT                                /FTId=PRO_0000153210.
FT   NP_BIND     239    241       ATP. {ECO:0000250|UniProtKB:P9WN39}.
FT   METAL       126    126       Magnesium 1.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
FT   METAL       128    128       Magnesium 2.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
FT   METAL       181    181       Magnesium 2.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
FT   METAL       188    188       Magnesium 2.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
FT   METAL       237    237       Magnesium 1; via pros nitrogen.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
FT   METAL       322    322       Magnesium 1.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
FT   BINDING     176    176       ATP. {ECO:0000250|UniProtKB:P9WN39}.
FT   BINDING     233    233       L-glutamate; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P12425}.
FT   BINDING     241    241       ATP. {ECO:0000250|UniProtKB:P77961}.
FT   BINDING     287    287       L-glutamate.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
FT   BINDING     293    293       L-glutamate.
FT                                {ECO:0000250|UniProtKB:P0A1P6}.
FT   BINDING     305    305       ATP. {ECO:0000250|UniProtKB:P9WN39}.
FT   BINDING     305    305       L-glutamate.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
FT   BINDING     310    310       ATP. {ECO:0000250|UniProtKB:P9WN39}.
FT   BINDING     324    324       L-glutamate.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
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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