ID   GUAAB_SULTO             Reviewed;         370 AA.
AC   Q96Y23; F9VPE2;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=GMP synthase [glutamine-hydrolyzing] subunit B;
DE            EC=6.3.5.2;
DE   AltName: Full=GMP synthetase;
GN   Name=guaAB; OrderedLocusNames=STK_23450;
OS   Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS   (Sulfolobus tokodaii).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfurisphaera.
OX   NCBI_TaxID=273063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX   PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA   Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA   Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA   Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA   Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT   "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT   Sulfolobus tokodaii strain7.";
RL   DNA Res. 8:123-140(2001).
CC   -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2
CC         H(+) + L-glutamate; Xref=Rhea:RHEA:11680, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58115,
CC         ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.2;
CC   -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC       route): step 1/1.
CC   -!- SUBUNIT: Heterodimer composed of a glutamine amidotransferase subunit
CC       (A) and a GMP-binding subunit (B). {ECO:0000305}.
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DR   EMBL; BA000023; BAK54789.1; -; Genomic_DNA.
DR   RefSeq; WP_010980429.1; NC_003106.2.
DR   AlphaFoldDB; Q96Y23; -.
DR   SMR; Q96Y23; -.
DR   STRING; 273063.STK_23450; -.
DR   EnsemblBacteria; BAK54789; BAK54789; STK_23450.
DR   GeneID; 1460427; -.
DR   KEGG; sto:STK_23450; -.
DR   PATRIC; fig|273063.9.peg.2649; -.
DR   eggNOG; arCOG00085; Archaea.
DR   OMA; EGGIKSH; -.
DR   OrthoDB; 31932at2157; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000001015; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR   CDD; cd01997; GMP_synthase_C; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00345; GMP_synthase_B; 1.
DR   InterPro; IPR001674; GMP_synth_C.
DR   InterPro; IPR026598; GMP_synthase_B.
DR   InterPro; IPR025777; GMPS_ATP_PPase_dom.
DR   InterPro; IPR022310; NAD/GMP_synthase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF00958; GMP_synt_C; 1.
DR   Pfam; PF02540; NAD_synthase; 1.
DR   PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; GMP biosynthesis; Ligase; Nucleotide-binding;
KW   Purine biosynthesis; Reference proteome.
FT   CHAIN           1..370
FT                   /note="GMP synthase [glutamine-hydrolyzing] subunit B"
FT                   /id="PRO_0000140252"
FT   DOMAIN          3..189
FT                   /note="GMPS ATP-PPase"
FT   BINDING         29..35
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   370 AA;  41880 MW;  B6ACB69CFB21F273 CRC64;
     MSFDPQKFVD EISPQLKEIV DGRAIAAVSG GVDSTTAAVL SYKILGDKVI PVMIDTGFLR
     ENEAENVKNM LKDLMPLQVI DEREKFISSL EGMSDAEEKR KKFRQLFYDT LSRIVKEFNA
     KYLIQGTIAA DWVETQGGIK TQHNVLVQLG IDTEKEWGFK VVEPLADLYK DEVRALAKYL
     GLPRDIYNRQ PFPGPGLLVR VVGKLTREKL EILRKVTTTV EKNLSELNLS QYFAVIFDSA
     AEYNKELSNE VGCDVKVYKT LATGVKGDVR AYGNIAGIEC RKDYESLREI MEKLTSYNIT
     HVVVKIKDKN PEGIYTIGIR AVNTQDFMTA DFAKINWNIL EKIANEINDK KIKEVVYDIT
     TKPPATIEYE