ID   GUAAB_ARCFU             Reviewed;         303 AA.
AC   O29986;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=GMP synthase [glutamine-hydrolyzing] subunit B;
DE            EC=6.3.5.2;
DE   AltName: Full=GMP synthetase;
GN   Name=guaAB; Synonyms=guaA-1; OrderedLocusNames=AF_0253;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
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; AE000782; AAB90977.1; -; Genomic_DNA.
DR   PIR; E69281; E69281.
DR   AlphaFoldDB; O29986; -.
DR   SMR; O29986; -.
DR   STRING; 224325.AF_0253; -.
DR   EnsemblBacteria; AAB90977; AAB90977; AF_0253.
DR   KEGG; afu:AF_0253; -.
DR   eggNOG; arCOG00085; Archaea.
DR   HOGENOM; CLU_014340_0_0_2; -.
DR   OMA; EGGIKSH; -.
DR   PhylomeDB; O29986; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000002199; 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   TIGRFAMs; TIGR00884; guaA_Cterm; 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..303
FT                   /note="GMP synthase [glutamine-hydrolyzing] subunit B"
FT                   /id="PRO_0000140237"
FT   DOMAIN          1..183
FT                   /note="GMPS ATP-PPase"
FT   BINDING         28..34
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   303 AA;  34119 MW;  FC6259333E624BC2 CRC64;
     MDVEKFVENA IKEIRERVKD GKAIIALSGG VDSSVCTVLA HKALGDRLIP VFVDTGLMRE
     GEPEKIKEIF GNMGLVFIDA KEEFFKALKG VTDPEEKRKV IGELFVRIFE RVAEEHNAEY
     LIQGTIYPDI IESQGGIKSH HNVGGFPTSY KFKDVIEPLR ELYKDEVREV ARYLGLPKEI
     SERMPFPGPG LAVRIVGEVT PEKVEIVRKA NKIVEEELAD YDKWQCFAAL IGKATGVKGD
     VRVWGYIIAV RAVESRDGMT ADPIKIDYDR LRRIALRITG EIDKVSRVVY DITPKPPATI
     EYE