ID   GUAA_THEMA              Reviewed;         501 AA.
AC   Q9X2E0;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=GMP synthase [glutamine-hydrolyzing];
DE            EC=6.3.5.2;
DE   AltName: Full=GMP synthetase;
DE   AltName: Full=Glutamine amidotransferase;
GN   Name=guaA; OrderedLocusNames=TM_1820;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
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: Homodimer. {ECO:0000250}.
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DR   EMBL; AE000512; AAD36883.1; -; Genomic_DNA.
DR   PIR; G72206; G72206.
DR   RefSeq; NP_229617.1; NC_000853.1.
DR   RefSeq; WP_004082366.1; NZ_CP011107.1.
DR   AlphaFoldDB; Q9X2E0; -.
DR   SMR; Q9X2E0; -.
DR   STRING; 243274.THEMA_05095; -.
DR   MEROPS; C26.957; -.
DR   EnsemblBacteria; AAD36883; AAD36883; TM_1820.
DR   KEGG; tma:TM1820; -.
DR   eggNOG; COG0518; Bacteria.
DR   eggNOG; COG0519; Bacteria.
DR   InParanoid; Q9X2E0; -.
DR   OMA; KRKIIGH; -.
DR   OrthoDB; 504464at2; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000008183; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003921; F:GMP synthase activity; IBA:GO_Central.
DR   GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR   GO; GO:0004810; F:tRNA adenylyltransferase activity; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006177; P:GMP biosynthetic process; IBA:GO_Central.
DR   CDD; cd01742; GATase1_GMP_Synthase; 1.
DR   CDD; cd01997; GMP_synthase_C; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   HAMAP; MF_00344; GMP_synthase; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR001674; GMP_synth_C.
DR   InterPro; IPR004739; GMP_synth_GATase.
DR   InterPro; IPR022955; GMP_synthase.
DR   InterPro; IPR025777; GMPS_ATP_PPase_dom.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR020536; ThiI_AANH.
DR   Pfam; PF00117; GATase; 1.
DR   Pfam; PF00958; GMP_synt_C; 1.
DR   Pfam; PF02568; ThiI; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   TIGRFAMs; TIGR00884; guaA_Cterm; 1.
DR   TIGRFAMs; TIGR00888; guaA_Nterm; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
DR   PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Glutamine amidotransferase; GMP biosynthesis; Ligase;
KW   Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT   CHAIN           1..501
FT                   /note="GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_0000140197"
FT   DOMAIN          1..185
FT                   /note="Glutamine amidotransferase type-1"
FT   DOMAIN          186..376
FT                   /note="GMPS ATP-PPase"
FT   ACT_SITE        75
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        159
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        161
FT                   /evidence="ECO:0000250"
FT   BINDING         213..219
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   501 AA;  57040 MW;  56E7EEB3FC587090 CRC64;
     MVLVVDYGSQ YSRLITRRIR ENEVYSEVVF PDDKVDLSKV DAVILSGGPR SVYEEDAPKL
     PEWFQEYKGP VLAICYGMQL IVKELGGEVR RGRGEYGRTL VELSRDPIFE GIPEKVHVWM
     SHGDEVVRLP EGFHPIAVSE TGVIAAATDG KRFWLLQFHP EVHHTEYGDR MISNFLFNVC
     KLEKNWKIGD LVEEKIRHIK ETIGNKKAIL ALSGGVDSSV AAVLVHRAIG KNLVCVFVDH
     GLLRKNEREE VERVFKEHFD MNLVVVDARK RFLEKLRGVT DPEKKRKIIG EEFIRVFEEE
     AKKHDVEFLV QGTIYSDVIE SAASGKTTAK IKSHHNVGGL PEKMNLKLVE PLRDLFKDEV
     RKVGKYLGIP DRIINRHPFP GPGLAVRVLG EVTEEKLEIL READYIFIET LRKHDYYDKV
     WQAFAVLLPI KSVGVKGDAR AYEYVVALRA VNSVEGMTAD WSRIPHDILD EAARRITREV
     KGVGRVVYDI TSKPPATIEW E