ID   GUAA_FRATO              Reviewed;         516 AA.
AC   Q0BLV0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=GMP synthase [glutamine-hydrolyzing] {ECO:0000255|HAMAP-Rule:MF_00344};
DE            EC=6.3.5.2 {ECO:0000255|HAMAP-Rule:MF_00344};
DE   AltName: Full=GMP synthetase {ECO:0000255|HAMAP-Rule:MF_00344};
DE   AltName: Full=Glutamine amidotransferase {ECO:0000255|HAMAP-Rule:MF_00344};
GN   Name=guaA {ECO:0000255|HAMAP-Rule:MF_00344}; OrderedLocusNames=FTH_1046;
OS   Francisella tularensis subsp. holarctica (strain OSU18).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=393011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OSU18;
RX   PubMed=16980500; DOI=10.1128/jb.00506-06;
RA   Petrosino J.F., Xiang Q., Karpathy S.E., Jiang H., Yerrapragada S., Liu Y.,
RA   Gioia J., Hemphill L., Gonzalez A., Raghavan T.M., Uzman A., Fox G.E.,
RA   Highlander S., Reichard M., Morton R.J., Clinkenbeard K.D., Weinstock G.M.;
RT   "Chromosome rearrangement and diversification of Francisella tularensis
RT   revealed by the type B (OSU18) genome sequence.";
RL   J. Bacteriol. 188:6977-6985(2006).
CC   -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000255|HAMAP-
CC       Rule:MF_00344}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00344};
CC   -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC       route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00344}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00344}.
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DR   EMBL; CP000437; ABI82934.1; -; Genomic_DNA.
DR   RefSeq; WP_010031593.1; NC_017463.1.
DR   AlphaFoldDB; Q0BLV0; -.
DR   SMR; Q0BLV0; -.
DR   MEROPS; C26.957; -.
DR   KEGG; fth:FTH_1046; -.
DR   OMA; KRKIIGH; -.
DR   UniPathway; UPA00189; UER00296.
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   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
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; IPR022310; NAD/GMP_synthase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF00117; GATase; 1.
DR   Pfam; PF00958; GMP_synt_C; 1.
DR   Pfam; PF02540; NAD_synthase; 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.
FT   CHAIN           1..516
FT                   /note="GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_1000120306"
FT   DOMAIN          8..198
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   DOMAIN          199..391
FT                   /note="GMPS ATP-PPase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   ACT_SITE        84
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   ACT_SITE        172
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   ACT_SITE        174
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   BINDING         226..232
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
SQ   SEQUENCE   516 AA;  57668 MW;  AB42554BEA2E585F CRC64;
     MTDIHNHKIL ILDFGSQYTQ LIARRVREVG VFCEIFPHDV AADFIKNYQA KGIILSGGPE
     SVYDSDVKAP EIVFELGVPV LGICYGMQTM VMQHGGEVKG ADQSEFGKAI INILNLTNNI
     FSNMEHEQLV WMSHSDKVTQ TGEHFEIIAS STNAPVAAVA HKNKPFFGVQ FHPETTHTEN
     GKQIIENFVV NICGCDTLWN IENIIENDIK EIKQKVGTDK VILGLSGGVD SSVVAAILHQ
     AIGDQLTCIF VDTGLLRLNE GDQVMQVFAE HMDINVIRIN AKNRFLDALR GICDPEQKRK
     IIGKLFVDIF DEEAAKIENA KWLAQGTIYS DVIESAGNNQ SKAHVIKSHH NVGGLPKEMK
     LKLLEPLREL FKDEVRKLGL GLGLPYNMLY RHPFPGPGLG VRILGEIKKE YVETLQKADA
     IFTEELYKHN LYHDVSQAFG VFLPIKSVGV VGDQRRYEYV IALRAVVSID FMTATWANLP
     YDFLSLVSNR IVNEVKQVSR VVYDVTGKPP GTIEWE