ID   GUAA_THEP1              Reviewed;         501 AA.
AC   A5ILP6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=Tpet_1105;
OS   Thermotoga petrophila (strain ATCC BAA-488 / DSM 13995 / JCM 10881 /
OS   RKU-1).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=390874;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-488 / DSM 13995 / JCM 10881 / RKU-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT   "Complete sequence of Thermotoga petrophila RKU-1.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000702; ABQ47119.1; -; Genomic_DNA.
DR   RefSeq; WP_011943643.1; NC_009486.1.
DR   AlphaFoldDB; A5ILP6; -.
DR   SMR; A5ILP6; -.
DR   STRING; 390874.Tpet_1105; -.
DR   EnsemblBacteria; ABQ47119; ABQ47119; Tpet_1105.
DR   KEGG; tpt:Tpet_1105; -.
DR   eggNOG; COG0518; Bacteria.
DR   eggNOG; COG0519; Bacteria.
DR   HOGENOM; CLU_014340_0_5_0; -.
DR   OMA; KRKIIGH; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000006558; 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   GO; GO:0004810; F:tRNA adenylyltransferase 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; 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.
FT   CHAIN           1..501
FT                   /note="GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_1000120446"
FT   DOMAIN          1..185
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   DOMAIN          186..376
FT                   /note="GMPS ATP-PPase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   ACT_SITE        75
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   ACT_SITE        159
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   ACT_SITE        161
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   BINDING         213..219
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
SQ   SEQUENCE   501 AA;  57070 MW;  2422D9FC221F2E5F CRC64;
     MVLVVDYGSQ YSRLITRRIR ENEVYSEVVF PDDKVDLSKV DTVILSGGPR 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