ID   GUAAB_THEKO             Reviewed;         307 AA.
AC   Q5JFM1;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=GMP synthase [glutamine-hydrolyzing] subunit B {ECO:0000255|HAMAP-Rule:MF_00345};
DE            EC=6.3.5.2 {ECO:0000255|HAMAP-Rule:MF_00345};
DE   AltName: Full=GMP synthetase {ECO:0000255|HAMAP-Rule:MF_00345};
GN   Name=guaAB {ECO:0000255|HAMAP-Rule:MF_00345}; OrderedLocusNames=TK0193;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
CC   -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000255|HAMAP-
CC       Rule:MF_00345}.
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_00345};
CC   -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC       route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00345}.
CC   -!- SUBUNIT: Heterodimer composed of a glutamine amidotransferase subunit
CC       (A) and a GMP-binding subunit (B). {ECO:0000255|HAMAP-Rule:MF_00345}.
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DR   EMBL; AP006878; BAD84382.1; -; Genomic_DNA.
DR   RefSeq; WP_011249148.1; NC_006624.1.
DR   AlphaFoldDB; Q5JFM1; -.
DR   SMR; Q5JFM1; -.
DR   IntAct; Q5JFM1; 1.
DR   MINT; Q5JFM1; -.
DR   STRING; 69014.TK0193; -.
DR   EnsemblBacteria; BAD84382; BAD84382; TK0193.
DR   GeneID; 3233684; -.
DR   KEGG; tko:TK0193; -.
DR   PATRIC; fig|69014.16.peg.192; -.
DR   eggNOG; arCOG00085; Archaea.
DR   HOGENOM; CLU_014340_0_0_2; -.
DR   InParanoid; Q5JFM1; -.
DR   OMA; EGGIKSH; -.
DR   OrthoDB; 31932at2157; -.
DR   PhylomeDB; Q5JFM1; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000000536; 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:0006177; P:GMP biosynthetic process; IBA:GO_Central.
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; 2.
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..307
FT                   /note="GMP synthase [glutamine-hydrolyzing] subunit B"
FT                   /id="PRO_0000140250"
FT   DOMAIN          1..184
FT                   /note="GMPS ATP-PPase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00345"
FT   BINDING         27..33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00345"
SQ   SEQUENCE   307 AA;  34467 MW;  725077FE88F5EF99 CRC64;
     MWENFIEEKV KEIRETVGDG KAIIALSGGV DSSTAAVLAH RAIGDRLHAV FVNTGFMRKG
     EPEFVVKTFR DEFGLNLHYV DASERFFREL KGVTDPEEKR KIIGRVFIEV FEEVAKEINA
     DFLIQGTIAP DWIESHGKIK SHHNVGGLPE RLNLKLIEPL RDLYKDEVRE LAKELGLPEK
     IYNRMPFPGP GLAVRVLGEV TPERVAIVRE ANAIVEEEIE KAGLKPWQAF AVLLGVKTVG
     VQGDIRAYKE TVAVRVVESL DGMTANAMNV PWEVLQRIAF RITSEIPEVG RVLYDITNKP
     PATIEFE