ID   GUAA_ALKHC              Reviewed;         513 AA.
AC   Q9KF78;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Putative GMP synthase [glutamine-hydrolyzing];
DE            EC=6.3.5.2;
DE   AltName: Full=GMP synthetase;
DE   AltName: Full=Glutamine amidotransferase;
GN   Name=guaA; OrderedLocusNames=BH0607;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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}.
CC   -!- CAUTION: Gln-172 is present instead of the conserved His which is
CC       expected to be an active site residue. {ECO:0000305}.
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DR   EMBL; BA000004; BAB04326.1; -; Genomic_DNA.
DR   PIR; G83725; G83725.
DR   RefSeq; WP_010896784.1; NC_002570.2.
DR   AlphaFoldDB; Q9KF78; -.
DR   SMR; Q9KF78; -.
DR   STRING; 272558.10173221; -.
DR   MEROPS; C26.957; -.
DR   EnsemblBacteria; BAB04326; BAB04326; BAB04326.
DR   KEGG; bha:BH0607; -.
DR   eggNOG; COG0518; Bacteria.
DR   eggNOG; COG0519; Bacteria.
DR   HOGENOM; CLU_014340_0_5_9; -.
DR   OMA; KRKIIGH; -.
DR   OrthoDB; 504464at2; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000001258; 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: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; Reference proteome.
FT   CHAIN           1..513
FT                   /note="Putative GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_0000140092"
FT   DOMAIN          8..198
FT                   /note="Glutamine amidotransferase type-1"
FT   DOMAIN          199..388
FT                   /note="GMPS ATP-PPase"
FT   ACT_SITE        85
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        174
FT                   /evidence="ECO:0000250"
FT   BINDING         226..232
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   513 AA;  57328 MW;  1308CA1ED1923379 CRC64;
     MEQLSEEMIV VLDFGGQYNQ LITRRIRDLG VYSELHPNTI TAEQLKEMKP KGIIFSGGPN
     SAYAEGAPKC DPAIFDLGVP ILGICYGMQL MTQHFGGKVD AAEHREYGKA TITVENQSKL
     FQGLPVEQTV WMSHGDLIVA PPEGFVVDAQ NPSCPVAAMS DEARNYYGVQ FQPEVRHSQF
     GDDMLKNFAF AVCGCEGNWS MENFIELEME KIREQVGDKQ VLCALSGGVD SSVVAVLIHK
     AIGDQLTCMF IDHGLLRKGE ADSVMKTFSE GFNMNVIKID AKDRFLSKLE GVSDPEQKRK
     IIGNEFIYVF EEEASKLKDM DFLAQGTLYT DIIESGTATA QTIKSHHNVG GLPEDMRFEL
     IEPLNTLFKD EVRKLGTELG IPDEVVWRQP FPGPGLGIRV LGEITEEKLE IVRESDAILR
     EEIKKAGLDR EIWQYFTALP NMRSVGVMGD ARTYDYTVGI RAVTSIDGMT SDWARIPWDV
     LEIISTRIVN EVKHVNRVVY DITSKPPATI EWE