ID   GUAA_LACRH              Reviewed;         517 AA.
AC   O85192;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 117.
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;
OS   Lacticaseibacillus rhamnosus (Lactobacillus rhamnosus).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=47715;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=X202;
RX   PubMed=10688693; DOI=10.1007/s002849910049;
RA   Grimaldi C., Dutertre M., Simonet J.-M.;
RT   "Genetic organization and polymorphism of the guaA gene encoding the GMP
RT   synthetase in Lactobacillus rhamnosus.";
RL   Curr. Microbiol. 40:245-249(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}.
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DR   EMBL; AF051937; AAC33274.1; -; Genomic_DNA.
DR   RefSeq; WP_005712824.1; NZ_NXEU01000002.1.
DR   AlphaFoldDB; O85192; -.
DR   SMR; O85192; -.
DR   STRING; 568703.LGG_01968; -.
DR   MEROPS; C26.957; -.
DR   eggNOG; COG0519; Bacteria.
DR   BRENDA; 6.3.5.2; 2891.
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..517
FT                   /note="GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_0000140139"
FT   DOMAIN          11..202
FT                   /note="Glutamine amidotransferase type-1"
FT   DOMAIN          203..392
FT                   /note="GMPS ATP-PPase"
FT   ACT_SITE        88
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        176
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        178
FT                   /evidence="ECO:0000250"
FT   BINDING         230..236
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   517 AA;  57792 MW;  3A9D6EE91AE8B7DA CRC64;
     MANDQNKDYD KIIVLDYGSQ YNQLITRRIR EFGIYSELKP HTITAAEVKK IAPKGIIFSG
     GPNSVYDEGA LGVDEDIFKL GIPILGVCYG MQLMAQRLGG DVEPADNREY GKADIEVTDA
     SAKLFHDLPK DQTVWMSHGD LVTRVPDGFR TTATSVNCPI SAMDDDDRKF YGIQFHAEVQ
     NTQYGHEILH HFAFDVCHAE ANWSMDDFIT KQIAKIRAEV GDKRVLLGLS GGVDSSVVGV
     LLHKAIGTQL TSIFVDHGLL RKGEAEQVMD SLKGKFGLNI IKVNAKDRFL NDLRGVTDPE
     KKRKIIGRDF IEVFNEEAAK LNGIEFLAQG TLYTDVVESG TDTAQTIKSH HNVGGLPEDL
     KFKLIEPLNK LFKDEVRELG EKLGMPHSLV WRQPFPGPGL GIRVIGEVTE DKLEIVRDSD
     YILREEIAKH GLDKDIWQYF TVLPGIRSVG VMGDGRTYDY TIGIRAITSI DGMTADFARI
     DWDVLQEISS RIVNEVKHVN RVVYDITSKP PATIEWE