ID   GUAA_BORBN              Reviewed;         511 AA.
AC   E4QHI6; O30439; P49056;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 57.
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; OrderedLocusNames=BbuN40_B18;
OS   Borreliella burgdorferi (strain N40) (Borrelia burgdorferi).
OG   Plasmid cp26 (circular 26 kb), and Plasmid N40_cp26.
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=521007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N40; PLASMID=N40_cp26;
RX   PubMed=20935092; DOI=10.1128/jb.01158-10;
RA   Schutzer S.E., Fraser-Liggett C.M., Casjens S.R., Qiu W.G., Dunn J.J.,
RA   Mongodin E.F., Luft B.J.;
RT   "Whole-genome sequences of thirteen isolates of Borrelia burgdorferi.";
RL   J. Bacteriol. 193:1018-1020(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13.
RC   STRAIN=N40; PLASMID=cp26 (circular 26 kb);
RX   PubMed=9282748; DOI=10.1046/j.1365-2958.1997.4711838.x;
RA   Tilly K., Casjens S., Stevenson B., Bono J.L., Samuels D.S., Hogan D.,
RA   Rosa P.;
RT   "The Borrelia burgdorferi circular plasmid cp26: conservation of plasmid
RT   structure and targeted inactivation of the ospC gene.";
RL   Mol. Microbiol. 25:361-374(1997).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002239; ADQ30075.1; -; Genomic_DNA.
DR   EMBL; U04240; AAC45539.1; -; Genomic_DNA.
DR   RefSeq; WP_010256184.1; NC_017401.1.
DR   AlphaFoldDB; E4QHI6; -.
DR   SMR; E4QHI6; -.
DR   MEROPS; C26.957; -.
DR   KEGG; bbn:BbuN40_B18; -.
DR   PATRIC; fig|521007.3.peg.1199; -.
DR   HOGENOM; CLU_014340_0_5_12; -.
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; Plasmid; Purine biosynthesis.
FT   CHAIN           1..511
FT                   /note="GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_0000406311"
FT   DOMAIN          5..195
FT                   /note="Glutamine amidotransferase type-1"
FT   DOMAIN          196..386
FT                   /note="GMPS ATP-PPase"
FT   ACT_SITE        82
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        169
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        171
FT                   /evidence="ECO:0000250"
FT   BINDING         223..229
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   511 AA;  58061 MW;  D8DCB6581DC5332A CRC64;
     MNAQAILVLD FGSQYSQLIA RRIREIGVYT KVIPYYTPLK EIKNMNISGI ILSGSPASVY
     SKEAPTLDME IFNLKIPVLG ICYGMQIIVK LFGGLVSKDS KQEYGRSEIF LKDEKSLLFS
     ELPNKFQIIM SHGDSIEKIP DNFKQLAFTK NCIASISNET QKIYGLQFHP EVTHSEFGDQ
     ILKNFVFKIC QAQINWSLEG NLETIVKKIK LKVGSKKVIL GLSGGTDSLV CALLIKKAIN
     ENLICVFVNT GLLRKNENKK ILELKHQYDL NIKYIDASTK FLNRLKNISD PEEKRKIIGK
     EFVDVFEKIT LEDQNIEYLA QGTIYSDVIE SKSKDSSSSK IKSHHNVGGL PDKMSLKLLE
     PLNEFFKDEI IQIGINLGIK KESLYRHPFP GPGLAIRIIG EVTQEKINIL QEADNILTEE
     LFINDLYYQI RQAFVVLLPV KSVGVMGDQR TYEYTAVIRC VNTQDFMTAE WTELPYSFLK
     KVSSRIINEV RGINRVCYDI SSKPPSTIEW E