ID   GUAA_BORBU              Reviewed;         511 AA.
AC   P0CL64; O30439; P49056;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   03-AUG-2022, entry version 52.
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=BB_B18;
OS   Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS   (Borrelia burgdorferi).
OG   Plasmid cp26 (circular 26 kb).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CA-11.2A;
RX   PubMed=7961392; DOI=10.1128/jb.176.21.6427-6432.1994;
RA   Margolis N., Hogan D., Tilly K., Rosa P.;
RT   "Plasmid location of Borrelia purine biosynthesis gene homologs.";
RL   J. Bacteriol. 176:6427-6432(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA   Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA   Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA   van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA   Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA   Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA   Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL   Nature 390:580-586(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-98.
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=9352937; DOI=10.1128/jb.179.21.6837-6842.1997;
RA   Sohaskey C.D., Arnold C., Barbour A.G.;
RT   "Analysis of promoters in Borrelia burgdorferi by use of a transiently
RT   expressed reporter gene.";
RL   J. Bacteriol. 179:6837-6842(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13.
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAA53232.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; L25883; AAA53232.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE000792; AAC66313.2; -; Genomic_DNA.
DR   EMBL; AF005937; AAC45804.1; -; Genomic_DNA.
DR   EMBL; U93693; AAC45520.1; -; Genomic_DNA.
DR   PIR; F70218; F70218.
DR   RefSeq; NP_047004.2; NC_001903.1.
DR   RefSeq; WP_010890581.1; NC_001903.1.
DR   AlphaFoldDB; P0CL64; -.
DR   SMR; P0CL64; -.
DR   MEROPS; C26.957; -.
DR   PRIDE; P0CL64; -.
DR   EnsemblBacteria; AAC66313; AAC66313; BB_B18.
DR   KEGG; bbu:BB_B18; -.
DR   PATRIC; fig|224326.49.peg.1606; -.
DR   HOGENOM; CLU_014340_0_5_12; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000001807; Plasmid cp26.
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; Reference proteome.
FT   CHAIN           1..511
FT                   /note="GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_0000140099"
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"
FT   VARIANT         3
FT                   /note="T -> A (in strain: CA-11.2A)"
FT   VARIANT         68
FT                   /note="N -> D (in strain: CA-11.2A)"
FT   VARIANT         78
FT                   /note="I -> V (in strain: CA-11.2A)"
FT   VARIANT         106
FT                   /note="S -> R (in strain: CA-11.2A)"
FT   VARIANT         112
FT                   /note="R -> K (in strain: CA-11.2A)"
FT   VARIANT         182
FT                   /note="I -> L (in strain: CA-11.2A)"
FT   VARIANT         258
FT                   /note="D -> N (in strain: CA-11.2A)"
SQ   SEQUENCE   511 AA;  58064 MW;  999D928F605F8C6B CRC64;
     MNTQAILVLD FGSQYSQLIA RRIREIGVYT KVIPYYTPLK EIKNMNISGI ILSGSPASVY
     SKEAPTLNME IFNLKIPILG ICYGMQIIVK LFGGLVSKDS KQEYGSSEIF LRDEKSLLFS
     ELPNKFQIIM SHGDSIEKIP DNFKQLAFTK NCIASISNET QKIYGLQFHP EVTHSEFGDQ
     IIKNFVFKIC QAQINWSLEG NLETIVKKIK LKVGSKKVIL GLSGGTDSLV CALLIKKAIN
     ENLICVFVNT GLLRKNEDKK 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