ID   GUAA_BORGP              Reviewed;         528 AA.
AC   Q6ASN4;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=GMP synthase [glutamine-hydrolyzing] {ECO:0000255|HAMAP-Rule:MF_00344};
DE            EC=6.3.5.2 {ECO:0000255|HAMAP-Rule:MF_00344};
DE   AltName: Full=GMP synthetase {ECO:0000255|HAMAP-Rule:MF_00344};
DE   AltName: Full=Glutamine amidotransferase {ECO:0000255|HAMAP-Rule:MF_00344};
GN   Name=guaA {ECO:0000255|HAMAP-Rule:MF_00344}; OrderedLocusNames=BGB17;
OS   Borrelia garinii subsp. bavariensis (strain ATCC BAA-2496 / DSM 23469 /
OS   PBi) (Borrelia bavariensis).
OG   Plasmid cp26.
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=290434;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2496 / DSM 23469 / PBi;
RX   PubMed=15547252; DOI=10.1093/nar/gkh953;
RA   Gloeckner G., Lehmann R., Romualdi A., Pradella S., Schulte-Spechtel U.,
RA   Schilhabel M., Wilske B., Suehnel J., Platzer M.;
RT   "Comparative analysis of the Borrelia garinii genome.";
RL   Nucleic Acids Res. 32:6038-6046(2004).
CC   -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000255|HAMAP-
CC       Rule:MF_00344}.
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_00344};
CC   -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC       route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00344}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00344}.
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DR   EMBL; CP000014; AAT93750.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6ASN4; -.
DR   SMR; Q6ASN4; -.
DR   EnsemblBacteria; AAT93750; AAT93750; BGB17.
DR   KEGG; bga:BGB17; -.
DR   HOGENOM; CLU_014340_0_5_12; -.
DR   OMA; KRKIIGH; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000002276; 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.
FT   CHAIN           1..528
FT                   /note="GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_0000229408"
FT   DOMAIN          22..212
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   DOMAIN          213..403
FT                   /note="GMPS ATP-PPase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   ACT_SITE        99
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   ACT_SITE        186
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   ACT_SITE        188
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   BINDING         240..246
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
SQ   SEQUENCE   528 AA;  60392 MW;  E2A007F263D3F9A0 CRC64;
     MKYALIRKLL FVLRTYMMNV RAILVLDFGS QYSQLIARRI REIGVYTKVI PYYTPLKEIK
     NMNIAGIILS GGPASVYAKD APTLNMEIFN LKIPVLGICY GMQLIVKLFG GLVSKDYKQE
     YGSSEIFLKN EKSLLFSELP NKFQIIMSHG DSIEKIPNNF KQLAFTKNCI ASISNEDQKI
     YGLQFHPEVT HSEFGDQILK NFVFKICQSQ TNWSLESNVE TIVEKIKLKV GSKKVILGLS
     GGTDSLVCAL LIKKAIKENL ICVFVNTGLL RKNEDKKILE LKHQYDLNIK YIDASEKFLN
     YLKNISDPEE KRKIIGKEFV NVFEKITLED QNIEYLAQGT IYSDVIESKS KNNASSKIKS
     HHNVGGLPDK MRLKLLEPLN EFFKDEIIQI GINLGIKKEA LYRHPFPGPG LAIRIIGEVT
     QEKINILQEA ENILTEELFT NDLYYEIRQA FVVLLPVKSV GVMGDQRTYE YTAVIRCVNT
     QDFMTAEWTE LPYNFLRKVS SRIINEVRGI NRVCYDISSK PPSTIEWE