ID   GUAA_LEPIC              Reviewed;         603 AA.
AC   Q72RB7;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Probable GMP synthase [glutamine-hydrolyzing];
DE            EC=6.3.5.2;
DE   AltName: Full=GMP synthetase;
DE   AltName: Full=Glutamine amidotransferase;
GN   Name=guaA; OrderedLocusNames=LIC_11831;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni
OS   (strain Fiocruz L1-130).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=267671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fiocruz L1-130;
RX   PubMed=15028702; DOI=10.1128/jb.186.7.2164-2172.2004;
RA   Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B.,
RA   Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V.,
RA   Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L.,
RA   Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S., Ferro M.I.T.,
RA   Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H.,
RA   Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M.,
RA   Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L.,
RA   Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A.,
RA   Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A.,
RA   Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A.;
RT   "Comparative genomics of two Leptospira interrogans serovars reveals novel
RT   insights into physiology and pathogenesis.";
RL   J. Bacteriol. 186:2164-2172(2004).
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; AE016823; AAS70417.1; -; Genomic_DNA.
DR   RefSeq; WP_000234667.1; NC_005823.1.
DR   AlphaFoldDB; Q72RB7; -.
DR   SMR; Q72RB7; -.
DR   MEROPS; C26.957; -.
DR   PaxDb; Q72RB7; -.
DR   EnsemblBacteria; AAS70417; AAS70417; LIC_11831.
DR   GeneID; 61141728; -.
DR   KEGG; lic:LIC_11831; -.
DR   HOGENOM; CLU_014340_0_2_12; -.
DR   OMA; KRKIIGH; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000007037; Chromosome I.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
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   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR001674; GMP_synth_C.
DR   InterPro; IPR004739; GMP_synth_GATase.
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; 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..603
FT                   /note="Probable GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_0000140141"
FT   DOMAIN          6..195
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   DOMAIN          196..392
FT                   /note="GMPS ATP-PPase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00886"
FT   ACT_SITE        81
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        170
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        172
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   BINDING         224..230
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00886"
SQ   SEQUENCE   603 AA;  67913 MW;  9C8920DEEA2C41B7 CRC64;
     MVIHKKIAVV DFGGQYAHLI ASRIRRLGAY TEILSNEEPI SNYQKYSGII LSGGPESVYE
     PNSPTVTTRI FDLGIPILGI CYGHQLIMKL LGGVVERSGT GEYGPASLQL HGTNGNSILK
     NFVGGEQVWM NHADEVVKLP EGFSKIAFSK DCGYAVVANS SKKIFGIQFH AEVSHSEKGS
     VLLDNFIQIC GVSKTWGIDQ FLKEKIKEIQ ETVKQEQKIF MLVSGGVDST VSYLLLCKAL
     GAERVLGFLI DTGFMRKDEV VSLQKKLTFQ NIHLTVRDES SLFYKSLKDK SDPEEKRKIV
     GNLFLEARDR AVKDLDLEYG DWLLGQGTIY PDTIESGGTK HSHTIKTHHN RVEAIQKLIE
     QGKVIEPIRD LYKDEVRDLG VLLGLESEWV GRHPFPGPGL VVRMLAVEKK GTDKDQLEID
     SYLSTQDGLS GKILPIASVG VKGDRRSYAN CVVLNDIETD WNTLDRVATH LSNRFSFINR
     VVLLPFESDL KKWNFQFTGM QLDKKCSDLL READFTVESV IRKLGLYNKI WQMPVVLLPI
     GEKENEKSIV LRPVESQEAM TANFFRMERS VLQEIKIEVL KIPEIRYLFF DLTNKPPGTI
     EWE