ID   GUAA_LEPIN              Reviewed;         603 AA.
AC   Q8F4F4;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   03-AUG-2022, entry version 112.
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=LA_2087;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS   56601).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=189518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=56601;
RX   PubMed=12712204; DOI=10.1038/nature01597;
RA   Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA   Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA   Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA   Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA   Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA   Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT   "Unique physiological and pathogenic features of Leptospira interrogans
RT   revealed by whole-genome sequencing.";
RL   Nature 422:888-893(2003).
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; AE010300; AAN49286.2; -; Genomic_DNA.
DR   RefSeq; NP_712268.2; NC_004342.2.
DR   RefSeq; WP_000234667.1; NC_004342.2.
DR   AlphaFoldDB; Q8F4F4; -.
DR   SMR; Q8F4F4; -.
DR   STRING; 189518.LA_2087; -.
DR   EnsemblBacteria; AAN49286; AAN49286; LA_2087.
DR   GeneID; 61141728; -.
DR   KEGG; lil:LA_2087; -.
DR   PATRIC; fig|189518.3.peg.2080; -.
DR   HOGENOM; CLU_014340_0_2_12; -.
DR   InParanoid; Q8F4F4; -.
DR   OMA; KRKIIGH; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000001408; Chromosome I.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003921; F:GMP synthase activity; IBA:GO_Central.
DR   GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006177; P:GMP biosynthetic process; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..603
FT                   /note="Probable GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_0000140142"
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   REGION          432..505
FT                   /note="Insert"
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