ID   GUAA_POLNS              Reviewed;         535 AA.
AC   B1XTW6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=Pnec_0530;
OS   Polynucleobacter necessarius subsp. necessarius (strain STIR1).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Polynucleobacter.
OX   NCBI_TaxID=452638;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=STIR1;
RX   PubMed=24167248; DOI=10.1073/pnas.1316687110;
RA   Boscaro V., Felletti M., Vannini C., Ackerman M.S., Chain P.S.,
RA   Malfatti S., Vergez L.M., Shin M., Doak T.G., Lynch M., Petroni G.;
RT   "Polynucleobacter necessarius, a model for genome reduction in both free-
RT   living and symbiotic bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:18590-18595(2013).
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; CP001010; ACB43793.1; -; Genomic_DNA.
DR   RefSeq; WP_012357560.1; NC_010531.1.
DR   AlphaFoldDB; B1XTW6; -.
DR   SMR; B1XTW6; -.
DR   STRING; 452638.Pnec_0530; -.
DR   MEROPS; C26.957; -.
DR   PRIDE; B1XTW6; -.
DR   EnsemblBacteria; ACB43793; ACB43793; Pnec_0530.
DR   KEGG; pne:Pnec_0530; -.
DR   eggNOG; COG0518; Bacteria.
DR   eggNOG; COG0519; Bacteria.
DR   HOGENOM; CLU_014340_0_5_4; -.
DR   OMA; KRKIIGH; -.
DR   OrthoDB; 504464at2; -.
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; Purine biosynthesis.
FT   CHAIN           1..535
FT                   /note="GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_1000120354"
FT   DOMAIN          4..210
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   DOMAIN          211..403
FT                   /note="GMPS ATP-PPase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   ACT_SITE        85
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   ACT_SITE        184
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   ACT_SITE        186
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   BINDING         238..244
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
SQ   SEQUENCE   535 AA;  59019 MW;  9C45A051C02796BE CRC64;
     MHDKILILDF GSQVTQLIAR RVRDGRVYSE IHPYDCDPEL IRKFIQEQGG KGIILSGGPS
     SVTEEGSPRA PQIVFELGVP VLGICYGMQT MATQLGGAVA SAESLGKARE FGYSEVRAHG
     HTNLLKGIQD FSTSEGHGIL KVWMSHGDSV TTLPSSFKLM ASTESCPIAG MADEERSFYA
     FQFHPEVTHT IQGTAIIERF VHEICKCKPD WVMGDYIAEA VENIRKQVGD EEVILGLSGG
     VDSSVAAALI HRAIGDQLTC VFVDHGLLRL NEGDMVMEMF ARNLGVKVIR VDAKETFMGE
     LAGVSDPEAK RKIIGKEFVE IFQAESGKIK NAKWLAQGTI YPDVIESAGK GKKGAHTIKS
     HHNVGGLPED MHLKLLEPLR ELFKDEVREL GVALGLPREM VYRHPFPGPG LGVRILGEVK
     AEFASLLQRA DAIFIEELRN TIDEVSQKSW YDLTSQAFAV FLPVKSVGVM GDGRTYEYVV
     ALRAVQTQDF MTAHWAHLPH ELLGKVFNRI INEVRGINRV VYDISGKPPA TIEWE