ID   GUAA_NEIMA              Reviewed;         521 AA.
AC   Q9JW60; A1IPY6;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 130.
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=NMA0534;
OS   Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS   Z2491).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15465 / Z2491;
RX   PubMed=10761919; DOI=10.1038/35006655;
RA   Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA   Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA   Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA   Barrell B.G.;
RT   "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT   Z2491.";
RL   Nature 404:502-506(2000).
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; AL157959; CAM07811.1; -; Genomic_DNA.
DR   PIR; G81971; G81971.
DR   RefSeq; WP_002236175.1; NC_003116.1.
DR   AlphaFoldDB; Q9JW60; -.
DR   SMR; Q9JW60; -.
DR   EnsemblBacteria; CAM07811; CAM07811; NMA0534.
DR   KEGG; nma:NMA0534; -.
DR   HOGENOM; CLU_014340_0_5_4; -.
DR   OMA; KRKIIGH; -.
DR   BioCyc; NMEN122587:NMA_RS02705-MON; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000000626; Chromosome.
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..521
FT                   /note="GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_0000140151"
FT   DOMAIN          5..197
FT                   /note="Glutamine amidotransferase type-1"
FT   DOMAIN          198..390
FT                   /note="GMPS ATP-PPase"
FT   ACT_SITE        81
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        171
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        173
FT                   /evidence="ECO:0000250"
FT   BINDING         225..231
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   521 AA;  57730 MW;  5380E6AE22831430 CRC64;
     MTQDKILILD FGSQVTQLIA RRVREAHVYC ELHSFDMPLD EIKAFNPKGI ILSGGPNSVY
     ESDYQADTGI FDLGIPILGI CYGMQFMAHH LGGEVQPGNQ REFGYAQVKT IDSELTRGIQ
     DDTPNTLDVW MSHGDKVSKL PTGFTVIGDT PSCPIAMMEN AEKQFYGIQF HPEVTHTKQG
     RALLNRFVLD ICGAQPGWTM PNYIEEAVAK IREQVGSDEV ILGLSGGVDS SVAAALIHRA
     IGDQLTCVFV DHGLLRLNEG KMVMDMFARN LGVKVIHVDA EGQFMAKLAG VTDPEKKRKI
     IGAEFIEVFD AEEKKLTNAK WLAQGTIYPD VIESAGAKTK KAHAIKSHHN VGGLPENMKL
     KLLEPLRDLF KDEVRELGVA LGLPREMVYR HPFPGPGLGV RILGEVKKEY ADLLRQADDI
     FIQELRNTTD ENGTSWYDLT SQAFAVFLPV KSVGVMGDGR TYDYVVALRA VITSDFMTAH
     WAELPYSLLG RVSNRIINEV KGINRVVYDV SGKPPATIEW E