ID   GUAA_CAMJE              Reviewed;         511 AA.
AC   Q9PN49; Q0P908;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 128.
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=Cj1248;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(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; AL111168; CAL35363.1; -; Genomic_DNA.
DR   PIR; B81332; B81332.
DR   RefSeq; WP_002853189.1; NC_002163.1.
DR   RefSeq; YP_002344639.1; NC_002163.1.
DR   AlphaFoldDB; Q9PN49; -.
DR   SMR; Q9PN49; -.
DR   IntAct; Q9PN49; 1.
DR   STRING; 192222.Cj1248; -.
DR   MEROPS; C26.957; -.
DR   PaxDb; Q9PN49; -.
DR   PRIDE; Q9PN49; -.
DR   EnsemblBacteria; CAL35363; CAL35363; Cj1248.
DR   GeneID; 905539; -.
DR   KEGG; cje:Cj1248; -.
DR   PATRIC; fig|192222.6.peg.1231; -.
DR   eggNOG; COG0518; Bacteria.
DR   eggNOG; COG0519; Bacteria.
DR   HOGENOM; CLU_014340_0_5_7; -.
DR   OMA; KRKIIGH; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000000799; 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; Reference proteome.
FT   CHAIN           1..511
FT                   /note="GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_0000140105"
FT   DOMAIN          5..195
FT                   /note="Glutamine amidotransferase type-1"
FT   DOMAIN          196..386
FT                   /note="GMPS ATP-PPase"
FT   ACT_SITE        82
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        169
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        171
FT                   /evidence="ECO:0000250"
FT   BINDING         223..229
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   511 AA;  56977 MW;  6EDE699C0E8ACFE3 CRC64;
     MKKADILVLD FGSQYTQLIA RRLREQGVYA EILPFNVSLA DIKAKEPKGI ILSGGPASVY
     ATDAYFCDKG IFDLNLPVLG ICYGMQLMAH HYKATVAPAG HKEYGKANIE IKKDNALFKN
     LPKKQTVWMS HSDKVENLPQ GFEVLATSEN SPFCVFGNED KKFFALQFHP EVQHSEFGKN
     ILKNFAKYAC NCESIWNMGS FAKTQAEKIR EEVGNDKVLC AVSGGVDSSV VAALLASAIK
     EQIIVVFVDN GLLRSGEKEQ VEFMFKNTLG IDLISIDASE IFLSRLVNVT DPEQKRKIIG
     NTFIEVFEEE AKKHKDVKYL AQGTLYTDII ESSVVGASKT IKSHHNVGGL PEKMNLKLIE
     PLKEIFKDEV RALGLELGLS KEVVYRHPFP GPGLAIRIMG EVNRASLELL RKADVILLEE
     LKSTGWYDKT WQAFCVLLNV KSVGVMGDNR TYDNAVCIRV VDASDGMTAT FSHLPYEILE
     NISRRIINEV EGINRVVYDI SSKPPATIEW E