ID   GUAA_KLULA              Reviewed;         524 AA.
AC   Q6CU71;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=GUA1; OrderedLocusNames=KLLA0C07172g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR   EMBL; CR382123; CAH01369.1; -; Genomic_DNA.
DR   RefSeq; XP_452518.1; XM_452518.1.
DR   AlphaFoldDB; Q6CU71; -.
DR   SMR; Q6CU71; -.
DR   STRING; 28985.XP_452518.1; -.
DR   MEROPS; C26.957; -.
DR   EnsemblFungi; CAH01369; CAH01369; KLLA0_C07172g.
DR   GeneID; 2892690; -.
DR   KEGG; kla:KLLA0_C07172g; -.
DR   eggNOG; KOG1622; Eukaryota.
DR   HOGENOM; CLU_014340_0_5_1; -.
DR   InParanoid; Q6CU71; -.
DR   OMA; KRKIIGH; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000000598; Chromosome C.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   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; Cytoplasm; Glutamine amidotransferase; GMP biosynthesis;
KW   Ligase; Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT   CHAIN           1..524
FT                   /note="GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_0000286151"
FT   DOMAIN          12..201
FT                   /note="Glutamine amidotransferase type-1"
FT   DOMAIN          202..399
FT                   /note="GMPS ATP-PPase"
FT   ACT_SITE        88
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        175
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        177
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         230..236
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   524 AA;  58555 MW;  0E7C87D904FE3FE5 CRC64;
     MSPVEVSNVF DTILVLDFGS QYSHLITRRL REFNVYAEML PCTQKIADLH WKPKGVILSG
     GPYSVYEKDA PHVDKAIFDL GVPILGICYG LQEIAWINNT EVGRGEKREY GPATLRVEDK
     SCPLFANVDH STVWMSHHDK VHNLPAGFKI TATSENSPFC GIANEDKQIY GIQFHPEVTH
     STQGKTLLRN FAVDICKASQ SWNMENFIDT EINRIRELVG PDAEVIGAVS GGVDSTVAAK
     LMDRAIGDRF HAIMVDNGVL RLNEAATVKK TLGEGLGINL TVVDASDEFL DKLKGVTDPE
     KKRKIIGNTF IHVFEREAAK IQPKNGKEIE FLLQGTLYPD VIESISFKGP SQTIKTHHNV
     GGLLENMKLK LIEPLRELFK DEVRELGELL GISHELVWRH PFPGPGIAIR VLGEVTREQV
     AIARKADYIY IEEIRKAGLY NNISQAFACL LPVKSVGVMG DQRTYEQVIA LRAIETTDFM
     TADWYPFEHS FLKKVASRIV NEVDGVARVT YDITSKPPAT VEWE