ID   GUAA_YARLI              Reviewed;         527 AA.
AC   Q6CEF3;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=YALI0B16104g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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; CR382128; CAG83212.1; -; Genomic_DNA.
DR   RefSeq; XP_500959.1; XM_500959.1.
DR   AlphaFoldDB; Q6CEF3; -.
DR   SMR; Q6CEF3; -.
DR   STRING; 4952.CAG83212; -.
DR   EnsemblFungi; CAG83212; CAG83212; YALI0_B16104g.
DR   GeneID; 2906785; -.
DR   KEGG; yli:YALI0B16104g; -.
DR   VEuPathDB; FungiDB:YALI0_B16104g; -.
DR   HOGENOM; CLU_014340_0_5_1; -.
DR   InParanoid; Q6CEF3; -.
DR   OMA; KRKIIGH; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000001300; Chromosome B.
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   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..527
FT                   /note="GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_0000286156"
FT   DOMAIN          13..202
FT                   /note="Glutamine amidotransferase type-1"
FT   DOMAIN          203..402
FT                   /note="GMPS ATP-PPase"
FT   ACT_SITE        89
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        176
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        178
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         231..237
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   527 AA;  58350 MW;  F885D9227D29BB5D CRC64;
     MPAPVNIPSM FDTILVLDFG SQYSHLITRR LREFNVYAEM LPCTQKIAEL PWKPKGVILS
     GGPYSVYAEG SPHVDHAVFD LGVPILGICY GMQELAWING KGVHAGEKKE FGHATIHVEK
     PSDPLFHGID NFQVWMSHGD KLNALPTGYE VVATSDNSPY AGIAHTSEKI WGIQFHPEVT
     HTTKGKQLLQ NFAVDICGAA QKWSMENFVD TEIQRIRDLV GPHAEVIGAV SGGVDSTVGA
     KLMKEAIGDR FHAILVDNGV MRLNECENVK KTLGEGLGIN LNVVDAADLF LGKLKGVTDP
     EKKRKIIGNT FIEVFEEEAA KIQPTHPEAG EIEFLLQGTL YPDVIESISF KGPSQTIKTH
     HNVGGLLDNM KLKLIEPLRE LFKDEVRKLG EIMGIPHDLV WRHPFPGPGI AIRVLGEVTP
     SQVEIARKAD FIYIEEIKKA GIYEEISQAF ACLLPVKSVG VMGDQRTYEQ VIALRAIETV
     DFMTADWYIF DANFLKTVAR RIVNEVPGVA RVVYDITSKP PATVEWE