GUAA_CANGA
ID GUAA_CANGA Reviewed; 525 AA.
AC Q6FUF3;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=CAGL0F03927g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380952; CAG59065.1; -; Genomic_DNA.
DR RefSeq; XP_446141.1; XM_446141.1.
DR AlphaFoldDB; Q6FUF3; -.
DR SMR; Q6FUF3; -.
DR STRING; 5478.XP_446141.1; -.
DR MEROPS; C26.957; -.
DR EnsemblFungi; CAG59065; CAG59065; CAGL0F03927g.
DR GeneID; 2887636; -.
DR KEGG; cgr:CAGL0F03927g; -.
DR CGD; CAL0129288; CAGL0F03927g.
DR VEuPathDB; FungiDB:CAGL0F03927g; -.
DR eggNOG; KOG1622; Eukaryota.
DR HOGENOM; CLU_014340_0_5_1; -.
DR InParanoid; Q6FUF3; -.
DR OMA; KRKIIGH; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000002428; Chromosome F.
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..525
FT /note="GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_0000286147"
FT DOMAIN 13..202
FT /note="Glutamine amidotransferase type-1"
FT DOMAIN 203..400
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 525 AA; 58584 MW; 370FEA87F8749EB0 CRC64;
MSSIEQVNEV FDTILVLDFG SQYSHLITRR LREFNIYAEM LPCTQKIADL HFKPKGVIMS
GGPYSVYAED APHVDHAIFD LGVPILGICY GMQELAWING KQVARGEKRE YGPATLNVLD
KEDALFKNVD HSTVWMSHGD KLHGLPTGFK VIATSDNSPY CGIVHESKQI YGIQFHPEVT
HSSNGKTLLK NFAVDLCHAK QNWTMKNFIG TEVQRIRDLV GPTAEVIGAV SGGVDSTVAS
KLMTEAIGDR FHAILVDNGV LRLNEAATVK KTLVDGLGIN LTVVDAADEF LDNLKGVTDP
EKKRKIIGNT FIHVFEREAE KIKPKDGKAI EFLLQGTLYP DVIESISFKG PSQTIKTHHN
VGGLLENMKL KLIEPLRELF KDEVRELGEL LGISHELVWR HPFPGPGIAI RVLGEVTREQ
VEIARKADHI YIEEIRKAGL YDKISQAFAC LLPVKSVGVM GDQRTYEQVI ALRAIETTDF
MTADWYPFEH SFLRKVASRI VNEVDGVARV TYDITSKPPA TVEWE
