ID   GUAA_YEAST              Reviewed;         525 AA.
AC   P38625; D6W042;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   27-MAR-2024, entry version 194.
DE   RecName: Full=GMP synthase [glutamine-hydrolyzing] {ECO:0000303|PubMed:8112582};
DE            EC=6.3.5.2 {ECO:0000305|PubMed:8112582};
DE   AltName: Full=GMP synthetase {ECO:0000303|PubMed:8112582};
DE   AltName: Full=Glutamine amidotransferase {ECO:0000305};
GN   Name=GUA1 {ECO:0000303|PubMed:8112582}; OrderedLocusNames=YMR217W;
GN   ORFNames=YM8261.11;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 44827 / SKQ2N;
RX   PubMed=8112582; DOI=10.1016/0378-1119(94)90535-5;
RA   Dujardin G., Kermorgant M., Slonimski P.P., Boucherie H.;
RT   "Cloning and sequencing of the GMP synthetase-encoding gene of
RT   Saccharomyces cerevisiae.";
RL   Gene 139:127-132(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-20.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7483834; DOI=10.1002/yea.320110702;
RA   Boucherie H., Dujardin G., Kermorgant M., Monribot C., Slonimski P.P.,
RA   Perrot M.;
RT   "Two-dimensional protein map of Saccharomyces cerevisiae: construction of a
RT   gene-protein index.";
RL   Yeast 11:601-613(1995).
RN   [5]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-241 AND LYS-426, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22106047; DOI=10.1002/pmic.201100166;
RA   Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT   "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL   Proteomics 12:236-240(2012).
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         Evidence={ECO:0000305|PubMed:8112582};
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; X70397; CAA49847.1; -; Genomic_DNA.
DR   EMBL; Z49809; CAA89932.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA10116.1; -; Genomic_DNA.
DR   PIR; S55099; S55099.
DR   RefSeq; NP_013944.1; NM_001182724.1.
DR   AlphaFoldDB; P38625; -.
DR   SMR; P38625; -.
DR   BioGRID; 35395; 46.
DR   IntAct; P38625; 5.
DR   MINT; P38625; -.
DR   STRING; 4932.YMR217W; -.
DR   MEROPS; C26.957; -.
DR   iPTMnet; P38625; -.
DR   MaxQB; P38625; -.
DR   PaxDb; 4932-YMR217W; -.
DR   PeptideAtlas; P38625; -.
DR   EnsemblFungi; YMR217W_mRNA; YMR217W; YMR217W.
DR   GeneID; 855257; -.
DR   KEGG; sce:YMR217W; -.
DR   AGR; SGD:S000004830; -.
DR   SGD; S000004830; GUA1.
DR   VEuPathDB; FungiDB:YMR217W; -.
DR   eggNOG; KOG1622; Eukaryota.
DR   GeneTree; ENSGT00390000006591; -.
DR   HOGENOM; CLU_014340_0_5_1; -.
DR   InParanoid; P38625; -.
DR   OMA; IWQSFAV; -.
DR   OrthoDB; 6206at2759; -.
DR   BioCyc; MetaCyc:YMR217W-MONOMER; -.
DR   BioCyc; YEAST:YMR217W-MONOMER; -.
DR   Reactome; R-SCE-73817; Purine ribonucleoside monophosphate biosynthesis.
DR   Reactome; R-SCE-9748787; Azathioprine ADME.
DR   UniPathway; UPA00189; UER00296.
DR   BioGRID-ORCS; 855257; 9 hits in 10 CRISPR screens.
DR   PRO; PR:P38625; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; P38625; Protein.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IMP:SGD.
DR   GO; GO:0003921; F:GMP synthase activity; IBA:GO_Central.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006177; P:GMP biosynthetic process; IMP:SGD.
DR   CDD; cd01742; GATase1_GMP_Synthase; 1.
DR   CDD; cd01997; GMP_synthase_C; 1.
DR   Gene3D; 3.30.300.10; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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   NCBIfam; TIGR00884; guaA_Cterm; 1.
DR   NCBIfam; TIGR00888; guaA_Nterm; 1.
DR   PANTHER; PTHR11922:SF2; GMP SYNTHASE [GLUTAMINE-HYDROLYZING]; 1.
DR   PANTHER; PTHR11922; GMP SYNTHASE-RELATED; 1.
DR   Pfam; PF00117; GATase; 1.
DR   Pfam; PF00958; GMP_synt_C; 1.
DR   Pfam; PF02540; NAD_synthase; 1.
DR   PRINTS; PR00097; ANTSNTHASEII.
DR   PRINTS; PR00096; GATASE.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF54810; GMP synthetase C-terminal dimerisation domain; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
DR   PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Direct protein sequencing;
KW   Glutamine amidotransferase; GMP biosynthesis; Isopeptide bond; Ligase;
KW   Nucleotide-binding; Purine biosynthesis; Reference proteome;
KW   Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:7483834"
FT   CHAIN           2..525
FT                   /note="GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_0000140258"
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|UniProtKB:P04079"
FT   ACT_SITE        176
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250|UniProtKB:P04079"
FT   ACT_SITE        178
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250|UniProtKB:P04079"
FT   BINDING         231..237
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04079"
FT   CROSSLNK        241
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   CROSSLNK        426
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   CONFLICT        325
FT                   /note="K -> R (in Ref. 1; CAA49847)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   525 AA;  58482 MW;  56509DE34A9830FA CRC64;
     MAAGEQVSNM FDTILVLDFG SQYSHLITRR LREFNIYAEM LPCTQKISEL GWTPKGVILS
     GGPYSVYAED APHVDHAIFD LNVPILGICY GMQELAWING KQVGRGDKRE YGPATLKVID
     DSNSLFKGMN DSTVWMSHGD KLHGLPTGYK TIATSDNSPY CGIVHETKPI YGIQFHPEVT
     HSTQGKTLLK NFAVDLCHAK QNWTMENFID TEINRIRKLV GPTAEVIGAV SGGVDSTVAS
     KLMTEAIGDR FHAILVDNGV LRLNEAANVK KTLVEGLGIN LMVVDASEEF LSKLKGVTDP
     EKKRKIIGNT FIHVFEREAE KIKPKDGKEI QFLLQGTLYP DVIESISFKG PSQTIKTHHN
     VGGLLENMKL KLIEPLRELF KDEVRHLGEL LGIPHDLVWR HPFPGPGIAI RVLGEVTKEQ
     VEIARKADNI YIEEIKKAGL YNQISQAFAC LLPVKSVGVM GDQRTYDQVI ALRAIETTDF
     MTADWFPFEH SFLKKVASRI VNEVDGVARV TYDITSKPPA TVEWE
//