GUAA_YEAST
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 03-AUG-2022, entry version 187.
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; 37.
DR IntAct; P38625; 5.
DR MINT; P38625; -.
DR STRING; 4932.YMR217W; -.
DR MEROPS; C26.957; -.
DR iPTMnet; P38625; -.
DR MaxQB; P38625; -.
DR PaxDb; P38625; -.
DR PRIDE; P38625; -.
DR EnsemblFungi; YMR217W_mRNA; YMR217W; YMR217W.
DR GeneID; 855257; -.
DR KEGG; sce:YMR217W; -.
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; KRKIIGH; -.
DR BioCyc; MetaCyc:YMR217W-MON; -.
DR BioCyc; YEAST:YMR217W-MON; -.
DR Reactome; R-SCE-73817; Purine ribonucleoside monophosphate biosynthesis.
DR Reactome; R-SCE-9748787; Azathioprine ADME.
DR UniPathway; UPA00189; UER00296.
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: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; IMP:SGD.
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 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
