GUAA_ASHGO
ID GUAA_ASHGO Reviewed; 525 AA.
AC Q756B7;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=AER350W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016818; AAS53030.1; -; Genomic_DNA.
DR RefSeq; NP_985206.1; NM_210560.1.
DR AlphaFoldDB; Q756B7; -.
DR SMR; Q756B7; -.
DR STRING; 33169.AAS53030; -.
DR MEROPS; C26.957; -.
DR EnsemblFungi; AAS53030; AAS53030; AGOS_AER350W.
DR GeneID; 4621421; -.
DR KEGG; ago:AGOS_AER350W; -.
DR eggNOG; KOG1622; Eukaryota.
DR HOGENOM; CLU_014340_0_5_1; -.
DR InParanoid; Q756B7; -.
DR OMA; KRKIIGH; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000000591; Chromosome V.
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..525
FT /note="GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_0000286143"
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; 58202 MW; D2564C3BF94DE6B9 CRC64;
MAAVEQVSSV FDTILVLDFG SQYSHLITRR LREFNVYAEM LPCTQKISEL GWKPKGVILS
GGPYSVYAAD APHVDRAVFE LGVPILGICY GLQELAWIAG AEVGRGEKRE YGRATLHVED
SACPLFNNVD SSTVWMSHGD KLHALPADFH VTATTENSPF CGIAHDSKPI FGIQFHPEVT
HSSQGKTLLK NFAVEICQAA QTWTMENFID TEIQRIRTLV GPTAEVIGAV SGGVDSTVAA
KLMTEAIGDR FHAILVDNGV LRLNEAANVK KILGEGLGIN LTVVDASEEF LTKLKGVTDP
EKKRKIIGNT FIHVFEREAA RIQPKNGEEI EFLLQGTLYP DVIESISFKG PSQTIKTHHN
VGGLLDNMKL KLIEPLRELF KDEVRHLGEL LGISHELVWR HPFPGPGIAI RVLGEVTKEQ
VEIARKADHI YIEEIRKAGL YNKISQAFAC LLPVKSVGVM GDQRTYDQVI ALRAIETTDF
MTADWYPFEH EFLKHVASRI VNEVEGVARV TYDITSKPPA TVEWE
