GUAA_DEBHA
ID GUAA_DEBHA Reviewed; 529 AA.
AC Q6BLS3;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=DEHA2F11110g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382138; CAG89193.1; -; Genomic_DNA.
DR RefSeq; XP_460848.1; XM_460848.1.
DR AlphaFoldDB; Q6BLS3; -.
DR SMR; Q6BLS3; -.
DR STRING; 4959.XP_460848.1; -.
DR MEROPS; C26.957; -.
DR EnsemblFungi; CAG89193; CAG89193; DEHA2F11110g.
DR GeneID; 2903588; -.
DR KEGG; dha:DEHA2F11110g; -.
DR VEuPathDB; FungiDB:DEHA2F11110g; -.
DR eggNOG; KOG1622; Eukaryota.
DR HOGENOM; CLU_014340_0_5_1; -.
DR InParanoid; Q6BLS3; -.
DR OMA; KRKIIGH; -.
DR OrthoDB; 392369at2759; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000000599; 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..529
FT /note="GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_0000286148"
FT DOMAIN 17..206
FT /note="Glutamine amidotransferase type-1"
FT DOMAIN 207..404
FT /note="GMPS ATP-PPase"
FT ACT_SITE 93
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 180
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 182
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT BINDING 235..241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 529 AA; 58792 MW; 9233BB0713F860DC CRC64;
MVNPADVPIE VSKVFDTILV LDFGSQYSHL ITRRLREFNV YAEMLPCTQK ISELTWKPKG
IILSGGPYSV YEDGSPHVDH DIFKLNVPIL GICYGMQELA WINGKGVARG DKREYGPATL
NVEDSSCSLF KGVDHSQVWM SHGDKLHALP TGFKVVATSD NSPFAAISNE KENIFGIQFH
PEVTHTKQGK VLLRNFAIDI CQASNNWTME NFIDTEIARI QKLVGPTAEV IGAVSGGVDS
TVGAKIMKEA IGDRFHAIYV DNGLMRLNET EQVYKTLTEG LGINLTVVDA TDLFLGKLQG
VTDPEKKRKI IGNNFIHVFE AEAAKIKPAS GQEIEYLLQG TLYPDVIESI SFKGPSQTIK
THHNVGGLLE DMKLKLIEPL RELFKDEVRH LGEIMGVPHD LVWRHPFPGP GLAIRVLGEV
TREQLKIARE ADNIFIEEIR KAGLYKDISQ AFAALLPVKS VGVMGDQRTY EQVIALRAIE
TTDFMTADWF VFEAAFLKKT ASRIVNEVDG VARVTYDITS KPPATVEWE
