GUAA_CANAL
ID GUAA_CANAL Reviewed; 530 AA.
AC Q5APF2; A0A1D8PEL6;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=CAALFM_C109490CA;
GN ORFNames=CaO19.12276, CaO19.4813;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(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; CP017623; AOW26582.1; -; Genomic_DNA.
DR RefSeq; XP_723499.1; XM_718406.2.
DR AlphaFoldDB; Q5APF2; -.
DR SMR; Q5APF2; -.
DR BioGRID; 1217857; 1.
DR STRING; 237561.Q5APF2; -.
DR PRIDE; Q5APF2; -.
DR GeneID; 3634763; -.
DR KEGG; cal:CAALFM_C109490CA; -.
DR CGD; CAL0000179678; GUA1.
DR VEuPathDB; FungiDB:C1_09490C_A; -.
DR eggNOG; KOG1622; Eukaryota.
DR HOGENOM; CLU_014340_0_5_1; -.
DR InParanoid; Q5APF2; -.
DR OMA; KRKIIGH; -.
DR OrthoDB; 392369at2759; -.
DR UniPathway; UPA00189; UER00296.
DR PRO; PR:Q5APF2; -.
DR Proteomes; UP000000559; Chromosome 1.
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 GO; GO:0046037; P:GMP metabolic process; IMP:CGD.
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..530
FT /note="GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_0000286146"
FT DOMAIN 18..207
FT /note="Glutamine amidotransferase type-1"
FT DOMAIN 208..405
FT /note="GMPS ATP-PPase"
FT ACT_SITE 94
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 181
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 183
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT BINDING 236..242
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 530 AA; 58813 MW; 87BCD288C209DF46 CRC64;
MSANIDDVPI EVSKVFDTIL VLDFGSQYSH LITRRLREFN VYAEMLPCTQ KIAELSWKPK
GIILSGGPYS VYAEDAPHVD HDIFKLGVPI LGICYGMQEL AWINGKGVAR GDKREYGPAT
LNVEDPECAL FKGVDHSQVW MSHGDKLHAL PTGFKVVATS DNSPFCGISN ESEHIYGIQF
HPEVTHTVQG KKLLKNFAVD ICQAKTNWSM ENFIDTEIAR IKKLVGPTAE VIGAVSGGVD
STVGAKIMKE AIGDRFHAIY VDNGVMRKNE TESVKKTLDE GLGINLTVVD AGDLFLGRLK
GVTDPEKKRK IIGNTFIHVF EEEAAKIKPR DGSEIEYLLQ GTLYPDVIES ISFKGPSQTI
KTHHNVGGLL EDMKLKLIEP LRELFKDEVR HLGELLGVPE DLVWRHPFPG PGLAIRVLGE
VTKEQVKIAR EADAIFIEEI KKAGLYRQIS QAFAALLPVK SVGVMGDQRT YEQVIALRAI
ETLDFMTADW FIFEAAFLKK VASRIVNEVD GVARVTYDIT SKPPATVEWE
