PYRG_CANGA
ID PYRG_CANGA Reviewed; 578 AA.
AC Q6FUD0;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=CTP synthase;
DE EC=6.3.4.2;
DE AltName: Full=CTP synthetase;
DE AltName: Full=UTP--ammonia ligase;
GN Name=URA7; OrderedLocusNames=CAGL0F04433g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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 -!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with
CC either L-glutamine or ammonia as the source of nitrogen.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-
CC glutamate + phosphate; Xref=Rhea:RHEA:26426, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:37563, ChEBI:CHEBI:43474, ChEBI:CHEBI:46398,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.4.2;
CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC CTP from UDP: step 2/2.
CC -!- SIMILARITY: Belongs to the CTP synthase family. {ECO:0000305}.
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DR EMBL; CR380952; CAG59088.1; -; Genomic_DNA.
DR RefSeq; XP_446164.1; XM_446164.1.
DR AlphaFoldDB; Q6FUD0; -.
DR SMR; Q6FUD0; -.
DR STRING; 5478.XP_446164.1; -.
DR EnsemblFungi; CAG59088; CAG59088; CAGL0F04433g.
DR GeneID; 2887710; -.
DR KEGG; cgr:CAGL0F04433g; -.
DR CGD; CAL0131306; URA7.
DR VEuPathDB; FungiDB:CAGL0F04433g; -.
DR eggNOG; KOG2387; Eukaryota.
DR HOGENOM; CLU_011675_5_0_1; -.
DR InParanoid; Q6FUD0; -.
DR OMA; EFNNAYR; -.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000002428; Chromosome F.
DR GO; GO:0097268; C:cytoophidium; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IEA:EnsemblFungi.
DR CDD; cd03113; CTPS_N; 1.
DR CDD; cd01746; GATase1_CTP_Synthase; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR004468; CTP_synthase.
DR InterPro; IPR017456; CTP_synthase_N.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR033828; GATase1_CTP_Synthase.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11550; PTHR11550; 1.
DR Pfam; PF06418; CTP_synth_N; 1.
DR Pfam; PF00117; GATase; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00337; PyrG; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding; Glutamine amidotransferase; Ligase; Nucleotide-binding;
KW Pyrimidine biosynthesis; Reference proteome.
FT CHAIN 1..578
FT /note="CTP synthase"
FT /id="PRO_0000138279"
FT DOMAIN 305..559
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 404
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 535
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 537
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 578 AA; 64589 MW; 98AEBB07FA526937 CRC64;
MKYVVVSGGV ISGIGKGVLA SSTGMLLKTL GLKVTSIKID PYMNIDAGTM SPLEHGECFV
LNDGGETDLD LGNYERYLNV TLTKDHNITT GKIYSHVIAK ERKGDYLGKT VQIVPHLTNA
IQEWIERVSR IPVDNTGMEP DVCIIELGGT VGDIESAPFV EALRQFQFRV GKENFALIHV
SLVPVIHGEQ KTKPTQAAIK DLRSLGLVPD MIACRCSETL EKGVIEKIAM FCHVGADQVV
NVHDVNSTYH VPLLLLEQKM INYLHQRLQL QEITLSSEDI QRGENLLSKW KSMTGNFDSS
METVKIALVG KYTNLKDSYL SVIKALEHSS MKCRRKLEIM WVEATDLEPE TQDTEKAKFH
EAWNKVSTAD GILVPGGFGS RGTEGMMLAS RWARENHIPF LGVCLGLQIA TIEFARNVLG
VKEGNSAEFF PELDESNQVV VFMPEIDKET MGGSMRLGLR PTYFQQGTEW CAIKKLYGSA
ESVEERHRHR YEINPNFIER LEEHGLMFVG RDETNKRCEI FEMKDHPFFV ATQYHPEYTS
KVLDPSKPFL GLVAASSGIL DDVIAGKYEF NGDGKSDF
