ID   URA8_YEAS7              Reviewed;         578 AA.
AC   A6ZQ59;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=CTP synthase 2;
DE            EC=6.3.4.2;
DE   AltName: Full=CTP synthetase 2;
DE   AltName: Full=UTP--ammonia ligase 2;
GN   Name=URA8; ORFNames=SCY_3020;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with
CC       either L-glutamine or ammonia as the source of nitrogen. Plays an
CC       important role in the regulation of phospholipid synthesis (By
CC       similarity). {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Activated by GTP. Subject to allosteric product
CC       inhibition by CTP. Inhibited by p-chloromercuriphenylsulfonic acid, N-
CC       ethylmaleimide and cyclopentenylcytosine (CPEC) (By similarity).
CC       {ECO:0000250}.
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC       CTP from UDP: step 2/2.
CC   -!- SUBUNIT: Homodimer. Oligomerizes to a tetramer in the presence of its
CC       substrates UTP and ATP (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CTP synthase family. {ECO:0000305}.
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DR   EMBL; AAFW02000040; EDN63419.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZQ59; -.
DR   SMR; A6ZQ59; -.
DR   EnsemblFungi; EDN63419; EDN63419; SCY_3020.
DR   HOGENOM; CLU_011675_5_0_1; -.
DR   UniPathway; UPA00159; UER00277.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   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; Cytoplasm; Glutamine amidotransferase; Ligase;
KW   Nucleotide-binding; Pyrimidine biosynthesis.
FT   CHAIN           1..578
FT                   /note="CTP synthase 2"
FT                   /id="PRO_0000377746"
FT   DOMAIN          305..564
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        537
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        539
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   578 AA;  64497 MW;  6381F30814CC2C12 CRC64;
     MKYVVVSGGV ISGIGKGVLA SSTGMLLKTL GLKVTSIKID PYMNIDAGTM SPLEHGECFV
     LDDGGETDLD LGNYERYLGI TLSRDHNITT GKIYSHVISR ERRGDYLGKT VQIVPHLTNA
     IQDWIQRVSK IPVDDTGLEP DVCIIELGGT VGDIESAPFV EALRQFQFEV GRENFALIHV
     SLVPVIHGEQ KTKPTQAAIK DLRSLGLIPD MIACRCSEEL NRSTIDKIAM FCHVGPEQVV
     NVHDVNSTYH VPLLLLKQHM IDYLHSRLKL GEVPLTLEDK ERGSQLLTNW ENMTKNLDDS
     DDVVKIALVG KYTNLKDSYL SVTKSLEHAS MKCRRQLEIL WVEASNLEPE TQEVDKNKFH
     DSWNKLSSAD GILVPGGFGT RGIEGMILAA KWARESGVPF LGVCLGLQVA AIEFARNVIG
     RPNSSSTEFL DETLLAPEDQ VVIYMPEIDK EHMGGTMRLG LRPTIFQPNS EWSNIRKLYG
     EVNEVHERHR HRYEINPKIV NDMESRGFIF VGKDETGQRC EIFELKGHPY YVGTQYHPEY
     TSKVLEPSRP FWGLVAAASG TLGDVIKDIN LSEGNENE