PYRG_DROPS
ID PYRG_DROPS Reviewed; 644 AA.
AC Q2M197; B5DQR1;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 2.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=CTP synthase;
DE EC=6.3.4.2;
DE AltName: Full=CTP synthetase;
DE AltName: Full=UTP--ammonia ligase;
GN Name=CTPsyn; ORFNames=GA23623;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
CC -!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with
CC either L-glutamine or ammonia as the source of nitrogen. Constitutes
CC the rate-limiting enzyme in the synthesis of cytosine nucleotides (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 -!- 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; CH379069; EDY73377.1; -; Genomic_DNA.
DR RefSeq; XP_015042586.1; XM_015187100.1.
DR AlphaFoldDB; Q2M197; -.
DR SMR; Q2M197; -.
DR STRING; 7237.FBpp0274763; -.
DR EnsemblMetazoa; FBtr0375070; FBpp0336544; FBgn0245023.
DR GeneID; 6900355; -.
DR KEGG; dpo:Dpse_GA23623; -.
DR eggNOG; KOG2387; Eukaryota.
DR InParanoid; Q2M197; -.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000001819; Chromosome X.
DR Bgee; FBgn0245023; Expressed in female reproductive system and 2 other tissues.
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; Glutamine amidotransferase; Ligase; Nucleotide-binding;
KW Pyrimidine biosynthesis; Reference proteome.
FT CHAIN 1..644
FT /note="CTP synthase"
FT /id="PRO_0000247039"
FT DOMAIN 300..551
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 399
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 527
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 529
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 644 AA; 71513 MW; 04BBAF42D4693FB4 CRC64;
MKYILVTGGV ISGVGKGVIA SSFGTLLKSC QLDVTSIKID PYINIDAGTF SPYEHGEVYV
LDDGAEVDLD LGNYERFLDI TLHRDNNITT GKIYKLVIEK ERTGEYLGKT VQVVPHITDA
IQEWVERVAQ TPVQGSSKPQ VCIIELGGTI GDIEGMPFVE AFRQFQFRVK RENFCVAHVS
LVPLPKATGE PKTKPTQSSV RELRGCGLSP DLIVCRSEKP IGLEVKEKIS NFCHVGPDQV
ICIHDLNSIY HVPLLMEQNG VIEYLNERLQ LNIDMSKRTK CLQHWRDLAR RTETVRREVS
IAIVGKYTKF ADSYASVVKA LQHAALAANR KLVLVFIESC QLEQETLVSE PSKYHKEWQR
LCDSDGILVP GGFGSRGMEG KIRACRWARE NQKPMLGICL GLQAAVIEFA RNKLGLKDAN
TTEIDPQTGN ALVIDMPEHH TGQLGGTMRL GKRTTVFSEG CTSIIRQLYG NPKSIEERHR
HRYEVNPKYV PQLEEHGMRF VATDVDKTRM EIIELRDHPY FVATQYHPEY LSRPLKPSPP
FLGLILASVD RLPQYIQRGC RLSPRQLSDA SSDEEETYVG ATKLMKSLQI TGTTTPTNGI
SRNACRSSNS STISTVSSDI EGACGGVGVG PTTTNGHGED IGKE
