PYRG2_RAT
ID PYRG2_RAT Reviewed; 586 AA.
AC Q5U2N0; Q5U3X4;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
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=Ctps2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568; SER-571 AND SER-574, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; BC085949; AAH85949.1; -; mRNA.
DR EMBL; BC085358; AAH85358.1; -; mRNA.
DR RefSeq; NP_001030170.1; NM_001034998.2.
DR RefSeq; XP_006256958.1; XM_006256896.2.
DR RefSeq; XP_006256959.1; XM_006256897.3.
DR RefSeq; XP_006256960.1; XM_006256898.3.
DR RefSeq; XP_006256961.1; XM_006256899.3.
DR RefSeq; XP_006256962.1; XM_006256900.2.
DR AlphaFoldDB; Q5U2N0; -.
DR SMR; Q5U2N0; -.
DR STRING; 10116.ENSRNOP00000055810; -.
DR MEROPS; C26.964; -.
DR iPTMnet; Q5U2N0; -.
DR PhosphoSitePlus; Q5U2N0; -.
DR jPOST; Q5U2N0; -.
DR PaxDb; Q5U2N0; -.
DR PRIDE; Q5U2N0; -.
DR GeneID; 619580; -.
DR KEGG; rno:619580; -.
DR UCSC; RGD:1563369; rat.
DR CTD; 56474; -.
DR RGD; 1563369; Ctps2.
DR VEuPathDB; HostDB:ENSRNOG00000004257; -.
DR eggNOG; KOG2387; Eukaryota.
DR HOGENOM; CLU_011675_5_0_1; -.
DR InParanoid; Q5U2N0; -.
DR OMA; FKPGTEW; -.
DR OrthoDB; 810128at2759; -.
DR PhylomeDB; Q5U2N0; -.
DR TreeFam; TF300379; -.
DR Reactome; R-RNO-499943; Interconversion of nucleotide di- and triphosphates.
DR UniPathway; UPA00159; UER00277.
DR PRO; PR:Q5U2N0; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000004257; Expressed in pancreas and 20 other tissues.
DR Genevisible; Q5U2N0; RN.
DR GO; GO:0097268; C:cytoophidium; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003883; F:CTP synthase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006241; P:CTP biosynthetic process; IBA:GO_Central.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
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 HAMAP; MF_01227; PyrG; 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 1: Evidence at protein level;
KW ATP-binding; Glutamine amidotransferase; Ligase; Nucleotide-binding;
KW Phosphoprotein; Pyrimidine biosynthesis; Reference proteome.
FT CHAIN 1..586
FT /note="CTP synthase 2"
FT /id="PRO_0000247035"
FT DOMAIN 300..554
FT /note="Glutamine amidotransferase type-1"
FT ACT_SITE 399
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 526
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 528
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT MOD_RES 568
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 571
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 574
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 586 AA; 65674 MW; A67D001E9C3E8D3B CRC64;
MKYILVTGGV ISGIGKGIIA SSIGTILKSC GLRVTAIKID PYINIDAGTF SPYEHGEVFV
LNDGGEVDLD LGNYERFLDI NLYKDNNITT GKIYQHVINK ERRGDYLGKT VQVVPHITDA
IQDWVMNQAK VSVDGNKEDP QICVIELGGT IGDIEGMAFV EAFRQFQFKA KRENFYNIHV
SLVPQPSATG EQKTKPTQNS VRALRGLGLS PDLIVCRSST PIEMAVKEKI SMFCHVNPEQ
VICIHDVSSI YRVPLLLEEQ GVVKYFQERL DLPINDCSNN LLFKWKTMAD RYERLQKICS
IALVGKYTKL RDCYASVFKA LEHSALAINH KLNLMYIDSI DLEPVTKAED PVKFHEAWQK
LCLADGILVP GGFGIRGTLG KLQAISWART KKIPFLGICL GMQLAVIEFA RNCLNLKDAN
STEFDPNTPV PLVIDMPEHN PGDLGGTMRL GLRRTVFTTE NSILKKLYGD VPYIEERHRH
RYEVNPNLIN QFENKDLCFV GEDVDGKRME IIELTGHPYF IGVQFHPEFS SRPMKPSPPY
LGLLLAATGT LNTHLQQMSK LSYSDIYSDA SDDSFSEAKF AELDIN
