PYRG2_BOVIN
ID PYRG2_BOVIN Reviewed; 586 AA.
AC Q1RMS2; A5D9B0;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BT030529; ABQ12969.1; -; mRNA.
DR EMBL; BC114742; AAI14743.1; -; mRNA.
DR RefSeq; NP_001070434.1; NM_001076966.1.
DR RefSeq; XP_005228512.1; XM_005228455.2.
DR RefSeq; XP_005228513.1; XM_005228456.2.
DR AlphaFoldDB; Q1RMS2; -.
DR SMR; Q1RMS2; -.
DR STRING; 9913.ENSBTAP00000022629; -.
DR MEROPS; C26.964; -.
DR PaxDb; Q1RMS2; -.
DR PRIDE; Q1RMS2; -.
DR Ensembl; ENSBTAT00000022629; ENSBTAP00000022629; ENSBTAG00000017017.
DR GeneID; 767849; -.
DR KEGG; bta:767849; -.
DR CTD; 56474; -.
DR VEuPathDB; HostDB:ENSBTAG00000017017; -.
DR VGNC; VGNC:27809; CTPS2.
DR eggNOG; KOG2387; Eukaryota.
DR GeneTree; ENSGT00910000144179; -.
DR HOGENOM; CLU_011675_4_1_1; -.
DR InParanoid; Q1RMS2; -.
DR OMA; FKPGTEW; -.
DR OrthoDB; 810128at2759; -.
DR TreeFam; TF300379; -.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000017017; Expressed in caput epididymis and 108 other tissues.
DR ExpressionAtlas; Q1RMS2; baseline and differential.
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; IBA:GO_Central.
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 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 2: Evidence at transcript 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_0000247032"
FT DOMAIN 300..554
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT REGION 564..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 399
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 526
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 528
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT MOD_RES 568
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRF8"
FT MOD_RES 571
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRF8"
FT MOD_RES 574
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRF8"
SQ SEQUENCE 586 AA; 65481 MW; 0A6E65BF35958831 CRC64;
MKYILVTGGV ISGIGKGIIA SSIGTILKSC GLRVTAIKID PYINIDAGTF SPYEHGEVFV
LNDGGEVDLD LGNYERFLDI NLYKDNNITT GKIYQHVINK ERRGDYLGKT VQVVPHITDA
VQEWVMNQAM VPVDGHKEEP QICVIELGGT IGDIEGMPFV EAFRQFQFKA KRENFCNIHV
SLVPQPSATG EQKTKPTQNS VRALRGLGLS PDLIVCRSST PIEMAVKEKI SMFCHVNPEQ
VICIHDVSST YRVPVLLEEQ GIIKYFKERL DLPIGDSASS LLSKWRNMAD RYERLQKTCS
IALVGKYTKL RDCYASVFKA LEHSALAINH KLNLMYIDSI DLEQTTEVED PVKFHEAWQK
LCKADGVLVP GGFGIRGTLG KLQAISWARS RKIPFLGVCL GMQLAVIEFA RNCLNLKDAD
STEFEPNARV PVVIDMPEHN PGNLGGTMRL GIRRTVFKTE NSILRKLYGD VPFIEERHRH
RYEVNPSLIS QLEQKDLSFV GQDVDGERME IIELANHPYF VGVQFHPEFS SRPMKPSPPY
LGLLLAATGN LNAYLLQGCK LSSSDRYSDA SDDSFSEPRL AELEIS
