URA7_YEAST
ID URA7_YEAST Reviewed; 579 AA.
AC P28274; D6VPW0;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=CTP synthase 1;
DE EC=6.3.4.2;
DE AltName: Full=CTP synthetase 1;
DE AltName: Full=UTP--ammonia ligase 1;
GN Name=URA7; OrderedLocusNames=YBL039C; ORFNames=YBL0410;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1753946; DOI=10.1007/bf00293815;
RA Ozier-Kalogeropoulos O., Fasiolo F., Adeline M.-T., Collin J., Lacroute F.;
RT "Cloning, sequencing and characterization of the Saccharomyces cerevisiae
RT URA7 gene encoding CTP synthetase.";
RL Mol. Gen. Genet. 231:7-16(1991).
RN [2]
RP SEQUENCE REVISION.
RA Ozier-Kalogeropoulos O.;
RL Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7871888; DOI=10.1002/yea.320101113;
RA de Wergifosse P., Jacques B., Jonniaux J.-L., Purnelle B., Skala J.,
RA Goffeau A.;
RT "The sequence of a 22.4 kb DNA fragment from the left arm of yeast
RT chromosome II reveals homologues to bacterial proline synthetase and murine
RT alpha-adaptin, as well as a new permease and a DNA-binding protein.";
RL Yeast 10:1489-1496(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP PROTEIN SEQUENCE OF 1-13, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP ACTIVITY REGULATION.
RX PubMed=8075080; DOI=10.1021/bi00201a028;
RA Yang W.-L., McDonough V.M., Ozier-Kalogeropoulos O., Adeline M.-T.,
RA Flocco M.T., Carman G.M.;
RT "Purification and characterization of CTP synthetase, the product of the
RT URA7 gene in Saccharomyces cerevisiae.";
RL Biochemistry 33:10785-10793(1994).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-422, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=SUB592;
RX PubMed=12872131; DOI=10.1038/nbt849;
RA Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA Roelofs J., Finley D., Gygi S.P.;
RT "A proteomics approach to understanding protein ubiquitination.";
RL Nat. Biotechnol. 21:921-926(2003).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
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 -!- ACTIVITY REGULATION: Activated by GTP and inhibited by CTP.
CC {ECO:0000269|PubMed:8075080}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=60 uM for UTP {ECO:0000269|PubMed:8075080};
CC KM=0.9 mM for ATP {ECO:0000269|PubMed:8075080};
CC KM=0.4 mM for L-glutamine {ECO:0000269|PubMed:8075080};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:8075080};
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. {ECO:0000269|PubMed:8075080}.
CC -!- MISCELLANEOUS: Present with 57600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CTP synthase family. {ECO:0000305}.
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DR EMBL; X53995; CAA37941.1; -; Genomic_DNA.
DR EMBL; X78214; CAA55055.1; -; Genomic_DNA.
DR EMBL; Z35800; CAA84859.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07080.1; -; Genomic_DNA.
DR PIR; S50291; S50291.
DR RefSeq; NP_009514.1; NM_001178279.1.
DR PDB; 7RMC; EM; 3.50 A; D/E/F/Q/R/S/T/U/V/W/g/h=1-572.
DR PDBsum; 7RMC; -.
DR AlphaFoldDB; P28274; -.
DR SMR; P28274; -.
DR BioGRID; 32658; 279.
DR DIP; DIP-2954N; -.
DR IntAct; P28274; 87.
DR MINT; P28274; -.
DR STRING; 4932.YBL039C; -.
DR MEROPS; C26.A36; -.
DR iPTMnet; P28274; -.
DR MaxQB; P28274; -.
DR PaxDb; P28274; -.
DR PRIDE; P28274; -.
DR EnsemblFungi; YBL039C_mRNA; YBL039C; YBL039C.
DR GeneID; 852241; -.
DR KEGG; sce:YBL039C; -.
DR SGD; S000000135; URA7.
DR VEuPathDB; FungiDB:YBL039C; -.
DR eggNOG; KOG2387; Eukaryota.
DR GeneTree; ENSGT00910000144179; -.
DR HOGENOM; CLU_011675_5_0_1; -.
DR InParanoid; P28274; -.
DR OMA; EFNNAYR; -.
DR BioCyc; YEAST:YBL039C-MON; -.
DR BRENDA; 6.3.4.2; 984.
DR Reactome; R-SCE-499943; Interconversion of nucleotide di- and triphosphates.
DR SABIO-RK; P28274; -.
DR UniPathway; UPA00159; UER00277.
DR PRO; PR:P28274; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P28274; protein.
DR GO; GO:0097268; C:cytoophidium; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003883; F:CTP synthase activity; IDA:SGD.
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; IDA:SGD.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IMP:SGD.
DR GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IMP:SGD.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Direct protein sequencing;
KW Glutamine amidotransferase; Isopeptide bond; Ligase; Nucleotide-binding;
KW Pyrimidine biosynthesis; Reference proteome; Ubl conjugation.
FT CHAIN 1..579
FT /note="CTP synthase 1"
FT /id="PRO_0000138283"
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"
FT CROSSLNK 422
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:12872131"
FT CONFLICT 307
FT /note="A -> R (in Ref. 1; CAA37941)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="V -> S (in Ref. 1; CAA37941)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 579 AA; 64710 MW; EC3766C83B22ED92 CRC64;
MKYVVVSGGV ISGIGKGVLA SSTGMLMKTL GLKVTSIKID PYMNIDAGTM SPLEHGECFV
LDDGGETDLD LGNYERYLGV TLTKDHNITT GKIYSHVIAK ERKGDYLGKT VQIVPHLTNA
IQDWIERVAK IPVDDTGMEP DVCIIELGGT VGDIESAPFV EALRQFQFKV GKENFALIHV
SLVPVIHGEQ KTKPTQAAIK GLRSLGLVPD MIACRCSETL DKPTIDKIAM FCHVGPEQVV
NVHDVNSTYH VPLLLLEQKM IDYLHARLKL DEISLTEEEK QRGLELLSKW KATTGNFDES
METVKIALVG KYTNLKDSYL SVIKALEHSS MKCRRKLDIK WVEATDLEPE AQESNKTKFH
EAWNMVSTAD GILIPGGFGV RGTEGMVLAA RWARENHIPF LGVCLGLQIA TIEFTRSVLG
RKDSHSAEFY PDIDEKNHVV VFMPEIDKET MGGSMRLGLR PTFFQNETEW SQIKKLYGDV
SEVHERHRHR YEINPKMVDE LENNGLIFVG KDDTGKRCEI LELKNHPYYI ATQYHPEYTS
KVLDPSKPFL GLVAASAGIL QDVIEGKYDL EAGENKFNF
