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Protein

CTP synthase 1

Gene

URA7

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen.

Catalytic activityi

ATP + UTP + L-glutamine = ADP + phosphate + CTP + L-glutamate.

Enzyme regulationi

Activated by GTP and inhibited by CTP.1 Publication

Kineticsi

  1. KM=60 µM for UTP1 Publication
  2. KM=0.9 mM for ATP1 Publication
  3. KM=0.4 mM for L-glutamine1 Publication

    pH dependencei

    Optimum pH is 8.0.1 Publication

    Pathwayi: CTP biosynthesis via de novo pathway

    This protein is involved in step 2 of the subpathway that synthesizes CTP from UDP.
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. no protein annotated in this organism
    2. CTP synthase 1 (URA7), CTP synthase 2 (URA8)
    This subpathway is part of the pathway CTP biosynthesis via de novo pathway, which is itself part of Pyrimidine metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes CTP from UDP, the pathway CTP biosynthesis via de novo pathway and in Pyrimidine metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei404 – 4041For GATase activityPROSITE-ProRule annotation
    Active sitei535 – 5351For GATase activityPROSITE-ProRule annotation
    Active sitei537 – 5371For GATase activityPROSITE-ProRule annotation

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-KW
    • CTP synthase activity Source: SGD

    GO - Biological processi

    • 'de novo' CTP biosynthetic process Source: UniProtKB-UniPathway
    • CTP biosynthetic process Source: SGD
    • glutamine metabolic process Source: UniProtKB-KW
    • phospholipid biosynthetic process Source: SGD
    • pyrimidine nucleobase biosynthetic process Source: SGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Pyrimidine biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:YBL039C-MONOMER.
    BRENDAi6.3.4.2. 984.
    SABIO-RKP28274.
    UniPathwayiUPA00159; UER00277.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    CTP synthase 1 (EC:6.3.4.2)
    Alternative name(s):
    CTP synthetase 1
    UTP--ammonia ligase 1
    Gene namesi
    Name:URA7
    Ordered Locus Names:YBL039C
    ORF Names:YBL0410
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componenti: Chromosome II

    Organism-specific databases

    EuPathDBiFungiDB:YBL039C.
    SGDiS000000135. URA7.

    Subcellular locationi

    GO - Cellular componenti

    • cytoophidium Source: SGD
    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 579579CTP synthase 1PRO_0000138283Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki422 – 422Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

    Keywords - PTMi

    Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiP28274.
    PeptideAtlasiP28274.

    PTM databases

    iPTMnetiP28274.

    Interactioni

    Subunit structurei

    Homodimer. Oligomerizes to a tetramer in the presence of its substrates UTP and ATP.1 Publication

    Protein-protein interaction databases

    BioGridi32658. 139 interactions.
    DIPiDIP-2954N.
    IntActiP28274. 67 interactions.
    MINTiMINT-506283.

    Structurei

    3D structure databases

    ProteinModelPortaliP28274.
    SMRiP28274. Positions 1-565.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini305 – 559255Glutamine amidotransferase type-1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the CTP synthase family.Curated
    Contains 1 glutamine amidotransferase type-1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Glutamine amidotransferase

    Phylogenomic databases

    GeneTreeiENSGT00390000012473.
    HOGENOMiHOG000077514.
    InParanoidiP28274.
    KOiK01937.
    OMAiHISPAMT.
    OrthoDBiEOG7HMS8X.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    3.40.50.880. 1 hit.
    InterProiIPR029062. Class_I_gatase-like.
    IPR004468. CTP_synthase.
    IPR017456. CTP_synthase_N.
    IPR017926. GATASE.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR11550. PTHR11550. 1 hit.
    PfamiPF06418. CTP_synth_N. 1 hit.
    PF00117. GATase. 1 hit.
    [Graphical view]
    SUPFAMiSSF52317. SSF52317. 1 hit.
    SSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00337. PyrG. 1 hit.
    PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P28274-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKYVVVSGGV ISGIGKGVLA SSTGMLMKTL GLKVTSIKID PYMNIDAGTM
    60 70 80 90 100
    SPLEHGECFV LDDGGETDLD LGNYERYLGV TLTKDHNITT GKIYSHVIAK
    110 120 130 140 150
    ERKGDYLGKT VQIVPHLTNA IQDWIERVAK IPVDDTGMEP DVCIIELGGT
    160 170 180 190 200
    VGDIESAPFV EALRQFQFKV GKENFALIHV SLVPVIHGEQ KTKPTQAAIK
    210 220 230 240 250
    GLRSLGLVPD MIACRCSETL DKPTIDKIAM FCHVGPEQVV NVHDVNSTYH
    260 270 280 290 300
    VPLLLLEQKM IDYLHARLKL DEISLTEEEK QRGLELLSKW KATTGNFDES
    310 320 330 340 350
    METVKIALVG KYTNLKDSYL SVIKALEHSS MKCRRKLDIK WVEATDLEPE
    360 370 380 390 400
    AQESNKTKFH EAWNMVSTAD GILIPGGFGV RGTEGMVLAA RWARENHIPF
    410 420 430 440 450
    LGVCLGLQIA TIEFTRSVLG RKDSHSAEFY PDIDEKNHVV VFMPEIDKET
    460 470 480 490 500
    MGGSMRLGLR PTFFQNETEW SQIKKLYGDV SEVHERHRHR YEINPKMVDE
    510 520 530 540 550
    LENNGLIFVG KDDTGKRCEI LELKNHPYYI ATQYHPEYTS KVLDPSKPFL
    560 570
    GLVAASAGIL QDVIEGKYDL EAGENKFNF
    Length:579
    Mass (Da):64,710
    Last modified:October 1, 1994 - v2
    Checksum:iEC3766C83B22ED92
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti307 – 3071A → R in CAA37941 (PubMed:1753946).Curated
    Sequence conflicti418 – 4181V → S in CAA37941 (PubMed:1753946).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X53995 Genomic DNA. Translation: CAA37941.1.
    X78214 Genomic DNA. Translation: CAA55055.1.
    Z35800 Genomic DNA. Translation: CAA84859.1.
    BK006936 Genomic DNA. Translation: DAA07080.1.
    PIRiS50291.
    RefSeqiNP_009514.1. NM_001178279.1.

    Genome annotation databases

    EnsemblFungiiYBL039C; YBL039C; YBL039C.
    GeneIDi852241.
    KEGGisce:YBL039C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X53995 Genomic DNA. Translation: CAA37941.1.
    X78214 Genomic DNA. Translation: CAA55055.1.
    Z35800 Genomic DNA. Translation: CAA84859.1.
    BK006936 Genomic DNA. Translation: DAA07080.1.
    PIRiS50291.
    RefSeqiNP_009514.1. NM_001178279.1.

    3D structure databases

    ProteinModelPortaliP28274.
    SMRiP28274. Positions 1-565.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi32658. 139 interactions.
    DIPiDIP-2954N.
    IntActiP28274. 67 interactions.
    MINTiMINT-506283.

    PTM databases

    iPTMnetiP28274.

    Proteomic databases

    MaxQBiP28274.
    PeptideAtlasiP28274.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYBL039C; YBL039C; YBL039C.
    GeneIDi852241.
    KEGGisce:YBL039C.

    Organism-specific databases

    EuPathDBiFungiDB:YBL039C.
    SGDiS000000135. URA7.

    Phylogenomic databases

    GeneTreeiENSGT00390000012473.
    HOGENOMiHOG000077514.
    InParanoidiP28274.
    KOiK01937.
    OMAiHISPAMT.
    OrthoDBiEOG7HMS8X.

    Enzyme and pathway databases

    UniPathwayiUPA00159; UER00277.
    BioCyciYEAST:YBL039C-MONOMER.
    BRENDAi6.3.4.2. 984.
    SABIO-RKP28274.

    Miscellaneous databases

    PROiP28274.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    3.40.50.880. 1 hit.
    InterProiIPR029062. Class_I_gatase-like.
    IPR004468. CTP_synthase.
    IPR017456. CTP_synthase_N.
    IPR017926. GATASE.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR11550. PTHR11550. 1 hit.
    PfamiPF06418. CTP_synth_N. 1 hit.
    PF00117. GATase. 1 hit.
    [Graphical view]
    SUPFAMiSSF52317. SSF52317. 1 hit.
    SSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00337. PyrG. 1 hit.
    PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Cloning, sequencing and characterization of the Saccharomyces cerevisiae URA7 gene encoding CTP synthetase."
      Ozier-Kalogeropoulos O., Fasiolo F., Adeline M.-T., Collin J., Lacroute F.
      Mol. Gen. Genet. 231:7-16(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Ozier-Kalogeropoulos O.
      Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "The sequence of a 22.4 kb DNA fragment from the left arm of yeast chromosome II reveals homologues to bacterial proline synthetase and murine alpha-adaptin, as well as a new permease and a DNA-binding protein."
      de Wergifosse P., Jacques B., Jonniaux J.-L., Purnelle B., Skala J., Goffeau A.
      Yeast 10:1489-1496(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. "Complete DNA sequence of yeast chromosome II."
      Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
      , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
      EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    6. "Purification and characterization of CTP synthetase, the product of the URA7 gene in Saccharomyces cerevisiae."
      Yang W.-L., McDonough V.M., Ozier-Kalogeropoulos O., Adeline M.-T., Flocco M.T., Carman G.M.
      Biochemistry 33:10785-10793(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-13, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ENZYME REGULATION.
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-422.
      Strain: SUB592.
    9. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiURA7_YEAST
    AccessioniPrimary (citable) accession number: P28274
    Secondary accession number(s): D6VPW0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: October 1, 1994
    Last modified: June 8, 2016
    This is version 152 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 57600 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome II
      Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.