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Protein

CTP synthase 2

Gene

URA8

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. Plays an important role in the regulation of phospholipid synthesis.

Catalytic activityi

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

Cofactori

Enzyme regulationi

Activated by GTP. Subject to allosteric product inhibition by CTP. Inhibited by p-chloromercuriphenylsulfonic acid, N-ethylmaleimide and cyclopentenylcytosine (CPEC).2 Publications

Kineticsi

  1. KM=74 µM for UTP1 Publication
  2. KM=22 µM for ATP1 Publication
  3. KM=0.14 mM for L-glutamine1 Publication

    pH dependencei

    Optimum pH is 7.5.1 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 sitei537 – 5371For GATase activityPROSITE-ProRule annotation
    Active sitei539 – 5391For 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:YJR103W-MONOMER.
    BRENDAi6.3.4.2. 984.
    ReactomeiR-SCE-499943. Synthesis and interconversion of nucleotide di- and triphosphates.
    UniPathwayiUPA00159; UER00277.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    CTP synthase 2 (EC:6.3.4.2)
    Alternative name(s):
    CTP synthetase 2
    UTP--ammonia ligase 2
    Gene namesi
    Name:URA8
    Ordered Locus Names:YJR103W
    ORF Names:J1962
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componenti: Chromosome X

    Organism-specific databases

    EuPathDBiFungiDB:YJR103W.
    SGDiS000003864. URA8.

    Subcellular locationi

    GO - Cellular componenti

    • cytoophidium Source: SGD
    • cytosol Source: SGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi161 – 1611E → K: Increases the specific activity 2-fold and decreases sensitivity to CTP product inhibition 5-fold. 1 Publication
    Mutagenesisi233 – 2331H → K: No effect on activity and product inhibition by CTP. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 578578CTP synthase 2PRO_0000138284Add
    BLAST

    Proteomic databases

    MaxQBiP38627.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi33859. 33 interactions.
    DIPiDIP-3941N.
    IntActiP38627. 1 interaction.
    MINTiMINT-506319.

    Structurei

    3D structure databases

    ProteinModelPortaliP38627.
    SMRiP38627. Positions 1-567.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini305 – 564260Glutamine 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

    GeneTreeiENSGT00840000131519.
    HOGENOMiHOG000077514.
    InParanoidiP38627.
    KOiK01937.
    OMAiPLMEATV.
    OrthoDBiEOG092C23X9.

    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.

    P38627-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKYVVVSGGV ISGIGKGVLA SSTGMLLKTL GLKVTSIKID PYMNIDAGTM
    60 70 80 90 100
    SPLEHGECFV LDDGGETDLD LGNYERYLGI TLSRDHNITT GKIYSHVISR
    110 120 130 140 150
    ERRGDYLGKT VQIVPHLTNA IQDWIQRVSK IPVDDTGLEP DVCIIELGGT
    160 170 180 190 200
    VGDIESAPFV EALRQFQFEV GRENFALIHV SLVPVIHGEQ KTKPTQAAIK
    210 220 230 240 250
    DLRSLGLIPD MIACRCSEEL NRSTIDKIAM FCHVGPEQVV NVHDVNSTYH
    260 270 280 290 300
    VPLLLLKQHM IDYLHSRLKL GEVPLTLEDK ERGSQLLTNW ENMTKNLDDS
    310 320 330 340 350
    DDVVKIALVG KYTNLKDSYL SVTKSLEHAS MKCRRQLEIL WVEASNLEPE
    360 370 380 390 400
    TQEVDKNKFH DSWNKLSSAD GILVPGGFGT RGIEGMILAA KWARESGVPF
    410 420 430 440 450
    LGVCLGLQVA AIEFARNVIG RPNSSSTEFL DETLLAPEDQ VVIYMPEIDK
    460 470 480 490 500
    EHMGGTMRLG LRPTIFQPNS EWSNIRKLYG EVNEVHERHR HRYEINPKIV
    510 520 530 540 550
    NDMESRGFIF VGKDETGQRC EIFELKGHPY YVGTQYHPEY TSKVLEPSRP
    560 570
    FWGLVAAASG TLGEVIKDIN LSEGNENE
    Length:578
    Mass (Da):64,511
    Last modified:September 21, 2011 - v4
    Checksum:i6381F30814CC2D57
    GO

    Sequence cautioni

    The sequence CAA89633 differs from that shown. Reason: Frameshift at position 559. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti96 – 972HV → QL in CAA48277 (PubMed:8121398).Curated
    Sequence conflicti204 – 2041S → L in CAA48277 (PubMed:8121398).Curated
    Sequence conflicti440 – 4467QVVIYMP → PSSHIHA in CAA48277 (PubMed:8121398).Curated
    Sequence conflicti557 – 5637AASGTLG → QLRHTC in CAA48277 (PubMed:8121398).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X68196 Genomic DNA. Translation: CAA48277.1.
    Z49603 Genomic DNA. Translation: CAA89633.1. Frameshift.
    BK006943 Genomic DNA. Translation: DAA08888.2.
    PIRiS57124.
    RefSeqiNP_012637.4. NM_001181761.4.

    Genome annotation databases

    EnsemblFungiiYJR103W; YJR103W; YJR103W.
    GeneIDi853567.
    KEGGisce:YJR103W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X68196 Genomic DNA. Translation: CAA48277.1.
    Z49603 Genomic DNA. Translation: CAA89633.1. Frameshift.
    BK006943 Genomic DNA. Translation: DAA08888.2.
    PIRiS57124.
    RefSeqiNP_012637.4. NM_001181761.4.

    3D structure databases

    ProteinModelPortaliP38627.
    SMRiP38627. Positions 1-567.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi33859. 33 interactions.
    DIPiDIP-3941N.
    IntActiP38627. 1 interaction.
    MINTiMINT-506319.

    Proteomic databases

    MaxQBiP38627.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYJR103W; YJR103W; YJR103W.
    GeneIDi853567.
    KEGGisce:YJR103W.

    Organism-specific databases

    EuPathDBiFungiDB:YJR103W.
    SGDiS000003864. URA8.

    Phylogenomic databases

    GeneTreeiENSGT00840000131519.
    HOGENOMiHOG000077514.
    InParanoidiP38627.
    KOiK01937.
    OMAiPLMEATV.
    OrthoDBiEOG092C23X9.

    Enzyme and pathway databases

    UniPathwayiUPA00159; UER00277.
    BioCyciYEAST:YJR103W-MONOMER.
    BRENDAi6.3.4.2. 984.
    ReactomeiR-SCE-499943. Synthesis and interconversion of nucleotide di- and triphosphates.

    Miscellaneous databases

    PROiP38627.

    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...

    Entry informationi

    Entry nameiURA8_YEAST
    AccessioniPrimary (citable) accession number: P38627
    Secondary accession number(s): D6VWS2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: September 21, 2011
    Last modified: September 7, 2016
    This is version 154 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 5370 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, 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 X
      Yeast (Saccharomyces cerevisiae) chromosome X: 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.