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Protein

CTP synthase

Gene

pyrG

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
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 (PubMed:15296735). Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates (By similarity).UniRule annotation1 Publication

Catalytic activityi

ATP + UTP + L-glutamine = ADP + phosphate + CTP + L-glutamate.UniRule annotation1 Publication

Enzyme regulationi

Allosterically activated by GTP, when glutamine is the substrate (PubMed:15296735). GTP has no effect on the reaction when ammonia is the substrate. The allosteric effector GTP functions by stabilizing the protein conformation that binds the tetrahedral intermediate(s) formed during glutamine hydrolysis. Inhibited by the product CTP, via allosteric rather than competitive inhibition (By similarity).UniRule annotation1 Publication

Kineticsi

kcat is 7.4 sec(-1) toward L-glutamine at unsaturating levels of ATP and UTP (0.5 mM) and 40 sec(-1) in the presence of GTP. kcat is 260 sec(-1) toward UTP.1 Publication

  1. KM=0.24 mM for L-glutamine (at unsaturating levels of ATP and UTP (0.5 mM))1 Publication
  2. KM=0.22 mM for L-glutamine (in the presence of GTP)1 Publication
  3. KM=0.37 mM for UTP1 Publication

    Pathwayi: CTP biosynthesis via de novo pathway

    This protein is involved in step 2 of the subpathway that synthesizes CTP from UDP.UniRule annotation
    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 (pyrG)
    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
    Binding sitei23 – 231Allosteric inhibitor CTP; alternateUniRule annotation
    Binding sitei23 – 231UTP; alternateUniRule annotation
    Binding sitei64 – 641L-glutamineCombined sources1 Publication
    Metal bindingi81 – 811MagnesiumUniRule annotation
    Binding sitei81 – 811ATPUniRule annotation
    Metal bindingi151 – 1511MagnesiumUniRule annotation
    Binding sitei234 – 2341Allosteric inhibitor CTP; alternateUniRule annotation
    Binding sitei234 – 2341UTP; alternateUniRule annotation
    Binding sitei252 – 2521ATP; via amide nitrogenUniRule annotation
    Binding sitei364 – 3641L-glutamine; via carbonyl oxygenCombined sources1 Publication
    Active sitei391 – 3911Nucleophile; for glutamine hydrolysisUniRule annotation1 Publication
    Binding sitei415 – 4151L-glutamineCombined sources1 Publication
    Binding sitei472 – 4721L-glutamine; via amide nitrogenCombined sources1 Publication
    Active sitei522 – 5221UniRule annotation1 Publication
    Active sitei524 – 5241UniRule annotation1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi24 – 296ATPUniRule annotation
    Nucleotide bindingi158 – 1603Allosteric inhibitor CTPUniRule annotation
    Nucleotide bindingi198 – 2036Allosteric inhibitor CTP; alternateUniRule annotation
    Nucleotide bindingi198 – 2036UTP; alternateUniRule annotation

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Pyrimidine biosynthesis

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciTTHE300852:GH8R-1502-MONOMER.
    BRENDAi6.3.4.2. 7852.
    UniPathwayiUPA00159; UER00277.

    Protein family/group databases

    MEROPSiC26.964.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    CTP synthaseUniRule annotation (EC:6.3.4.2UniRule annotation1 Publication)
    Alternative name(s):
    Cytidine 5'-triphosphate synthaseUniRule annotation
    Cytidine triphosphate synthetaseUniRule annotation
    Short name:
    CTP synthetase1 PublicationUniRule annotation
    Short name:
    CTPSUniRule annotation
    UTP--ammonia ligaseUniRule annotation
    Gene namesi
    Name:pyrGUniRule annotation
    Ordered Locus Names:TTHA1466
    OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
    Taxonomic identifieri300852 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
    Proteomesi
    • UP000000532 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 550550CTP synthasePRO_0000266251Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer in the presence of UTP and ATP. Is in a protein concentration-dependent equilibrium between monomer, dimer, and tetramer in the absence of UTP and ATP.1 Publication

    Protein-protein interaction databases

    STRINGi300852.TTHA1466.

    Structurei

    Secondary structure

    1
    550
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi13 – 197Combined sources
    Beta strandi21 – 233Combined sources
    Helixi27 – 3913Combined sources
    Turni40 – 423Combined sources
    Beta strandi45 – 517Combined sources
    Helixi58 – 603Combined sources
    Helixi81 – 899Combined sources
    Helixi95 – 973Combined sources
    Beta strandi98 – 1003Combined sources
    Helixi101 – 11313Combined sources
    Turni114 – 1196Combined sources
    Turni124 – 1263Combined sources
    Helixi127 – 14216Combined sources
    Beta strandi146 – 1527Combined sources
    Helixi159 – 1613Combined sources
    Helixi162 – 1698Combined sources
    Helixi171 – 1755Combined sources
    Beta strandi179 – 1879Combined sources
    Turni192 – 1954Combined sources
    Helixi200 – 21112Combined sources
    Beta strandi217 – 2259Combined sources
    Helixi229 – 23911Combined sources
    Helixi243 – 2453Combined sources
    Beta strandi246 – 2505Combined sources
    Helixi257 – 2659Combined sources
    Helixi267 – 2748Combined sources
    Helixi285 – 29511Combined sources
    Beta strandi298 – 30811Combined sources
    Helixi314 – 3163Combined sources
    Helixi317 – 32913Combined sources
    Beta strandi332 – 3409Combined sources
    Helixi341 – 3433Combined sources
    Helixi349 – 3524Combined sources
    Turni353 – 3553Combined sources
    Beta strandi359 – 3613Combined sources
    Helixi370 – 38213Combined sources
    Beta strandi387 – 3904Combined sources
    Helixi392 – 40413Combined sources
    Turni414 – 4163Combined sources
    Beta strandi423 – 4286Combined sources
    Helixi430 – 4323Combined sources
    Beta strandi442 – 4509Combined sources
    Helixi455 – 4606Combined sources
    Beta strandi463 – 47513Combined sources
    Helixi477 – 48610Combined sources
    Beta strandi488 – 4936Combined sources
    Beta strandi497 – 5015Combined sources
    Beta strandi505 – 5106Combined sources
    Beta strandi513 – 5219Combined sources
    Helixi523 – 5264Combined sources
    Beta strandi529 – 5313Combined sources
    Helixi534 – 54613Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1VCMX-ray2.35A1-550[»]
    1VCNX-ray2.25A1-550[»]
    1VCOX-ray2.15A1-550[»]
    ProteinModelPortaliQ5SIA8.
    SMRiQ5SIA8. Positions 10-548.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ5SIA8.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini302 – 549248Glutamine amidotransferase type-1UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 277277Amidoligase domainUniRule annotationAdd
    BLAST
    Regioni392 – 3954L-glutamine bindingCombined sources1 Publication

    Sequence similaritiesi

    Belongs to the CTP synthase family.UniRule annotation
    Contains 1 glutamine amidotransferase type-1 domain.UniRule annotation

    Keywords - Domaini

    Glutamine amidotransferase

    Phylogenomic databases

    eggNOGiENOG4105C8D. Bacteria.
    COG0504. LUCA.
    HOGENOMiHOG000077515.
    KOiK01937.
    OMAiTMRLGEY.
    PhylomeDBiQ5SIA8.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    3.40.50.880. 1 hit.
    HAMAPiMF_01227. PyrG. 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.

    Q5SIA8-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MNGSADAGPR PRKYVFITGG VVSSLGKGIL TSSLGALLRA RGYRVTAIKI
    60 70 80 90 100
    DPYVNVDAGT MRPYEHGEVF VTADGAETDL DIGHYERFLD MDLSRGNNLT
    110 120 130 140 150
    TGQVYLSVIQ KERRGEYLSQ TVQVIPHITD EIKERIRKVA EEQKAEIVVV
    160 170 180 190 200
    EVGGTVGDIE SLPFLEAIRQ FRFDEGEGNT LYLHLTLVPY LETSEEFKTK
    210 220 230 240 250
    PTQHSVATLR GVGIQPDILV LRSARPVPEE VRRKVALFTN VRPGHVFSSP
    260 270 280 290 300
    TVEHLYEVPL LLEEQGLGRA VERALGLEAV IPNLSFWQEA VRVLKHPERT
    310 320 330 340 350
    VKIAIAGKYV KMPDAYLSLL EALRHAGIKN RARVEVKWVD AESLEAADLD
    360 370 380 390 400
    EAFRDVSGIL VPGGFGVRGI EGKVRAAQYA RERKIPYLGI CLGLQIAVIE
    410 420 430 440 450
    FARNVAGLKG ANSTEFDPHT PHPVIDLMPE QLEVEGLGGT MRLGDWPMRI
    460 470 480 490 500
    KPGTLLHRLY GKEEVLERHR HRYEVNPLYV DGLERAGLVV SATTPGMRGR
    510 520 530 540 550
    GAGLVEAIEL KDHPFFLGLQ SHPEFKSRPM RPSPPFVGFV EAALAYQERA
    Length:550
    Mass (Da):61,003
    Last modified:December 21, 2004 - v1
    Checksum:iF3D20D9FC50DFDF8
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AP008226 Genomic DNA. Translation: BAD71289.1.
    RefSeqiWP_011228700.1. NC_006461.1.
    YP_144732.1. NC_006461.1.

    Genome annotation databases

    EnsemblBacteriaiBAD71289; BAD71289; BAD71289.
    GeneIDi3169502.
    KEGGittj:TTHA1466.
    PATRICi23957889. VBITheThe93045_1440.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AP008226 Genomic DNA. Translation: BAD71289.1.
    RefSeqiWP_011228700.1. NC_006461.1.
    YP_144732.1. NC_006461.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1VCMX-ray2.35A1-550[»]
    1VCNX-ray2.25A1-550[»]
    1VCOX-ray2.15A1-550[»]
    ProteinModelPortaliQ5SIA8.
    SMRiQ5SIA8. Positions 10-548.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi300852.TTHA1466.

    Protein family/group databases

    MEROPSiC26.964.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiBAD71289; BAD71289; BAD71289.
    GeneIDi3169502.
    KEGGittj:TTHA1466.
    PATRICi23957889. VBITheThe93045_1440.

    Phylogenomic databases

    eggNOGiENOG4105C8D. Bacteria.
    COG0504. LUCA.
    HOGENOMiHOG000077515.
    KOiK01937.
    OMAiTMRLGEY.
    PhylomeDBiQ5SIA8.

    Enzyme and pathway databases

    UniPathwayiUPA00159; UER00277.
    BioCyciTTHE300852:GH8R-1502-MONOMER.
    BRENDAi6.3.4.2. 7852.

    Miscellaneous databases

    EvolutionaryTraceiQ5SIA8.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    3.40.50.880. 1 hit.
    HAMAPiMF_01227. PyrG. 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 nameiPYRG_THET8
    AccessioniPrimary (citable) accession number: Q5SIA8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 12, 2006
    Last sequence update: December 21, 2004
    Last modified: September 7, 2016
    This is version 86 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    CTPSs have evolved a hybrid strategy for distinguishing between UTP and CTP. The overlapping regions of the product feedback inhibitory and substrate sites recognize a common feature in both compounds, the triphosphate moiety. To differentiate isosteric substrate and product pyrimidine rings, an additional pocket far from the expected kinase/ligase catalytic site, specifically recognizes the cytosine and ribose portions of the product inhibitor.UniRule annotation

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    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.