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Protein

CTP synthase

Gene

pyrG

Organism
Escherichia coli (strain K12)
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. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.1 Publication2 Publications

Catalytic activityi

ATP + UTP + L-glutamine = ADP + phosphate + CTP + L-glutamate.3 Publications

Enzyme regulationi

Allosterically activated by GTP, when glutamine is the substrate; GTP has no effect on the reaction when ammonia is the substrate (PubMed:4550559). The allosteric effector GTP functions by stabilizing the protein conformation that binds the tetrahedral intermediate(s) formed during glutamine hydrolysis (PubMed:11336655). Also activated by magnesium; the enzyme requires more Mg2+ for full catalytic activity than required simply to complex the nucleotide substrates (PubMed:8385490). Inhibited by the product CTP, via allosteric rather than competitive inhibition (PubMed:8385490, PubMed:16216072). Also inhibited by divalent metal ions such as copper and zinc (PubMed:8385490). Is potently inhibited by the intermediate analog inhibitor glutamate gamma-semialdehyde (PubMed:11336655).1 Publication3 Publications

Kineticsi

kcat is 13 sec(-1) with ammonia as substrate. kcat is 6.6 sec(-1) with L-glutamine as substrate (in the presence of 0.25 mM GTP).1 Publication

  1. KM=2.0 mM for ammonia1 Publication
  2. KM=0.30 mM for L-glutamine (in the presence of 0.25 mM GTP)1 Publication

    pH dependencei

    Optimum pH is 8.7.1 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 sitei14 – 141Allosteric inhibitor CTP; alternate1 Publication
    Binding sitei14 – 141UTP; alternate1 Publication
    Metal bindingi72 – 721MagnesiumCombined sources1 Publication
    Binding sitei72 – 721ATPCombined sources1 Publication
    Metal bindingi140 – 1401MagnesiumCombined sources1 Publication
    Binding sitei223 – 2231Allosteric inhibitor CTP; alternateCombined sources1 Publication
    Binding sitei223 – 2231UTP; alternate1 Publication
    Binding sitei352 – 3521L-glutamine; via carbonyl oxygenUniRule annotation
    Active sitei379 – 3791Nucleophile; for glutamine hydrolysis2 Publications
    Binding sitei403 – 4031L-glutamineUniRule annotation
    Binding sitei470 – 4701L-glutamine; via amide nitrogenUniRule annotation
    Active sitei515 – 51511 Publication
    Active sitei517 – 51711 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi15 – 206ATPCombined sources1 Publication
    Nucleotide bindingi147 – 1493Allosteric inhibitor CTPCombined sources1 Publication
    Nucleotide bindingi187 – 1926Allosteric inhibitor CTP; alternateCombined sources1 Publication
    Nucleotide bindingi187 – 1926UTP; alternate1 Publication
    Nucleotide bindingi239 – 2413ATPCombined sources1 Publication

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-KW
    • CTP synthase activity Source: EcoCyc
    • identical protein binding Source: EcoCyc

    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

    BioCyciEcoCyc:CTPSYN-MONOMER.
    ECOL316407:JW2751-MONOMER.
    MetaCyc:CTPSYN-MONOMER.
    BRENDAi6.3.4.2. 2026.
    UniPathwayiUPA00159; UER00277.

    Protein family/group databases

    MEROPSiC26.964.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    CTP synthase1 Publication (EC:6.3.4.23 Publications)
    Alternative name(s):
    Cytidine 5'-triphosphate synthase1 Publication
    Cytidine triphosphate synthetase1 Publication
    Short name:
    CTP synthetase1 Publication
    Short name:
    CTPS1 Publication
    UTP--ammonia ligase
    Gene namesi
    Name:pyrG1 Publication
    Ordered Locus Names:b2780, JW2751
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10810. pyrG.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: UniProtKB
    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi349 – 3491V → S: 30% increase in both glutamine-dependent and ammonia-dependent activities. 1 Publication
    Mutagenesisi352 – 3521G → P: Loss of glutamine-dependent activity, but no change in ammonia-dependent activity. 1 Publication
    Mutagenesisi379 – 3791C → A or S: Loss of glutamine-dependent activity, but no change in ammonia-dependent activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemoved1 Publication
    Chaini2 – 545544CTP synthasePRO_0000138183Add
    BLAST

    Proteomic databases

    EPDiP0A7E5.
    PaxDbiP0A7E5.
    PRIDEiP0A7E5.

    2D gel databases

    SWISS-2DPAGEP0A7E5.

    Interactioni

    Subunit structurei

    Homodimer that associates to form homotetramer in the presence of ATP and UTP. The substrate nucleotides ATP and UTP act synergistically to promote oligomerization of CTPS from inactive dimers to active tetramers.1 Publication

    GO - Molecular functioni

    • identical protein binding Source: EcoCyc

    Protein-protein interaction databases

    DIPiDIP-10628N.
    IntActiP0A7E5. 8 interactions.
    STRINGi511145.b2780.

    Structurei

    Secondary structure

    1
    545
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 107Combined sources
    Beta strandi12 – 143Combined sources
    Helixi18 – 3013Combined sources
    Turni31 – 333Combined sources
    Beta strandi36 – 427Combined sources
    Helixi49 – 513Combined sources
    Turni54 – 563Combined sources
    Beta strandi60 – 623Combined sources
    Beta strandi68 – 703Combined sources
    Helixi72 – 798Combined sources
    Helixi86 – 883Combined sources
    Beta strandi89 – 913Combined sources
    Helixi92 – 10413Combined sources
    Turni105 – 1106Combined sources
    Helixi115 – 13117Combined sources
    Beta strandi135 – 1417Combined sources
    Helixi148 – 1503Combined sources
    Helixi151 – 16414Combined sources
    Beta strandi168 – 1769Combined sources
    Turni181 – 1844Combined sources
    Helixi189 – 19911Combined sources
    Turni200 – 2023Combined sources
    Beta strandi206 – 2149Combined sources
    Helixi218 – 2269Combined sources
    Helixi232 – 2343Combined sources
    Beta strandi235 – 2395Combined sources
    Helixi244 – 2463Combined sources
    Helixi247 – 2537Combined sources
    Helixi256 – 2638Combined sources
    Helixi274 – 28411Combined sources
    Beta strandi287 – 29812Combined sources
    Helixi302 – 3054Combined sources
    Helixi306 – 31813Combined sources
    Beta strandi321 – 3299Combined sources
    Helixi330 – 3367Combined sources
    Turni338 – 3436Combined sources
    Beta strandi345 – 3495Combined sources
    Helixi358 – 37013Combined sources
    Beta strandi375 – 3784Combined sources
    Helixi380 – 39415Combined sources
    Turni402 – 4043Combined sources
    Beta strandi411 – 4144Combined sources
    Turni416 – 4183Combined sources
    Beta strandi440 – 4489Combined sources
    Helixi453 – 4575Combined sources
    Beta strandi460 – 46910Combined sources
    Helixi475 – 4839Combined sources
    Beta strandi487 – 4915Combined sources
    Beta strandi493 – 4953Combined sources
    Beta strandi498 – 5025Combined sources
    Beta strandi506 – 5149Combined sources
    Helixi516 – 5183Combined sources
    Turni522 – 5243Combined sources
    Helixi527 – 54216Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1S1MX-ray2.30A/B1-545[»]
    2AD5X-ray2.80A/B1-545[»]
    ProteinModelPortaliP0A7E5.
    SMRiP0A7E5. Positions 1-545.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A7E5.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini291 – 542252Glutamine amidotransferase type-1UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 266265Amidoligase domain1 PublicationAdd
    BLAST
    Regioni380 – 3834L-glutamine bindingUniRule annotation

    Domaini

    Sequence consists of two domains: the C-terminal glutamine amide transfer (GAT) domain catalyzes the hydrolysis of glutamine; the N-terminal synthase domain catalyzes the amination of UTP (PubMed:3514618, PubMed:3298209). Structure shows each subunit consists of three distinct segments: the N-terminal amidoligase (ALase) domain, which mediates oligomerization and contains the ALase active site where ATP and UTP substrates bind, and an interrupted helical interdomain linker segment that connects the ALase domain to the Type I glutamine amidotransferase (GATase) C-terminal domain, which generates ammonia via glutamine hydrolysis (PubMed:15157079). A gated channel that spans 25 Angstroms between the glutamine hydrolysis and amidoligase active sites provides a path for ammonia diffusion; the channel is accessible to solvent at the base of a cleft adjoining the glutamine hydrolysis active site, providing an entry point for exogenous ammonia (PubMed:15157079).3 Publications

    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.
    InParanoidiP0A7E5.
    KOiK01937.
    OMAiMRLGEYE.
    OrthoDBiEOG6RC3NR.
    PhylomeDBiP0A7E5.

    Family and domain databases

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

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0A7E5-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTTNYIFVTG GVVSSLGKGI AAASLAAILE ARGLNVTIMK LDPYINVDPG
    60 70 80 90 100
    TMSPIQHGEV FVTEDGAETD LDLGHYERFI RTKMSRRNNF TTGRIYSDVL
    110 120 130 140 150
    RKERRGDYLG ATVQVIPHIT NAIKERVLEG GEGHDVVLVE IGGTVGDIES
    160 170 180 190 200
    LPFLEAIRQM AVEIGREHTL FMHLTLVPYM AASGEVKTKP TQHSVKELLS
    210 220 230 240 250
    IGIQPDILIC RSDRAVPANE RAKIALFCNV PEKAVISLKD VDSIYKIPGL
    260 270 280 290 300
    LKSQGLDDYI CKRFSLNCPE ANLSEWEQVI FEEANPVSEV TIGMVGKYIE
    310 320 330 340 350
    LPDAYKSVIE ALKHGGLKNR VSVNIKLIDS QDVETRGVEI LKGLDAILVP
    360 370 380 390 400
    GGFGYRGVEG MITTARFARE NNIPYLGICL GMQVALIDYA RHVANMENAN
    410 420 430 440 450
    STEFVPDCKY PVVALITEWR DENGNVEVRS EKSDLGGTMR LGAQQCQLVD
    460 470 480 490 500
    DSLVRQLYNA PTIVERHRHR YEVNNMLLKQ IEDAGLRVAG RSGDDQLVEI
    510 520 530 540
    IEVPNHPWFV ACQFHPEFTS TPRDGHPLFA GFVKAASEFQ KRQAK
    Length:545
    Mass (Da):60,374
    Last modified:January 23, 2007 - v2
    Checksum:iFBB9E2E18FA355FC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti338 – 3381V → L in AAA24485 (PubMed:3514618).Curated
    Sequence conflicti476 – 4761M → S in AAA24485 (PubMed:3514618).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M12843 mRNA. Translation: AAA24485.1.
    U29580 Genomic DNA. Translation: AAA69290.1.
    U00096 Genomic DNA. Translation: AAC75822.1.
    AP009048 Genomic DNA. Translation: BAE76854.1.
    PIRiH65059. SYECTP.
    RefSeqiNP_417260.1. NC_000913.3.
    WP_000210878.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75822; AAC75822; b2780.
    BAE76854; BAE76854; BAE76854.
    GeneIDi946116.
    KEGGiecj:JW2751.
    eco:b2780.
    PATRICi32120976. VBIEscCol129921_2880.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M12843 mRNA. Translation: AAA24485.1.
    U29580 Genomic DNA. Translation: AAA69290.1.
    U00096 Genomic DNA. Translation: AAC75822.1.
    AP009048 Genomic DNA. Translation: BAE76854.1.
    PIRiH65059. SYECTP.
    RefSeqiNP_417260.1. NC_000913.3.
    WP_000210878.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1S1MX-ray2.30A/B1-545[»]
    2AD5X-ray2.80A/B1-545[»]
    ProteinModelPortaliP0A7E5.
    SMRiP0A7E5. Positions 1-545.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-10628N.
    IntActiP0A7E5. 8 interactions.
    STRINGi511145.b2780.

    Protein family/group databases

    MEROPSiC26.964.

    2D gel databases

    SWISS-2DPAGEP0A7E5.

    Proteomic databases

    EPDiP0A7E5.
    PaxDbiP0A7E5.
    PRIDEiP0A7E5.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75822; AAC75822; b2780.
    BAE76854; BAE76854; BAE76854.
    GeneIDi946116.
    KEGGiecj:JW2751.
    eco:b2780.
    PATRICi32120976. VBIEscCol129921_2880.

    Organism-specific databases

    EchoBASEiEB0803.
    EcoGeneiEG10810. pyrG.

    Phylogenomic databases

    eggNOGiENOG4105C8D. Bacteria.
    COG0504. LUCA.
    HOGENOMiHOG000077515.
    InParanoidiP0A7E5.
    KOiK01937.
    OMAiMRLGEYE.
    OrthoDBiEOG6RC3NR.
    PhylomeDBiP0A7E5.

    Enzyme and pathway databases

    UniPathwayiUPA00159; UER00277.
    BioCyciEcoCyc:CTPSYN-MONOMER.
    ECOL316407:JW2751-MONOMER.
    MetaCyc:CTPSYN-MONOMER.
    BRENDAi6.3.4.2. 2026.

    Miscellaneous databases

    EvolutionaryTraceiP0A7E5.
    PROiP0A7E5.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    3.40.50.880. 1 hit.
    HAMAPiMF_01227. PyrG.
    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. "Nucleotide sequence of Escherichia coli pyrG encoding CTP synthetase."
      Weng M., Makaroff C.A., Zalkin H.
      J. Biol. Chem. 261:5568-5574(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DOMAIN.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
      Link A.J., Robison K., Church G.M.
      Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-13.
      Strain: K12 / EMG2.
    5. "Role of an allosteric effector. Guanosine triphosphate activation in cytosine triphosphate synthetase."
      Levitzki A., Koshland D.E. Jr.
      Biochemistry 11:241-246(1972) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION.
    6. "Ligand-induced dimer-to-tetramer transformation in cytosine triphosphate synthetase."
      Levitzki A., Koshland D.E. Jr.
      Biochemistry 11:247-253(1972) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    7. "Structural role for a conserved region in the CTP synthetase glutamine amide transfer domain."
      Weng M., Zalkin H.
      J. Bacteriol. 169:3023-3028(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN, MUTAGENESIS OF VAL-349; GLY-351 AND GLY-352.
    8. "Characterization of metal ion activation and inhibition of CTP synthetase."
      Robertson J.G., Villafranca J.J.
      Biochemistry 32:3769-3777(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    9. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    10. "Inhibition of Escherichia coli CTP synthase by glutamate gamma-semialdehyde and the role of the allosteric effector GTP in glutamine hydrolysis."
      Bearne S.L., Hekmat O., MacDonnell J.E.
      Biochem. J. 356:223-232(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, MUTAGENESIS OF CYS-379, ACTIVE SITE.
    11. "Crystal structure of Escherichia coli cytidine triphosphate synthetase, a nucleotide-regulated glutamine amidotransferase/ATP-dependent amidoligase fusion protein and homologue of anticancer and antiparasitic drug targets."
      Endrizzi J.A., Kim H., Anderson P.M., Baldwin E.P.
      Biochemistry 43:6447-6463(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS), FUNCTION, DOMAIN, ACTIVE SITE.
    12. "Mechanisms of product feedback regulation and drug resistance in cytidine triphosphate synthetases from the structure of a CTP-inhibited complex."
      Endrizzi J.A., Kim H., Anderson P.M., Baldwin E.P.
      Biochemistry 44:13491-13499(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH ADP; CTP AND MAGNESIUM, ENZYME REGULATION.

    Entry informationi

    Entry nameiPYRG_ECOLI
    AccessioniPrimary (citable) accession number: P0A7E5
    Secondary accession number(s): P08398, Q2MA52
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: January 23, 2007
    Last modified: July 6, 2016
    This is version 103 of the entry and version 2 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.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. 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.