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The annotation and conditions in this rule are derived from the following entries: P28248 (DCD_ECOLI), Q57872 (DCDB_METJA), P9WP17 (DCDB_MYCTU), Q9KFV3 (DCDB_BACHD)

If a protein meets these conditions... i

Common conditions

Special conditions

    • Subsequence at position 148 - 148 aligns to "Q" in entry P9WP17
    • Subsequence at position 116 - 117 aligns to "G-[FWY]" in entry P9WP17
    • Subsequence at position 148 - 148 does not align to "Q" in entry P9WP17
    • Subsequence at position 116 - 117 does not align to "G-[FWY]" in entry P9WP17
    • Subsequence at position 148 - 148 aligns to "Q" in entry P9WP17
    • Subsequence at position 116 - 117 aligns to "G-[FWY]" in entry P9WP17
    • Subsequence at position 101 - 106 aligns to "[KR]-S-[ST]-x-[GA]-R" in entry P9WP17 (individually applies "dCTP binding")
    • Subsequence at position 119 - 119 aligns to "D" in entry P9WP17 (individually applies "dCTP")
    • Subsequence at position 127 - 129 aligns to "[TV]-L-E" in entry P9WP17 (individually applies "dCTP binding")
    • Subsequence at position 129 - 129 aligns to "E" in entry P9WP17 (individually applies "Proton donor/acceptor")
    • Subsequence at position 162 - 162 aligns to "Y" in entry P9WP17 (individually applies "dCTP")
    • Subsequence at position 170 - 170 aligns to "K" in entry P9WP17 (individually applies "dCTP")
    • Subsequence at position 174 - 174 aligns to "Q" in entry P9WP17 (individually applies "dCTP")

... then these annotations are applied i

Protein namesi

  • Recommended name:
    dCTP deaminase, dUMP-forming (EC:3.5.4.30)
    Alternative name(s):
    DCD-DUT
    Bifunctional dCTP deaminase:dUTPase
  • Recommended name:
    dCTP deaminase (EC:3.5.4.13)
    Alternative name(s):
    Deoxycytidine triphosphate deaminase

Gene namei

  • Name:dcd

Subunit structurei

  • Homotrimer.

Pathwayi

  • Pathwayi: dUMP biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes dUMP from dCTP. This subpathway is part of the pathway dUMP biosynthesis, which is itself part of Pyrimidine metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes dUMP from dCTP, the pathway dUMP biosynthesis and in Pyrimidine metabolism.
  • Pathwayi: dUMP biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes dUMP from dCTP (dUTP route). This subpathway is part of the pathway dUMP biosynthesis, which is itself part of Pyrimidine metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes dUMP from dCTP (dUTP route), the pathway dUMP biosynthesis and in Pyrimidine metabolism.

Sequence similaritiesi

Catalytic activityi

  • dCTP + 2 H2O = dUMP + diphosphate + NH3.
  • dCTP + H2O = dUTP + NH3.

Functioni

  • Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate.
  • Catalyzes the deamination of dCTP to dUTP.

Active sitei

  • Proton donor/acceptor (to residues corresponding to position 129)

Binding sitei

  • dCTP (to residues corresponding to position 148)
  • dCTP (to residues corresponding to position 119)
  • dCTP (to residues corresponding to position 162)
  • dCTP (to residues corresponding to position 170)
  • dCTP (to residues corresponding to position 174)

Nucleotide bindingi

  • dCTP binding (to residues corresponding to positions 101 - 106)
  • dCTP binding (to residues corresponding to positions 127 - 129)

Sitei

  • Important for bifunctional activity (to residues corresponding to positions 116 - 117)

Keywordsi

GO (Gene Ontology) termsi

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