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Annotation rule MF_00297 |
General rule information
[?]
Accession |
MF_00297 |
Dates |
1-JUN-2001 (Created) 9-SEP-2020 (Last updated, Version 26) |
Propagated annotation
[?]
Identifier, protein and gene names
[?]
Protein name |
RecName:
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Full=NAD-capped RNA hydrolase NudC;
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Short=DeNADding enzyme NudC;
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EC 3.6.1.-;
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AltName:
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Full=NADH pyrophosphatase;
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EC 3.6.1.22;
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Function |
mRNA decapping enzyme that specifically removes the nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by hydrolyzing the diphosphate linkage to produce nicotinamide mononucleotide (NMN) and 5' monophosphate mRNA. The NAD-cap is present at the 5'-end of some mRNAs and stabilizes RNA against 5'-processing. Has preference for mRNAs with a 5'-end purine. Catalyzes the hydrolysis of a broad range of dinucleotide pyrophosphates. |
Catalytic activity |
RHEA:60876: a 5'-end NAD(+)-phospho-ribonucleoside in mRNA + H2O = a 5'-end phospho-adenosine-phospho-ribonucleoside in mRNA + beta-nicotinamide D-ribonucleotide + 2 H(+)
PhysiologicalDirection=left-to-right
(RHEA:60877)
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RHEA:11800: H2O + NAD(+) = AMP + beta-nicotinamide D-ribonucleotide + 2 H(+)
EC 3.6.1.22
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RHEA:48868: H2O + NADH = AMP + 2 H(+) + reduced beta-nicotinamide D-ribonucleotide
EC 3.6.1.22
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Cofactor |
Mg(2+) Mn(2+) Note: Divalent metal cations. Mg(2+) or Mn(2+). |
case <FTTag:zinc>
Cofactor |
Zn(2+) Note: Binds 1 zinc ion per subunit. |
end case
Subunit |
Homodimer. |
Similarity |
Belongs to the Nudix hydrolase family. NudC subfamily. |
case <FTTag:zinc>
end case
GO:0000210; Molecular function: NAD+ diphosphatase activity.
GO:0000287; Molecular function: magnesium ion binding.
GO:0030145; Molecular function: manganese ion binding.
case <FTTag:zinc>
end case
From: NUDC_ECOLI (P32664) |
Key
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From
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To
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Description
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Tag
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Condition
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FTGroup
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REGION (Optional)
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192
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199
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Substrate binding
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Q-x-W-[PA]-F-P-x-[SN]
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MOTIF
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159
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180
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Nudix box
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METAL (Optional)
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98
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98
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Zinc
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zinc
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C
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METAL (Optional)
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101
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101
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Zinc
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zinc
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C
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METAL (Optional)
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116
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116
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Zinc
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zinc
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C
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METAL (Optional)
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119
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119
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Zinc
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zinc
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C
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METAL
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158
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158
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Divalent metal cation 1; via carbonyl oxygen
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A
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METAL
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174
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174
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Divalent metal cation 2
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E
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METAL
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174
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174
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Divalent metal cation 3
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E
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METAL
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178
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178
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Divalent metal cation 1
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E
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METAL
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178
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178
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Divalent metal cation 3
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E
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METAL
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219
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219
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Divalent metal cation 1
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E
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METAL
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219
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219
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Divalent metal cation 3
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E
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BINDING (Optional)
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25
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25
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Substrate
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K
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BINDING (Optional)
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69
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69
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Substrate
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R
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BINDING (Optional)
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111
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111
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Substrate
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E
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BINDING (Optional)
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124
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124
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Substrate
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Y
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BINDING (Optional)
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241
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241
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Substrate; via amide nitrogen
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A
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Additional information
[?]
Size range |
257-313 amino acids |
Related rules |
None |
Fusion |
None |
Comments |
Possible wrong start in MYCTU |