HAMAP rule MF_00297
General rule information
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| Accession | MF_00297 |
| Dates | 1-JUN-2001 (Created)
2-SEP-2024 (Last updated, Version 30) |
| Name | Nudix_NudC |
| Scope(s) |
Bacteria |
| Template(s) | P32664 (NUDC_ECOLI); [ Recover all ] |
| Triggered by |
HAMAP; MF_00297 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | NUDC |
| Protein name | RecName: Full=NAD-capped RNA hydrolase NudC; Short=DeNADding enzyme NudC; EC=3.6.1.-; AltName: Full=NADH pyrophosphatase; EC=3.6.1.22; |
| Gene name | Name=nudC; |
Comments
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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 | Reaction=a 5'-end NAD(+)-phospho-ribonucleoside in mRNA + H2O = a 5'- end phospho-adenosine-phospho-ribonucleoside in mRNA + beta- nicotinamide D-ribonucleotide + 2 H(+); Xref=Rhea:RHEA:60876, Rhea:RHEA-COMP:15698, Rhea:RHEA-COMP:15719, ChEBI:CHEBI:14649, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:144029, ChEBI:CHEBI:144051; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60877; |
| CATALYTIC ACTIVITY | Reaction=NAD(+) + H2O = beta-nicotinamide D-ribonucleotide + AMP + 2 H(+); Xref=Rhea:RHEA:11800, ChEBI:CHEBI:14649, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:456215; EC=3.6.1.22; |
| CATALYTIC ACTIVITY | Reaction=NADH + H2O = reduced beta-nicotinamide D-ribonucleotide + AMP + 2 H(+); Xref=Rhea:RHEA:48868, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57945, ChEBI:CHEBI:90832, ChEBI:CHEBI:456215; EC=3.6.1.22; |
| COFACTOR | Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Note=Divalent metal cations. Mg(2+) or Mn(2+).; |
| case <FTTag:zinc> | |
| COFACTOR | Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.; |
| end case | |
| SUBUNIT | Homodimer. |
| SIMILARITY | Belongs to the Nudix hydrolase family. NudC subfamily. |
Keywords
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Gene Ontology
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| GO:0000210; Molecular function:NAD+ diphosphatase activity | |
| GO:0000287; Molecular function:magnesium ion binding | |
| GO:0030145; Molecular function:manganese ion binding | |
| case <FTTag:zinc> | |
| GO:0008270; Molecular function:zinc ion binding | |
| end case | |
Cross-references
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| Pfam | PF00293; NUDIX; 1; |
| Pfam | PF09296; NUDIX-like; 1; |
| Pfam | PF09297; zf-NADH-PPase; 1; |
| PRINTS | PR00502; NUDIXFAMILY; 1; |
| PROSITE | PS51462; NUDIX; 1; |
| PROSITE | PS00893; NUDIX_BOX; 1; |
Features
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| From: NUDC_ECOLI (P32664) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 192 | 199 | /ligand="substrate" | Q-x-W-[PA]-F-P-x-[SN] | ||||||||
| MOTIF | 159 | 180 | /note="Nudix box" | |||||||||
| BINDING | 98 | 98 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
zinc | C | |||||||
| BINDING | 101 | 101 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
zinc | C | |||||||
| BINDING | 116 | 116 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
zinc | C | |||||||
| BINDING | 119 | 119 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
zinc | C | |||||||
| BINDING | 158 | 158 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="1" |
A | ||||||||
| BINDING | 174 | 174 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="2" |
E | ||||||||
| BINDING | 174 | 174 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="3" |
E | ||||||||
| BINDING | 178 | 178 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="1" |
E | ||||||||
| BINDING | 178 | 178 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="3" |
E | ||||||||
| BINDING | 219 | 219 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="1" |
E | ||||||||
| BINDING | 219 | 219 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="3" |
E | ||||||||
| BINDING | 25 | 25 | /ligand="substrate" | K | ||||||||
| BINDING | 69 | 69 | /ligand="substrate" | R | ||||||||
| BINDING | 111 | 111 | /ligand="substrate" | E | ||||||||
| BINDING | 124 | 124 | /ligand="substrate" | Y | ||||||||
| BINDING | 241 | 241 | /ligand="substrate" | A | ||||||||
Additional information
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| Size range | 257-313 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |
| Comments | Possible wrong start in MYCTU |