AC MF_00297; DC Protein; auto TR HAMAP; MF_00297; -; 1; level=0 XX Names: Nudix_NudC XX ID NUDC DE RecName: Full=NAD-capped RNA hydrolase NudC; DE Short=DeNADding enzyme NudC; DE EC=3.6.1.-; DE AltName: Full=NADH pyrophosphatase; DE EC=3.6.1.22; GN Name=nudC; XX CC -!- FUNCTION: mRNA decapping enzyme that specifically removes the CC nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by CC hydrolyzing the diphosphate linkage to produce nicotinamide CC mononucleotide (NMN) and 5' monophosphate mRNA. The NAD-cap is present CC at the 5'-end of some mRNAs and stabilizes RNA against 5'-processing. CC Has preference for mRNAs with a 5'-end purine. Catalyzes the hydrolysis CC of a broad range of dinucleotide pyrophosphates. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 5'-end NAD(+)-phospho-ribonucleoside in mRNA + H2O = a 5'- CC end phospho-adenosine-phospho-ribonucleoside in mRNA + beta- CC nicotinamide D-ribonucleotide + 2 H(+); Xref=Rhea:RHEA:60876, CC Rhea:RHEA-COMP:15698, Rhea:RHEA-COMP:15719, ChEBI:CHEBI:14649, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:144029, CC ChEBI:CHEBI:144051; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60877; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + NAD(+) = AMP + beta-nicotinamide D-ribonucleotide + 2 CC H(+); Xref=Rhea:RHEA:11800, ChEBI:CHEBI:14649, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:456215; CC EC=3.6.1.22; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + NADH = AMP + 2 H(+) + reduced beta-nicotinamide D- CC ribonucleotide; Xref=Rhea:RHEA:48868, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57945, ChEBI:CHEBI:90832, CC ChEBI:CHEBI:456215; EC=3.6.1.22; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Note=Divalent metal cations. Mg(2+) or Mn(2+).; case CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 1 zinc ion per subunit.; end case CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudC subfamily. XX DR Pfam; PF00293; NUDIX; 1; trigger=no DR Pfam; PF09296; NUDIX-like; 1; trigger=no DR Pfam; PF09297; zf-NADH-PPase; 1; trigger=no DR PRINTS; PR00502; NUDIXFAMILY; 1; trigger=no DR PROSITE; PS51462; NUDIX; 1; trigger=yes DR PROSITE; PS00893; NUDIX_BOX; 1; trigger=no XX KW Hydrolase KW Magnesium KW Manganese KW Metal-binding KW NAD case KW Zinc end case XX GO GO:0000210; F:NAD+ diphosphatase activity GO GO:0000287; F:magnesium ion binding GO GO:0030145; F:manganese ion binding case GO GO:0008270; F:zinc ion binding end case XX FT From: NUDC_ECOLI (P32664) FT BINDING 192..199 FT /ligand="substrate" FT Optional; Condition: Q-x-W-[PA]-F-P-x-[SN] FT MOTIF 159..180 FT /note="Nudix box" FT BINDING 98 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Tag: zinc; Optional; Condition: C FT BINDING 101 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Tag: zinc; Optional; Condition: C FT BINDING 116 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Tag: zinc; Optional; Condition: C FT BINDING 119 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Tag: zinc; Optional; Condition: C FT BINDING 158 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT Condition: A FT BINDING 174 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT Condition: E FT BINDING 174 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="3" FT Condition: E FT BINDING 178 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT Condition: E FT BINDING 178 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="3" FT Condition: E FT BINDING 219 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT Condition: E FT BINDING 219 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="3" FT Condition: E FT BINDING 25 FT /ligand="substrate" FT Optional; Condition: K FT BINDING 69 FT /ligand="substrate" FT Optional; Condition: R FT BINDING 111 FT /ligand="substrate" FT Optional; Condition: E FT BINDING 124 FT /ligand="substrate" FT Optional; Condition: Y FT BINDING 241 FT /ligand="substrate" FT Optional; Condition: A XX Size: 257-313; Related: None; Template: P32664; Scope: Bacteria Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: Possible wrong start in MYCTU XX # Revision 1.29 2022/11/19 //