UniProt functional annotation for P32664

UniProt code: P32664.

Organism:		Escherichia coli (strain K12).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.
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 (PubMed:25533955, PubMed:27561816, PubMed:27428510). The NAD-cap is present at the 5'-end of some mRNAs and stabilizes RNA against 5'-processing (PubMed:25533955). Has preference for mRNAs with a 5'-end purine (PubMed:27428510). Catalyzes the hydrolysis of a broad range of dinucleotide pyrophosphates, but uniquely prefers the reduced form of NADH (PubMed:7829480, PubMed:25533955). {ECO:0000269|PubMed:25533955, ECO:0000269|PubMed:27428510, ECO:0000269|PubMed:27561816, ECO:0000269|PubMed:7829480}.
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; Evidence={ECO:0000269|PubMed:25533955, ECO:0000269|PubMed:27428510, ECO:0000269|PubMed:27561816}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60877; Evidence={ECO:0000269|PubMed:25533955, ECO:0000269|PubMed:27428510, ECO:0000269|PubMed:27561816};
Catalytic activity:		Reaction=H2O + NAD(+) = AMP + beta-nicotinamide D-ribonucleotide + 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; Evidence={ECO:0000269|PubMed:25533955, ECO:0000269|PubMed:7829480};
Catalytic activity:		Reaction=H2O + NADH = AMP + 2 H(+) + reduced beta-nicotinamide D- ribonucleotide; Xref=Rhea:RHEA:48868, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57945, ChEBI:CHEBI:90832, ChEBI:CHEBI:456215; EC=3.6.1.22; Evidence={ECO:0000269|PubMed:25533955, ECO:0000269|PubMed:7829480};
Cofactor:		Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:27561816, ECO:0000269|PubMed:7829480}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:7829480}; Note=Divalent metal cations. Mg(2+) or Mn(2+). {ECO:0000269|PubMed:7829480};
Cofactor:		Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:27428510, ECO:0000269|PubMed:27561816, ECO:0000269|Ref.8}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:27428510, ECO:0000269|PubMed:27561816, ECO:0000269|Ref.8};
Biophysicochemical properties:		Kinetic parameters: KM=0.11 mM for NADH {ECO:0000269|PubMed:7829480}; KM=5.1 mM for NAD(+) {ECO:0000269|PubMed:7829480}; KM=0.29 mM for deamino-NADH {ECO:0000269|PubMed:7829480}; KM=2.6 mM for deamino-NAD(+) {ECO:0000269|PubMed:7829480}; KM=0.67 mM for AppA {ECO:0000269|PubMed:7829480}; KM=1.8 mM for ADP-ribose {ECO:0000269|PubMed:7829480}; Vmax=7.6 umol/min/mg enzyme with NADH as substrate {ECO:0000269|PubMed:7829480}; Vmax=2.9 umol/min/mg enzyme with NAD(+) as substrate {ECO:0000269|PubMed:7829480}; Vmax=8.9 umol/min/mg enzyme with deamino-NADH as substrate {ECO:0000269|PubMed:7829480}; Vmax=3.2 umol/min/mg enzyme with deamino-NAD(+) as substrate {ECO:0000269|PubMed:7829480}; Vmax=4.7 umol/min/mg enzyme with AppA as substrate {ECO:0000269|PubMed:7829480}; Vmax=4.8 umol/min/mg enzyme with ADP-ribose as substrate {ECO:0000269|PubMed:7829480}; pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:7829480};
Subunit:		Homodimer. {ECO:0000269|PubMed:27428510, ECO:0000269|PubMed:27561816, ECO:0000305|PubMed:7829480, ECO:0000305|Ref.8}.
Similarity:		Belongs to the Nudix hydrolase family. NudC subfamily. {ECO:0000305}.
Sequence caution:		Sequence=D12624; Type=Frameshift; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.