A0A3V2G391 · A0A3V2G391_SALET
- ProteinNAD-capped RNA hydrolase NudC
- GenenudC
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids257 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
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
- NAD+ + H2O = beta-nicotinamide D-ribonucleotide + AMP + 2 H+
- a 5'-end NAD+-phospho-ribonucleoside in mRNA + H2O = a 5'-end phospho-adenosine-phospho-ribonucleoside in mRNA + beta-nicotinamide D-ribonucleotide + 2 H+This reaction proceeds in the forward direction.
Cofactor
Protein has several cofactor binding sites:
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Note: Divalent metal cations. Mg2+ or Mn2+.
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 69 | substrate | |||
Binding site | 98 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 101 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 111 | substrate | |||
Binding site | 116 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 119 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 124 | substrate | |||
Binding site | 158 | a divalent metal cation 1 (UniProtKB | ChEBI) | |||
Binding site | 174 | a divalent metal cation 2 (UniProtKB | ChEBI) | |||
Binding site | 174 | a divalent metal cation 3 (UniProtKB | ChEBI) | |||
Binding site | 178 | a divalent metal cation 1 (UniProtKB | ChEBI) | |||
Binding site | 178 | a divalent metal cation 3 (UniProtKB | ChEBI) | |||
Binding site | 192-199 | substrate | |||
Binding site | 219 | a divalent metal cation 3 (UniProtKB | ChEBI) | |||
Binding site | 219 | a divalent metal cation 1 (UniProtKB | ChEBI) | |||
Binding site | 241 | substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | magnesium ion binding | |
Molecular Function | manganese ion binding | |
Molecular Function | NAD+ diphosphatase activity | |
Molecular Function | NADH pyrophosphatase activity | |
Molecular Function | zinc ion binding | |
Biological Process | NAD catabolic process | |
Biological Process | NADH metabolic process | |
Biological Process | NADP catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNAD-capped RNA hydrolase NudC
- EC number
- Short namesDeNADding enzyme NudC
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Salmonella
Accessions
- Primary accessionA0A3V2G391
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length257
- Mass (Da)29,607
- Last updated2019-05-08 v1
- MD5 ChecksumDEA4CB3D9ED03BC3FC1A9D566691D543
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AAHCWL010000033 EMBL· GenBank· DDBJ | EBU6917470.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAHFAS010000055 EMBL· GenBank· DDBJ | EBV3763838.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAHGTQ010000048 EMBL· GenBank· DDBJ | EBV9203391.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAHIGD010000028 EMBL· GenBank· DDBJ | EBW4106976.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAHIXO010000026 EMBL· GenBank· DDBJ | EBW6734716.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAHKXZ010000032 EMBL· GenBank· DDBJ | EBX3357689.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAHOXC010000035 EMBL· GenBank· DDBJ | EBY7387599.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAHPAD010000026 EMBL· GenBank· DDBJ | EBY7629244.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAHWIJ010000027 EMBL· GenBank· DDBJ | ECB0525998.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAKLND010000051 EMBL· GenBank· DDBJ | ECT0412963.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAKPQX010000023 EMBL· GenBank· DDBJ | ECU3485579.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AALIQJ010000054 EMBL· GenBank· DDBJ | EDA0177589.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AALLSV010000028 EMBL· GenBank· DDBJ | EDA9404214.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AALLTD010000029 EMBL· GenBank· DDBJ | EDA9439406.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAMGJL010000017 EMBL· GenBank· DDBJ | EDH0980933.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAMIHV010000035 EMBL· GenBank· DDBJ | EDH6431380.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DAAMJL010000017 EMBL· GenBank· DDBJ | HAC6918218.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DAARLP010000016 EMBL· GenBank· DDBJ | HAE2915332.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DAARUC010000054 EMBL· GenBank· DDBJ | HAE3942402.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DAARUZ010000052 EMBL· GenBank· DDBJ | HAE4051278.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DAASLG010000020 EMBL· GenBank· DDBJ | HAE6002753.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DAASLQ010000045 EMBL· GenBank· DDBJ | HAE6032858.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DAASRW010000019 EMBL· GenBank· DDBJ | HAE6748816.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DAATPN010000020 EMBL· GenBank· DDBJ | HAE9563751.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DAAUAM010000072 EMBL· GenBank· DDBJ | HAF0865039.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
RSGD01000032 EMBL· GenBank· DDBJ | MID47794.1 EMBL· GenBank· DDBJ | Genomic DNA |