ID NUDC_SALHS Reviewed; 257 AA. AC B4TCT5; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 23-SEP-2008, sequence version 1. DT 02-OCT-2024, entry version 76. DE RecName: Full=NAD-capped RNA hydrolase NudC {ECO:0000255|HAMAP-Rule:MF_00297}; DE Short=DeNADding enzyme NudC {ECO:0000255|HAMAP-Rule:MF_00297}; DE EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_00297}; DE AltName: Full=NADH pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00297}; DE EC=3.6.1.22 {ECO:0000255|HAMAP-Rule:MF_00297}; GN Name=nudC {ECO:0000255|HAMAP-Rule:MF_00297}; OrderedLocusNames=SeHA_C4497; OS Salmonella heidelberg (strain SL476). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=454169; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SL476; RX PubMed=21602358; DOI=10.1128/jb.00297-11; RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G., RA Leclerc J.E., Ravel J., Cebula T.A.; RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for RT CRISPR-mediated adaptive sublineage evolution."; RL J. Bacteriol. 193:3556-3568(2011). 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. {ECO:0000255|HAMAP- CC Rule:MF_00297}. 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; Evidence={ECO:0000255|HAMAP-Rule:MF_00297}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60877; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00297}; 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; Evidence={ECO:0000255|HAMAP-Rule:MF_00297}; 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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00297}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00297}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00297}; CC Note=Divalent metal cations. Mg(2+) or Mn(2+). {ECO:0000255|HAMAP- CC Rule:MF_00297}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00297}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00297}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00297}. CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudC subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00297}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001120; ACF66801.1; -; Genomic_DNA. DR RefSeq; WP_000373960.1; NC_011083.1. DR AlphaFoldDB; B4TCT5; -. DR SMR; B4TCT5; -. DR KEGG; seh:SeHA_C4497; -. DR HOGENOM; CLU_037162_0_1_6; -. DR Proteomes; UP000001866; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0000210; F:NAD+ diphosphatase activity; IEA:UniProtKB-UniRule. DR GO; GO:0035529; F:NADH pyrophosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0110153; F:RNA NAD-cap (NMN-forming) hydrolase activity; IEA:RHEA. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0019677; P:NAD catabolic process; IEA:TreeGrafter. DR GO; GO:0006734; P:NADH metabolic process; IEA:TreeGrafter. DR GO; GO:0006742; P:NADP catabolic process; IEA:TreeGrafter. DR CDD; cd03429; NADH_pyrophosphatase; 1. DR Gene3D; 3.90.79.20; -; 1. DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1. DR HAMAP; MF_00297; Nudix_NudC; 1. DR InterPro; IPR050241; NAD-cap_RNA_hydrolase_NudC. DR InterPro; IPR049734; NudC-like_C. DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR022925; RNA_Hydrolase_NudC. DR InterPro; IPR015376; Znr_NADH_PPase. DR PANTHER; PTHR42904:SF6; NAD-CAPPED RNA HYDROLASE NUDT12; 1. DR PANTHER; PTHR42904; NUDIX HYDROLASE, NUDC SUBFAMILY; 1. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF09297; zf-NADH-PPase; 1. DR SUPFAM; SSF55811; Nudix; 2. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 3: Inferred from homology; KW Hydrolase; Magnesium; Manganese; Metal-binding; NAD; Zinc. FT CHAIN 1..257 FT /note="NAD-capped RNA hydrolase NudC" FT /id="PRO_1000115250" FT DOMAIN 125..248 FT /note="Nudix hydrolase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00297" FT MOTIF 159..180 FT /note="Nudix box" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00297" FT BINDING 69 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00297" FT BINDING 98 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00297" FT BINDING 101 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00297" FT BINDING 111 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00297" FT BINDING 116 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00297" FT BINDING 119 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00297" FT BINDING 124 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00297" FT BINDING 158 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00297" FT BINDING 174 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00297" FT BINDING 174 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="3" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00297" FT BINDING 178 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00297" FT BINDING 178 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="3" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00297" FT BINDING 192..199 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00297" FT BINDING 219 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00297" FT BINDING 219 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="3" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00297" FT BINDING 241 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00297" SQ SEQUENCE 257 AA; 29635 MW; D8F0B689D0F4555C CRC64; MDRIIEKLES GWWIVSHEQK LWLPYGELPH GLAANFDLVG QRALRIGEWQ GEPVWLVLQH RRHDMGSVRQ VIDQDAGLFQ LAGRGVQLAE FYRSHKFCGY CGHPMHPSKT EWAMLCSHCR ERYYPQIAPC IIVAIRREDS ILLARHVRHR NGVHTVLAGF VEVGETLEQA VAREVMEESG IKVKNLRYVT SQPWPFPQSL MTAFMAEYDS GEIVIDPKEL LEANWYRYDD LPLLPPPGTV ARRLIEDTVA MCRAEYD //