ID A0A5I2WV80_SALET Unreviewed; 257 AA. AC A0A5I2WV80; DT 11-DEC-2019, integrated into UniProtKB/TrEMBL. DT 11-DEC-2019, sequence version 1. DT 24-JUL-2024, entry version 22. DE RecName: Full=NAD-capped RNA hydrolase NudC {ECO:0000256|HAMAP-Rule:MF_00297}; DE Short=DeNADding enzyme NudC {ECO:0000256|HAMAP-Rule:MF_00297}; DE EC=3.6.1.- {ECO:0000256|HAMAP-Rule:MF_00297}; DE AltName: Full=NADH pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_00297}; DE EC=3.6.1.22 {ECO:0000256|HAMAP-Rule:MF_00297}; GN Name=nudC {ECO:0000256|HAMAP-Rule:MF_00297, GN ECO:0000313|EMBL:ECB8847373.1}; GN ORFNames=APM01_23080 {ECO:0000313|EMBL:ECS2231151.1}, BFV08_22450 GN {ECO:0000313|EMBL:ECT7930094.1}, DM677_23175 GN {ECO:0000313|EMBL:EBU9895995.1}, DN927_22070 GN {ECO:0000313|EMBL:ECT0134668.1}, DOG83_22505 GN {ECO:0000313|EMBL:ECV3391360.1}, DPE57_22935 GN {ECO:0000313|EMBL:EBS3934698.1}, DQK10_24005 GN {ECO:0000313|EMBL:MLO07687.1}, DYS13_21830 GN {ECO:0000313|EMBL:ECV1599414.1}, DYT81_20305 GN {ECO:0000313|EMBL:ECT2693329.1}, E5908_22465 GN {ECO:0000313|EMBL:ECB8847373.1}, EWI81_21765 GN {ECO:0000313|EMBL:ECB3379513.1}, G4R07_004403 GN {ECO:0000313|EMBL:HAE8739171.1}; OS Salmonella enterica subsp. enterica serovar Reading. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=165302 {ECO:0000313|EMBL:EBS3934698.1}; RN [1] {ECO:0000313|EMBL:HAE8739171.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M210 {ECO:0000313|EMBL:HAE8739171.1}; RX PubMed=30286803; DOI=10.1186/s13059-018-1540-z; RA Souvorov A., Agarwala R., Lipman D.J.; RT "SKESA: strategic k-mer extension for scrupulous assemblies."; RL Genome Biol. 19:153-153(2018). RN [2] {ECO:0000313|EMBL:ECT0134668.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FSIS11812504 {ECO:0000313|EMBL:ECT2693329.1}, FSIS31800512 RC {ECO:0000313|EMBL:ECT0134668.1}, FSIS31800555 RC {ECO:0000313|EMBL:ECV3391360.1}, FSIS31800800 RC {ECO:0000313|EMBL:ECV1599414.1}, and FSIS31901531 RC {ECO:0000313|EMBL:ECB3379513.1}; RG GenomeTrakr network: Whole genome sequencing for foodborne pathogen traceback; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:EBS3934698.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=146074 {ECO:0000313|EMBL:EBS3934698.1}, 275776 RC {ECO:0000313|EMBL:MLO07687.1}, and 298956 RC {ECO:0000313|EMBL:EBU9895995.1}; RA Ashton P.M., Dallman T., Nair S., De Pinna E., Peters T., Grant K.; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:ECT7930094.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PNUSAS003387 {ECO:0000313|EMBL:ECT7930094.1}; RG PulseNet: The National Subtyping Network for Foodborne Disease Surveillance; RA Tarr C.L., Trees E., Katz L.S., Carleton-Romer H.A., Stroika S., RA Kucerova Z., Roache K.F., Sabol A.L., Besser J., Gerner-Smidt P.; RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:HAE8739171.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M210 {ECO:0000313|EMBL:HAE8739171.1}; RG NCBI Pathogen Detection Project; RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000313|EMBL:ECB8847373.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CVM N55400 {ECO:0000313|EMBL:ECS2231151.1}, and FSIS11919862 RC {ECO:0000313|EMBL:ECB8847373.1}; RG NARMS: The National Antimicrobial Resistance Monitoring System; RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP- CC 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:0000256|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:0000256|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:0000256|ARBA:ARBA00023679}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60877; CC Evidence={ECO:0000256|ARBA:ARBA00023679}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00297}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00297}; CC Note=Divalent metal cations. Mg(2+) or Mn(2+). {ECO:0000256|HAMAP- CC Rule:MF_00297}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00297}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00297}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00297}. CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudC subfamily. CC {ECO:0000256|ARBA:ARBA00009595, ECO:0000256|HAMAP-Rule:MF_00297}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00297}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EBS3934698.1}. 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; AAGVGK010000039; EBS3934698.1; -; Genomic_DNA. DR EMBL; AAHDUY010000030; EBU9895995.1; -; Genomic_DNA. DR EMBL; AAHXHM010000054; ECB3379513.1; -; Genomic_DNA. DR EMBL; AAHYZU010000033; ECB8847373.1; -; Genomic_DNA. DR EMBL; AAKIXE010000028; ECS2231151.1; -; Genomic_DNA. DR EMBL; AAKLKV010000039; ECT0134668.1; -; Genomic_DNA. DR EMBL; AAKMFT010000094; ECT2693329.1; -; Genomic_DNA. DR EMBL; AAKNWZ010000014; ECT7930094.1; -; Genomic_DNA. DR EMBL; AAKSPP010000061; ECV1599414.1; -; Genomic_DNA. DR EMBL; AAKSBI010000052; ECV3391360.1; -; Genomic_DNA. DR EMBL; DAATIJ010000017; HAE8739171.1; -; Genomic_DNA. DR EMBL; RVCL01000025; MLO07687.1; -; Genomic_DNA. DR RefSeq; WP_000373956.1; NZ_MZFK01000019.1. DR AlphaFoldDB; A0A5I2WV80; -. DR SMR; A0A5I2WV80; -. DR Proteomes; UP000885381; Unassembled WGS sequence. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0005777; C:peroxisome; 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: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 {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00297}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00297}; KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_00297}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00297}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00297}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00297}. FT DOMAIN 125..248 FT /note="Nudix hydrolase" FT /evidence="ECO:0000259|PROSITE:PS51462" FT MOTIF 159..180 FT /note="Nudix box" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00297" FT BINDING 69 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00297" FT BINDING 98 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00297" FT BINDING 101 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00297" FT BINDING 111 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00297" FT BINDING 116 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00297" FT BINDING 119 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00297" FT BINDING 124 FT /ligand="substrate" FT /evidence="ECO:0000256|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:0000256|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:0000256|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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00297" FT BINDING 192..199 FT /ligand="substrate" FT /evidence="ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00297" FT BINDING 241 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00297" SQ SEQUENCE 257 AA; 29593 MW; 05C99052BD43DD3D CRC64; MDRIIEKLES GWWIVSHEQK LWLPYGELPH GLAANFDLVG QRALRIGEWQ GEPVWLVLQH RRHDMGSVRQ VIDQDAGLFQ LAGRGVQLAE FYRSHKFCGY CGHPMHPSKT EWAMLCSHCR ERYYPQIAPC IIVAIRREDS ILLAQHVRHR NGVHTVLAGF VEVGETLEQA VAREVMEESG IKVKNLRYVT SQPWPFPQSL MTAFMAEYDS GDIVIDPKEL LEANWYRYDD LPLLPPPGTV ARRLIEDTVA MCRAEYD //