ID A0A4U0YGU5_9GAMM Unreviewed; 280 AA. AC A0A4U0YGU5; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 14-DEC-2022, entry version 14. 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:TKA90308.1}; GN ORFNames=FA869_14390 {ECO:0000313|EMBL:TKA90308.1}; OS Halopseudomonas bauzanensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Halopseudomonas. OX NCBI_TaxID=653930 {ECO:0000313|EMBL:TKA90308.1, ECO:0000313|Proteomes:UP000305198}; RN [1] {ECO:0000313|EMBL:TKA90308.1, ECO:0000313|Proteomes:UP000305198} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SBBB {ECO:0000313|EMBL:TKA90308.1, RC ECO:0000313|Proteomes:UP000305198}; RA Bhattacharya S., Roy C., Mondal N., Sarkar J., Mandal S., Rameez M.J., RA Ghosh W.; RT "Crypto-aerobic microbial life in anoxic (sulfidic) marine sediments."; 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|HAMAP-Rule:MF_00297}; 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:TKA90308.1}. 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; SWAV01000005; TKA90308.1; -; Genomic_DNA. DR AlphaFoldDB; A0A4U0YGU5; -. DR Proteomes; UP000305198; Unassembled WGS sequence. 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 HAMAP; MF_00297; Nudix_NudC; 1. DR InterPro; IPR015375; NADH_PPase-like_N. DR InterPro; IPR020476; Nudix_hydrolase. 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 Pfam; PF00293; NUDIX; 1. DR Pfam; PF09296; NUDIX-like; 1. DR Pfam; PF09297; zf-NADH-PPase; 1. DR PRINTS; PR00502; NUDIXFAMILY. 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 143..267 FT /note="Nudix hydrolase" FT /evidence="ECO:0000259|PROSITE:PS51462" FT MOTIF 177..198 FT /note="Nudix box" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00297" FT BINDING 86 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 129 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00297" FT BINDING 134 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00297" FT BINDING 137 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00297" FT BINDING 142 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00297" FT BINDING 176 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 192 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 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 196 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 196 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 210..217 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00297" FT BINDING 237 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 237 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00297" SQ SEQUENCE 280 AA; 31561 MW; 481D012864C31D31 CRC64; MIPVQRFTRF TASLTTETHA DGWVLIRHEQ SFAMYQGNLL HDPDMARYLG DAEYQMTLGL VDDRPCQLVR VKEQIDLPGL SWHGLRSLLG QVDDSTFRLL GVAQQLDIWH DTHRFCGRCG QPTQVRPDER AMECSGCGNR QYPKLAPCII VLITRGEEVL LARSANFRAG FFSTLAGFIE PGESAEEALR REVMEEVGVT VDHIEYLGSQ NWPFPNSLML GFHASYVDGE IVPQPGEIEE AHWWNIHQLP AIPPQGTISR WLIDCYLARL AGQPQPPVPA //