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Database: UniProt
Entry: A0A1B2ADX8_9SPHN
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ID   A0A1B2ADX8_9SPHN        Unreviewed;       290 AA.
AC   A0A1B2ADX8;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=NAD(+) diphosphatase {ECO:0000256|ARBA:ARBA00012381};
DE            EC=3.6.1.22 {ECO:0000256|ARBA:ARBA00012381};
GN   Name=nudC {ECO:0000313|EMBL:ANY20343.1};
GN   ORFNames=A6F68_01833 {ECO:0000313|EMBL:ANY20343.1};
OS   Tsuneonella dongtanensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Tsuneonella.
OX   NCBI_TaxID=692370 {ECO:0000313|EMBL:ANY20343.1, ECO:0000313|Proteomes:UP000092932};
RN   [1] {ECO:0000313|EMBL:ANY20343.1, ECO:0000313|Proteomes:UP000092932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 22672 {ECO:0000313|EMBL:ANY20343.1,
RC   ECO:0000313|Proteomes:UP000092932};
RA   Cheng H., Wu Y.-H., Zhou P., Huo Y.-Y., Wang C.-S., Xu X.-W.;
RT   "Complete genome sequence of Altererythrobacter dongtanensis KCTC 22672, a
RT   type strain with esterase isolated from tidal flat.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudC subfamily.
CC       {ECO:0000256|ARBA:ARBA00009595}.
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DR   EMBL; CP016591; ANY20343.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B2ADX8; -.
DR   STRING; 692370.A6F68_01833; -.
DR   KEGG; ado:A6F68_01833; -.
DR   PATRIC; fig|692370.5.peg.1846; -.
DR   Proteomes; UP000092932; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000210; F:NAD+ diphosphatase activity; IEA:UniProtKB-EC.
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   CDD; cd03429; NADH_pyrophosphatase; 1.
DR   Gene3D; 3.90.79.20; -; 1.
DR   Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR   InterPro; IPR015375; NADH_PPase-like_N.
DR   InterPro; IPR049734; NudC-like_C.
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; 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; PF09296; NUDIX-like; 1.
DR   Pfam; PF09297; zf-NADH-PPase; 1.
DR   PRINTS; PR00502; NUDIXFAMILY.
DR   SUPFAM; SSF55811; Nudix; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003476};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092932}.
FT   DOMAIN          151..275
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS51462"
SQ   SEQUENCE   290 AA;  32178 MW;  85BD155F41BDE604 CRC64;
     MIAFSGSPLD RADHLRTDPD ALAGLMDWRA RLLRLDGLLP TFDNTTGALG WGSLAEVPED
     ADLVFLGLLD GKACFAAVPD QGAEGPAYAQ PQVWQAMQVL SPQDLAVYGG ARSLVDWHAR
     HRFCARCGAR TRVAKGGWQR DCPECSAAHF PRTDPVTIML VEYEDKLLLG RQPRFPPRIF
     SALAGFVEPG ETIEEAVARE VFEEAGVRVR EVTYIASQPW PFPSQLMIGC HSVAEDDALT
     IDRTELEEAR WFTRAELIEA RAAGPEGNEN LIFPRSFAIA HHLVTWWLDR
//
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