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Database: UniProt
Entry: S9QXA0_9RHOB
LinkDB: S9QXA0_9RHOB
Original site: S9QXA0_9RHOB 
ID   S9QXA0_9RHOB            Unreviewed;       299 AA.
AC   S9QXA0;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=NAD(+) diphosphatase {ECO:0000256|ARBA:ARBA00012381};
DE            EC=3.6.1.22 {ECO:0000256|ARBA:ARBA00012381};
GN   ORFNames=ruthe_02414 {ECO:0000313|EMBL:EPX84202.1};
OS   Rubellimicrobium thermophilum DSM 16684.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Rubellimicrobium.
OX   NCBI_TaxID=1123069 {ECO:0000313|EMBL:EPX84202.1, ECO:0000313|Proteomes:UP000015346};
RN   [1] {ECO:0000313|EMBL:EPX84202.1, ECO:0000313|Proteomes:UP000015346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16684 {ECO:0000313|EMBL:EPX84202.1,
RC   ECO:0000313|Proteomes:UP000015346};
RX   PubMed=24501632; DOI=10.4056/sigs.4247911;
RA   Fiebig A., Riedel T., Gronow S., Petersen J., Klenk H.P., Goker M.;
RT   "Genome sequence of the reddish-pigmented Rubellimicrobium thermophilum
RT   type strain (DSM 16684(T)), a member of the Roseobacter clade.";
RL   Stand. Genomic Sci. 8:480-490(2013).
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}.
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:EPX84202.1}.
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DR   EMBL; AOLV01000028; EPX84202.1; -; Genomic_DNA.
DR   AlphaFoldDB; S9QXA0; -.
DR   STRING; 1123069.ruthe_02414; -.
DR   PATRIC; fig|1123069.3.peg.2391; -.
DR   HOGENOM; CLU_037162_0_4_5; -.
DR   OrthoDB; 9791656at2; -.
DR   Proteomes; UP000015346; Unassembled WGS sequence.
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; 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   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:0000313|EMBL:EPX84202.1};
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:UP000015346}.
FT   DOMAIN          157..283
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS51462"
SQ   SEQUENCE   299 AA;  31594 MW;  37D68B19221BAFE0 CRC64;
     MTFVQTVAFP GIAFGAGGLD RAAHLRRQDG AAAQGPGTLL RFCGGDPLMA EEGLTLWRER
     VPGRPEGAVF LGLEGGRPLW ALEAAAGTPA PAGTVWAGLR GIMSQLPAPE AEAAATARAL
     LGWHANHGFC AACGAPTRMA EAGWRRDCPA CGATHFPRTD PVVIMLVTRG NAVLLARNPL
     WPPGMHSLLA GFMEPGETVE AAVRREVQEE AGVQVGRVGY LASQPWPFPA SLMLGMRAEA
     LTTEIAIDRE EIESASWVSR ERLMAVFMGR DPAIRAPRSG SIAGAILREW LAGRIAPAP
//
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