ID N2ADY2_9FIRM Unreviewed; 293 AA.
AC N2ADY2;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=NAD(+) diphosphatase {ECO:0000256|ARBA:ARBA00012381};
DE EC=3.6.1.22 {ECO:0000256|ARBA:ARBA00012381};
GN ORFNames=C823_03307 {ECO:0000313|EMBL:EMZ24350.1};
OS Eubacterium plexicaudatum ASF492.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=1235802 {ECO:0000313|EMBL:EMZ24350.1, ECO:0000313|Proteomes:UP000012589};
RN [1] {ECO:0000313|EMBL:EMZ24350.1, ECO:0000313|Proteomes:UP000012589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASF492 {ECO:0000313|EMBL:EMZ24350.1,
RC ECO:0000313|Proteomes:UP000012589};
RX PubMed=24723722;
RA Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT "Draft genome sequences of the altered schaedler flora, a defined bacterial
RT community from gnotobiotic mice.";
RL Genome Announc. 2:e00287-e00214(2014).
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:EMZ24350.1}.
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DR EMBL; AQFT01000099; EMZ24350.1; -; Genomic_DNA.
DR RefSeq; WP_004064835.1; NZ_AQFT02000001.1.
DR AlphaFoldDB; N2ADY2; -.
DR STRING; 1235802.C823_03307; -.
DR GeneID; 78437124; -.
DR PATRIC; fig|1235802.3.peg.3495; -.
DR eggNOG; COG2816; Bacteria.
DR HOGENOM; CLU_037162_0_1_9; -.
DR OrthoDB; 9787476at2; -.
DR Proteomes; UP000012589; 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 CDD; cd03429; NADH_pyrophosphatase; 1.
DR Gene3D; 3.90.79.20; -; 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
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; 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};
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:UP000012589}.
FT DOMAIN 162..287
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 293 AA; 34012 MW; 3B25F2FB887547FB CRC64;
MIQDIEPKRL CNQYQLPKQN RNDYIAVFSG NQILIKETNG RLELPKRADM EAAGCALHAD
TYLFCIDDDR YFLCSEDAEE WKTGNKVDIS NDRAAAADFR RISMRQFREE ADHELCFAVY
TAYHLYQWYK NNRFCGCCGS RTVPDKKERM LFCAKCGNQI YPSIAPAVIA AVTNGDSILL
TKYANREYKR YALIAGFTEI GETAEDTVRR EVMEETGIRV KNIRYYKSQP WGIDGNLLLG
YFAELDGSDR ISIDENELSC AEWVRRDQLK DMDDSFSLTR EMMRVFYEKY DSV
//