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Database: UniProt
Entry: A0A1N7M1C0_9RHOB
LinkDB: A0A1N7M1C0_9RHOB
Original site: A0A1N7M1C0_9RHOB 
ID   A0A1N7M1C0_9RHOB        Unreviewed;       324 AA.
AC   A0A1N7M1C0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=NAD(+) diphosphatase {ECO:0000256|ARBA:ARBA00012381};
DE            EC=3.6.1.22 {ECO:0000256|ARBA:ARBA00012381};
GN   ORFNames=SAMN05421774_102335 {ECO:0000313|EMBL:SIS79853.1};
OS   Gemmobacter megaterium.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Gemmobacter.
OX   NCBI_TaxID=1086013 {ECO:0000313|EMBL:SIS79853.1, ECO:0000313|Proteomes:UP000186141};
RN   [1] {ECO:0000313|EMBL:SIS79853.1, ECO:0000313|Proteomes:UP000186141}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26375 {ECO:0000313|EMBL:SIS79853.1,
RC   ECO:0000313|Proteomes:UP000186141};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) 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; FTOT01000002; SIS79853.1; -; Genomic_DNA.
DR   RefSeq; WP_076529534.1; NZ_FTOT01000002.1.
DR   AlphaFoldDB; A0A1N7M1C0; -.
DR   STRING; 1086013.SAMN05421774_102335; -.
DR   OrthoDB; 9791656at2; -.
DR   Proteomes; UP000186141; 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; 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; 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:UP000186141}.
FT   DOMAIN          185..310
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS51462"
SQ   SEQUENCE   324 AA;  34826 MW;  95DA46A544689147 CRC64;
     MRDGETVTFG GLGGLDRAAE LRGDAARQAA LWGEGTARVI VLWRGKPMVA GEARDRLALL
     PAGHPLVAGA RGPRLFLGIA ADGPVFALDL SAWEPVGIDA AAQGGAFFDA TEQRHPAVPA
     DHLFVELRGV MTRLSPLDAE LAATARGLFE WHRSHGFCAR CGHASDMAMA GWQRHCPACN
     APHFPRTDPV VIMLVTHGNR VLLGRSHGWP EGMYSLLAGF IEPGETIEAA VRREVVEETG
     VKVDAVRYLA SQPWPFPASL MLGCAAEAVS DAITLDPAEI EDALWISRED MIEVLGGRHP
     RVKPARRGAI AHFLINAWVA DLLD
//
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