ID A0A410UKC9_9GAMM Unreviewed; 319 AA.
AC A0A410UKC9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=NAD(+) diphosphatase {ECO:0000256|ARBA:ARBA00012381};
DE EC=3.6.1.22 {ECO:0000256|ARBA:ARBA00012381};
GN ORFNames=EO087_12440 {ECO:0000313|EMBL:QAU24692.1};
OS Dyella sp. M7H15-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dyella.
OX NCBI_TaxID=2501295 {ECO:0000313|EMBL:QAU24692.1, ECO:0000313|Proteomes:UP000288967};
RN [1] {ECO:0000313|EMBL:QAU24692.1, ECO:0000313|Proteomes:UP000288967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M7H15-1 {ECO:0000313|EMBL:QAU24692.1,
RC ECO:0000313|Proteomes:UP000288967};
RA Gao Z.-H., Qiu L.-H., Yang Z.;
RT "Dyella phosphatilytica sp. nov. strain M7H15-1T., a phosphate solubilizing
RT bacterium isolated from forest soil and analysis of the complete genome
RT sequence.";
RL Submitted (JAN-2019) 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; CP035300; QAU24692.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A410UKC9; -.
DR KEGG; dye:EO087_12440; -.
DR OrthoDB; 9791656at2; -.
DR Proteomes; UP000288967; 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; 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:QAU24692.1};
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:UP000288967}.
FT DOMAIN 171..294
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 319 AA; 35406 MW; 0F9DC1030628EC3D CRC64;
MAATNLNTFA GLSLILDRVS EQRDISEWVT AKADSPDARY LLLDPAGDAY LHRHDENLRW
LDARERAHLL PDASWSLLGI AEGQPHFMLV LDERHDHAAL ESALNARRMG LREAGLRLPA
YEAGLFAYAK GLSHWQREAR FCSRCGSPVR LVSSGHRAQC THPACGRLHF PRTDTAIIVL
VEYEGACLLG RQAGWPPGRY STLAGFIEPG EALEDAVRRE VAEESGVIVG DVHYHSSQPW
PLPASLMVGF IAHAVSSAIR LRDGELEDAR WYTPRQIVEG LADGTLGTPS RLSVSYQLIS
HWLRERAGLD LDSLVERTH
//
