ID A0A0Q8QTR8_9SPHN Unreviewed; 297 AA.
AC A0A0Q8QTR8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=NAD(+) diphosphatase {ECO:0000256|ARBA:ARBA00012381};
DE EC=3.6.1.22 {ECO:0000256|ARBA:ARBA00012381};
GN ORFNames=ASE00_01130 {ECO:0000313|EMBL:KRB85433.1};
OS Sphingomonas sp. Root710.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736594 {ECO:0000313|EMBL:KRB85433.1, ECO:0000313|Proteomes:UP000051854};
RN [1] {ECO:0000313|EMBL:KRB85433.1, ECO:0000313|Proteomes:UP000051854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root710 {ECO:0000313|EMBL:KRB85433.1,
RC ECO:0000313|Proteomes:UP000051854};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB85433.1, ECO:0000313|Proteomes:UP000051854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root710 {ECO:0000313|EMBL:KRB85433.1,
RC ECO:0000313|Proteomes:UP000051854};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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}.
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:KRB85433.1}.
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DR EMBL; LMIB01000001; KRB85433.1; -; Genomic_DNA.
DR RefSeq; WP_056377068.1; NZ_LMIB01000001.1.
DR AlphaFoldDB; A0A0Q8QTR8; -.
DR STRING; 1736594.ASE00_01130; -.
DR OrthoDB; 9791656at2; -.
DR Proteomes; UP000051854; 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; 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; 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:UP000051854}.
FT DOMAIN 159..282
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 297 AA; 32657 MW; DD72E0BDDF5DD5F0 CRC64;
MADIPTPGFT GSPLVRIDIE RDNRAYFDQQ LGSLSARLLR LDGLTPQVTD DGRLSWGSLA
EADPEADLAL LGLLDGKPRF VSLARVDEDP AQRNAAMNTA LTMLEREEAA TYAAARCLVD
WHSRHAYCAR CGQPSRVFRS GWARQCARET GGCGTEHFPR TDPVVIMLAE YEGRVLVGRQ
HRWPKGRYSA LAGFIEVGES IEEAVARELH EEAGVVVSDV RYVASQPWPF PSQLMIACIA
RAESSEISLD ANELEHALWA TRDDIRAALE ASDDAPFLAP PPYAIAHTLL STWLSEG
//
