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Database: UniProt
Entry: A0A073AVG6_9PSEU
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ID   A0A073AVG6_9PSEU        Unreviewed;       302 AA.
AC   A0A073AVG6;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=NAD(+) diphosphatase {ECO:0000256|ARBA:ARBA00012381};
DE            EC=3.6.1.22 {ECO:0000256|ARBA:ARBA00012381};
GN   ORFNames=GU90_16330 {ECO:0000313|EMBL:KEI43331.1};
OS   Saccharopolyspora rectivirgula.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharopolyspora.
OX   NCBI_TaxID=28042 {ECO:0000313|EMBL:KEI43331.1, ECO:0000313|Proteomes:UP000031419};
RN   [1] {ECO:0000313|EMBL:KEI43331.1, ECO:0000313|Proteomes:UP000031419}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43113 {ECO:0000313|EMBL:KEI43331.1,
RC   ECO:0000313|Proteomes:UP000031419};
RA   Barrera C., Millon L., Rognon B., Zaugg C., Monod M.;
RT   "Saccharopolyspora rectivirgula DSM-43113 Genome sequencing.";
RL   Submitted (JUN-2014) 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:KEI43331.1}.
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DR   EMBL; JNVU01000039; KEI43331.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A073AVG6; -.
DR   STRING; 28042.GU90_16330; -.
DR   eggNOG; COG2816; Bacteria.
DR   OrthoDB; 9791656at2; -.
DR   Proteomes; UP000031419; 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; 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};
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:UP000031419}.
FT   DOMAIN          163..290
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS51462"
SQ   SEQUENCE   302 AA;  32907 MW;  EF1C1C77C22CC223 CRC64;
     MTSELNAQLE FQLDAVPLLS RSTVDRKEVW RDGPDGGAEL WAHGKLVLVD AKGRAPLDGG
     RLVCQRAVDY GDQPPPNAVL LGVQNGTGYW ALRVERGSSD QWRDLRSAGA VLDDTAAGLL
     TTAVGLLNWH DHARYCAVCG AATMQVRAGW ARRCTGCERE EYPRTDPAII CLVHDGDDHV
     LLARQPSWPQ GRYSVLAGFV EVGESLEACV QREVAEEVGV QVDNVRYLGS QPWPFPRSLM
     LGFAATADRS TPLRPADGEI AEARWVHRST VLAALETGEA DGLRLPPSVS IAYRMLRGWA
     TA
//
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