ID A0A1H7H6X1_9ACTN Unreviewed; 324 AA.
AC A0A1H7H6X1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=NAD(+) diphosphatase {ECO:0000256|ARBA:ARBA00012381};
DE EC=3.6.1.22 {ECO:0000256|ARBA:ARBA00012381};
GN ORFNames=SAMN05660976_00604 {ECO:0000313|EMBL:SEK46173.1};
OS Nonomuraea pusilla.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=46177 {ECO:0000313|EMBL:SEK46173.1, ECO:0000313|Proteomes:UP000198953};
RN [1] {ECO:0000313|EMBL:SEK46173.1, ECO:0000313|Proteomes:UP000198953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43357 {ECO:0000313|EMBL:SEK46173.1,
RC ECO:0000313|Proteomes:UP000198953};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOBF01000001; SEK46173.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7H6X1; -.
DR STRING; 46177.SAMN05660976_00604; -.
DR OrthoDB; 9791656at2; -.
DR Proteomes; UP000198953; 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:UP000198953}.
FT DOMAIN 183..307
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 324 AA; 34899 MW; 0D60396AF4B6F68B CRC64;
METSAEEQLI GPLLLARGTI DRSSALRADE QWLKRAWNDP STRVLVIDNG HTLVRRNGDG
VEAVLLGSAD APEGERFLLG LEQGVAYFAV AAPLPGVPGG DLNGRVTVPI SLSDTPEGEP
VAAGLRQVGG LLGDRDAGLL VHAVALEAWH TTHGHCPRCG ARTEVRAGGH IRVCPDDGSQ
HFPRVDPAVI MLVRDADDRC LLARGPHWPE GRLSILAGFV EPGESLEHAV VREVAEEVGV
TVVNPRYLGS QPWPFPRSLM LGFFADATTT ALTPDAEEIA EARWYSREEL AAALESGALR
LPPPVSIARR LIETWYGDHL TGDW
//
