ID A0A0J8D924_CLOCY Unreviewed; 280 AA.
AC A0A0J8D924;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, 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 Name=nudC {ECO:0000313|EMBL:KMT22520.1};
GN ORFNames=CLCY_10c00650 {ECO:0000313|EMBL:KMT22520.1};
OS Clostridium cylindrosporum DSM 605.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121307 {ECO:0000313|EMBL:KMT22520.1, ECO:0000313|Proteomes:UP000036756};
RN [1] {ECO:0000313|EMBL:KMT22520.1, ECO:0000313|Proteomes:UP000036756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 605 {ECO:0000313|EMBL:KMT22520.1,
RC ECO:0000313|Proteomes:UP000036756};
RA Poehlein A., Schiel-Bengelsdorf B., Bengelsdorf F., Daniel R., Duerre P.;
RT "Draft genome sequence of the purine-degrading Clostridium cylindrosporum
RT HC-1 (DSM 605).";
RL Submitted (JUN-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:KMT22520.1}.
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DR EMBL; LFVU01000007; KMT22520.1; -; Genomic_DNA.
DR RefSeq; WP_048569934.1; NZ_LFVU01000007.1.
DR AlphaFoldDB; A0A0J8D924; -.
DR STRING; 1121307.CLCY_10c00650; -.
DR PATRIC; fig|1121307.3.peg.69; -.
DR OrthoDB; 9787476at2; -.
DR Proteomes; UP000036756; 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 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; 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, ECO:0000313|EMBL:KMT22520.1};
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:UP000036756}.
FT DOMAIN 150..275
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 280 AA; 32595 MW; 612010F7CC0E6C98 CRC64;
MIQDIEPRIF DNNFKDKVAE PQDLFLSYEG DTVLIREDKD KLWYPSFSDF QVEYPGLIDN
AQFLFSIDNI NYYLVNEKGL DSINGWSYAS INRFRTEPKY WRSFVGVVGW QLNRWYDSHR
FCSKCSKSMK HSKKQRMLYC ESCGFKVYPT ISPCVIVAVY NGNRLLLTKY AGRAYNNYAL
IAGFAEIGES LEQTVYREVK EEVGLKVKNL KFYKSQPWPF SDTLLVGFFA ELDGDDEITI
DEDELSLGVW VDREDIPSPN LNISLTSEMM EAFRTESVEL
//
