ID A0A1X7BUG5_9RHOB Unreviewed; 321 AA.
AC A0A1X7BUG5;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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:SMC13150.1};
GN ORFNames=ROA7745_02986 {ECO:0000313|EMBL:SMC13150.1};
OS Roseovarius aestuarii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=475083 {ECO:0000313|EMBL:SMC13150.1, ECO:0000313|Proteomes:UP000193224};
RN [1] {ECO:0000313|EMBL:SMC13150.1, ECO:0000313|Proteomes:UP000193224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7745 {ECO:0000313|EMBL:SMC13150.1,
RC ECO:0000313|Proteomes:UP000193224};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) 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; FWXB01000011; SMC13150.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7BUG5; -.
DR OrthoDB; 9791656at2; -.
DR Proteomes; UP000193224; 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; IPR015375; NADH_PPase-like_N.
DR InterPro; IPR049734; NudC-like_C.
DR InterPro; IPR020476; Nudix_hydrolase.
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 PRINTS; PR00502; NUDIXFAMILY.
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:0000256|RuleBase:RU003476};
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:UP000193224}.
FT DOMAIN 182..308
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 321 AA; 35057 MW; CAC050E6F4EE13E5 CRC64;
MVDPETVTFG GSGLDRAAEL RGDDDAIAEA ISTGRAACTL IWRGKPLVAE GTQDRLIRLP
MDHPILAEAT MSLLLGRNET GDLLFAHDIS DWTPAGVDED ALNKFLDTSE QQHPALPGAI
FVELRRIMTR LDARDAELAA TARAVINWHV SHRFCACCGA ESRPVQAGWQ RSCDACGGQH
FPRTDPVVIM LITRGNSVLM GRSPGWPEGM YSLLAGFVEP GETIEAAVRR EVYEEAGIRV
GPVGYLASQP WAFPSSLMIG CRGTALTQDL TIDPSEIEDA RWFAREEILR AFAGLHPTLA
PARQGAIAHF LLRNWLADIN Y
//