ID A0A2W1ZPJ8_9MICO Unreviewed; 311 AA.
AC A0A2W1ZPJ8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, 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 ORFNames=DEJ23_08410 {ECO:0000313|EMBL:PZF56968.1};
OS Curtobacterium sp. MCSS17_008.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=2175647 {ECO:0000313|EMBL:PZF56968.1, ECO:0000313|Proteomes:UP000248620};
RN [1] {ECO:0000313|EMBL:PZF56968.1, ECO:0000313|Proteomes:UP000248620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCSS17_008 {ECO:0000313|EMBL:PZF56968.1,
RC ECO:0000313|Proteomes:UP000248620};
RA Chase A.B., Gomez-Lunar Z., Lopez A.E., Li J., Allison S.D., Martiny A.C.,
RA Martiny J.B.H.;
RT "Emergence of Soil Bacterial Ecotypes Along a Climate Gradient.";
RL Submitted (JUN-2018) 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:PZF56968.1}.
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DR EMBL; QKSM01000006; PZF56968.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W1ZPJ8; -.
DR OrthoDB; 9791656at2; -.
DR Proteomes; UP000248620; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 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 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:UP000248620}.
FT DOMAIN 169..301
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 311 AA; 33833 MW; B1D4C87AE487D84B CRC64;
MTVEFAARLP LSRNELDRDA EFRTTPDLDR VLRADPSTRW LPVRGAELLR EADGALRFVG
ADAVPEDAVT LYLGRAVSDA PDAPAGTRFV AALLDASAAA AIESDDDAWV SLRMFGTELS
ARDQGLAVEA VAMANWHAVH GFSPRTGSPS AVVSGGWVRR DPEGHDLFPR TDAAIIVGVT
DAEDRILLGS NAAWDADRYS LLAGFVEPGE SLEDAVRREV WEESGVRVEE PEYLGSQPWP
FPASLMVGFR ARAVDGDPST VRPDGVEILD VRWFSRDEVR ERAGDTLLLP GRTSIARAII
EEWYGGPLDL P
//
