ID A0A430FKL8_9BIFI Unreviewed; 363 AA.
AC A0A430FKL8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=NAD(+) diphosphatase {ECO:0000256|ARBA:ARBA00012381};
DE EC=3.6.1.22 {ECO:0000256|ARBA:ARBA00012381};
GN ORFNames=D2E25_0766 {ECO:0000313|EMBL:RSX53443.1};
OS Bifidobacterium goeldii.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=2306975 {ECO:0000313|EMBL:RSX53443.1, ECO:0000313|Proteomes:UP000287533};
RN [1] {ECO:0000313|EMBL:RSX53443.1, ECO:0000313|Proteomes:UP000287533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2034B {ECO:0000313|EMBL:RSX53443.1,
RC ECO:0000313|Proteomes:UP000287533};
RA Lugli G.A., Duranti S., Milani C.;
RT "Characterization of the phylogenetic diversity of five novel species
RT belonging to the genus Bifidobacterium.";
RL Submitted (SEP-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:RSX53443.1}.
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DR EMBL; QXGL01000002; RSX53443.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A430FKL8; -.
DR Proteomes; UP000287533; 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; 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};
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:UP000287533}.
FT DOMAIN 225..356
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 363 AA; 39730 MW; ED9B5BF02C6E5B12 CRC64;
MFSPLALTQT LPFLPLAQGD IDYQVDRRTD PNLFDDLFAD PATKVILVRD GLLAVPRGQG
GFVDYEAAKM RLSTLPGAYM GVQLAAHPEA VAMFLGSYGG ARSEHVVAID ITRIQGPRSP
MLADSAANSA DGAFDDGGSE EPLAHHSKTD LLVQAVDRFD WVDLRGFTPH ASAREAGQAT
SAVSLSMWHN RQRFCPTCGA PVESVSGGWA QRCTSEADGN RMLFPRIEPA VITAIVDSQD
RLLLQHNAAW RNPKLYSVCA GFVEAGENLE HAVRREAKEE TGIDLGEVRY LGSQPWPFPA
SLMMAFKAQA LSTDVTPDGE ETKIARFVTR DEYMNELITG KLEAPGKATI ARYMIEEWYG
REL
//
