ID Q8G4Z6_BIFLO Unreviewed; 430 AA.
AC Q8G4Z6;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE RecName: Full=NAD(+) diphosphatase {ECO:0000256|ARBA:ARBA00012381};
DE EC=3.6.1.22 {ECO:0000256|ARBA:ARBA00012381};
GN OrderedLocusNames=BL1222 {ECO:0000313|EMBL:AAN25029.1};
OS Bifidobacterium longum (strain NCC 2705).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=206672 {ECO:0000313|EMBL:AAN25029.1, ECO:0000313|Proteomes:UP000000439};
RN [1] {ECO:0000313|EMBL:AAN25029.1, ECO:0000313|Proteomes:UP000000439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCC 2705 {ECO:0000313|Proteomes:UP000000439};
RX PubMed=12381787; DOI=10.1073/pnas.212527599;
RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA Zwahlen M.C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT the human gastrointestinal tract.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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; AE014295; AAN25029.1; -; Genomic_DNA.
DR RefSeq; NP_696393.1; NC_004307.2.
DR RefSeq; WP_011068355.1; NC_004307.2.
DR AlphaFoldDB; Q8G4Z6; -.
DR STRING; 206672.BL1222; -.
DR EnsemblBacteria; AAN25029; AAN25029; BL1222.
DR KEGG; blo:BL1222; -.
DR PATRIC; fig|206672.9.peg.939; -.
DR HOGENOM; CLU_037162_0_4_11; -.
DR OrthoDB; 9791656at2; -.
DR PhylomeDB; Q8G4Z6; -.
DR Proteomes; UP000000439; Chromosome.
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:UP000000439}.
FT DOMAIN 292..423
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 430 AA; 45266 MW; C0A3AC460BFBDC9C CRC64;
MTADIHFSPL ALTHALPFLP LAQGDIDYQV DRRSEPGLID ELLAEPTTKV VLTRGGLVAV
PRGQGELVDY ENVKMRLATL PGAYVSAELA RYPEAVAMFL GSYVGARGES VVAVDITRVP
EAGVPGVGGI AGVSGAAGGV LGTQDSGTVD GALGKNGISG GAAAGIRQPG NAKGNGGVAA
AKIAGPLGVP DSAGQGADDA FDDSVGAPVQ PLAPKPTLLQ QAVTRFDWVD LRGFAPHSNA
REAGQATSAI TLSIWHSRQR FCPTCGAAVR PALAGWAQRC TNEADGNRVL FPRVEPAVIT
AIVDGHDRLL LQHNAAWKDS RLYSVSAGFV EAGENLEHAC RREAMEETGI KLGEVRYLGS
QPWPFPASLM MAFKAHAITT DVRVDGEETM TARWVTRDEY TAELIAGRMA APGRATIARY
MIEEWLGREL
//
