ID U2KDK5_9FIRM Unreviewed; 293 AA.
AC U2KDK5;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Hydrolase, NUDIX family {ECO:0000313|EMBL:ERJ96591.1};
DE Flags: Fragment;
GN ORFNames=RUMCAL_01030 {ECO:0000313|EMBL:ERJ96591.1};
OS Ruminococcus callidus ATCC 27760.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=411473 {ECO:0000313|EMBL:ERJ96591.1, ECO:0000313|Proteomes:UP000016662};
RN [1] {ECO:0000313|EMBL:ERJ96591.1, ECO:0000313|Proteomes:UP000016662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27760 {ECO:0000313|EMBL:ERJ96591.1,
RC ECO:0000313|Proteomes:UP000016662};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (JUL-2013) 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:ERJ96591.1}.
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DR EMBL; AWVF01000115; ERJ96591.1; -; Genomic_DNA.
DR AlphaFoldDB; U2KDK5; -.
DR STRING; 411473.RUMCAL_01030; -.
DR eggNOG; COG2816; Bacteria.
DR HOGENOM; CLU_037162_0_1_9; -.
DR OrthoDB; 9787476at2; -.
DR Proteomes; UP000016662; 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 Gene3D; 3.90.79.20; -; 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
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 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:ERJ96591.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 143..267
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT NON_TER 293
FT /evidence="ECO:0000313|EMBL:ERJ96591.1"
SQ SEQUENCE 293 AA; 33804 MW; 572EF5F5376DF375 CRC64;
MIQDIFPHKL ENQYRPEAQP EQDSYVLCYR GAEVLLKDGE MLPTVSEVFA EHYRYLFQID
NRSYFLPETP VSENDVMQYE KIRRIRGTQA IPQFQRYAIM TGKHLADWYK STRYCGSCGG
VLHHSAEQRA MVCDHCHKSI YPKIMPAVIV GVISGDSLLL TKYRTGFPYF ALVAGFTEIG
ETLEETVERE VMEETGLHVR NIRYYKSQPW GIANDILAGF YCEVDGDPTI QMDTSELKYA
QWVKRENIIL QPDDASLTNE MMQKFRDGEI RNINHVNTFW AISHKDCAAD ASS
//