GenomeNet

Database: UniProt
Entry: A0A1F4XIX1_9BACT
LinkDB: A0A1F4XIX1_9BACT
Original site: A0A1F4XIX1_9BACT 
ID   A0A1F4XIX1_9BACT        Unreviewed;       176 AA.
AC   A0A1F4XIX1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Nudix hydrolase domain-containing protein {ECO:0000259|PROSITE:PS51462};
GN   ORFNames=A2V81_05210 {ECO:0000313|EMBL:OGC81637.1};
OS   Candidatus Abawacabacteria bacterium RBG_16_42_10.
OC   Bacteria; Candidatus Abawacabacteria.
OX   NCBI_TaxID=1817814 {ECO:0000313|EMBL:OGC81637.1, ECO:0000313|Proteomes:UP000177614};
RN   [1] {ECO:0000313|EMBL:OGC81637.1, ECO:0000313|Proteomes:UP000177614}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGC81637.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; MEWR01000023; OGC81637.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F4XIX1; -.
DR   STRING; 1817814.A2V81_05210; -.
DR   Proteomes; UP000177614; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
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.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          5..149
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS51462"
SQ   SEQUENCE   176 AA;  20133 MW;  2142479B136D734D CRC64;
     MTNPHLHEVV ITAIIVKDDK YLITRRVKTK KRFPGMWTVP GGKLEVDDYK KLPKDTKEYW
     YNVLEKTLRR EVSEEVGIDI DNIEYVTSLA TVHADGAPSL VISCMADYAS GEITLQPEET
     DEFAWVDIEE AKKYDLIDGI LDELVVADNK RKGIRVKWQK VVQTEVTIPQ DAKVAR
//
DBGET integrated database retrieval system