ID A0A1C2JB43_ACITH Unreviewed; 149 AA.
AC A0A1C2JB43;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Phosphatase NudJ {ECO:0000256|ARBA:ARBA00015552, ECO:0000256|RuleBase:RU364043};
DE EC=3.6.1.- {ECO:0000256|RuleBase:RU364043};
GN Name=nudJ {ECO:0000256|RuleBase:RU364043};
GN ORFNames=A6P07_01070 {ECO:0000313|EMBL:OCX77045.1};
OS Acidithiobacillus thiooxidans (Thiobacillus thiooxidans).
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=930 {ECO:0000313|EMBL:OCX77045.1, ECO:0000313|Proteomes:UP000094893};
RN [1] {ECO:0000313|EMBL:OCX77045.1, ECO:0000313|Proteomes:UP000094893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A02 {ECO:0000313|EMBL:OCX77045.1,
RC ECO:0000313|Proteomes:UP000094893};
RA Zhang X., Feng X., Tao J., Ma L., Xiao Y., Liang Y., Liu X., Yin H.;
RT "Comparative genomics of the extreme acidophile Acidithiobacillus
RT thiooxidans reveals intraspecific divergence and niche adaptation.";
RL Int. J. Mol. Sci. 0:0-0(2016).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU364043};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245,
CC ECO:0000256|RuleBase:RU364043}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudJ subfamily.
CC {ECO:0000256|ARBA:ARBA00007608, ECO:0000256|RuleBase:RU364043}.
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:OCX77045.1}.
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; LWSA01000011; OCX77045.1; -; Genomic_DNA.
DR RefSeq; WP_024894113.1; NZ_LZYI01000078.1.
DR AlphaFoldDB; A0A1C2JB43; -.
DR STRING; 930.GCA_002079865_01282; -.
DR GeneID; 60695224; -.
DR eggNOG; COG1051; Bacteria.
DR Proteomes; UP000094893; Unassembled WGS sequence.
DR GO; GO:0017110; F:nucleoside diphosphate phosphatase activity; IEA:InterPro.
DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:InterPro.
DR GO; GO:0004787; F:thiamine diphosphate phosphatase activity; IEA:InterPro.
DR CDD; cd03675; Nudix_Hydrolase_2; 1.
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 InterPro; IPR033713; NudJ.
DR PANTHER; PTHR43222; NUDIX HYDROLASE 23; 1.
DR PANTHER; PTHR43222:SF11; PHOSPHATASE NUDJ; 1.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; Nudix; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU364043, ECO:0000313|EMBL:OCX77045.1};
KW Magnesium {ECO:0000256|RuleBase:RU364043}.
FT DOMAIN 2..131
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 149 AA; 17005 MW; 0673B44D4CF68550 CRC64;
MVWKPHVTVA AIVEQDGRFL LVEEMVEGRR CFNQPAGHWD PGETLLDAVV RETLEETAYA
FEPEYLTGIY HWEHPAKDLT YLRFAFGGKL GDQRPDYTLD TGIIGPVWMT PAEIQAQSGH
LRNVMVQRCM ADYLAGNRYP LEILHSLTD
//
