NUDL_SHIB3
ID NUDL_SHIB3 Reviewed; 192 AA.
AC B2U449;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Uncharacterized Nudix hydrolase NudL {ECO:0000255|HAMAP-Rule:MF_01592};
DE EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_01592};
GN Name=nudL {ECO:0000255|HAMAP-Rule:MF_01592};
GN OrderedLocusNames=SbBS512_E2074;
OS Shigella boydii serotype 18 (strain CDC 3083-94 / BS512).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=344609;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 3083-94 / BS512;
RA Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R.,
RA Jiang L., Ravel J., Sebastian Y.;
RT "Complete sequence of Shigella boydii serotype 18 strain BS512.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probably mediates the hydrolysis of some nucleoside
CC diphosphate derivatives. {ECO:0000255|HAMAP-Rule:MF_01592}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01592};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01592};
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. PCD1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01592}.
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DR EMBL; CP001063; ACD07237.1; -; Genomic_DNA.
DR RefSeq; WP_000456725.1; NC_010658.1.
DR AlphaFoldDB; B2U449; -.
DR SMR; B2U449; -.
DR STRING; 344609.SbBS512_E2074; -.
DR EnsemblBacteria; ACD07237; ACD07237; SbBS512_E2074.
DR GeneID; 66674298; -.
DR KEGG; sbc:SbBS512_E2074; -.
DR HOGENOM; CLU_040940_5_2_6; -.
DR OMA; YYIWGAT; -.
DR Proteomes; UP000001030; Chromosome.
DR GO; GO:0010945; F:CoA pyrophosphatase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009132; P:nucleoside diphosphate metabolic process; IEA:InterPro.
DR CDD; cd03426; CoAse; 1.
DR HAMAP; MF_01592; Nudix_NudL; 1.
DR InterPro; IPR045121; CoAse.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR000059; NUDIX_hydrolase_NudL_CS.
DR InterPro; IPR023735; Nudix_NudL.
DR PANTHER; PTHR12992; PTHR12992; 1.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS01293; NUDIX_COA; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Manganese; Metal-binding.
FT CHAIN 1..192
FT /note="Uncharacterized Nudix hydrolase NudL"
FT /id="PRO_1000147828"
FT DOMAIN 29..160
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01592"
FT MOTIF 67..89
FT /note="Nudix box"
FT BINDING 83
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01592"
FT BINDING 87
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01592"
SQ SEQUENCE 192 AA; 21464 MW; 54CAFB50BF52F5A2 CRC64;
MEYRSLTLDD FLSRFQLLRP QINRETLNHR QAAVLIPIVR RPQPGLLLTQ RSIHLRKHAG
QVAFPGGAVD DTDASVIAAA LREAEEEVAI PPSAVEVIGV LPPVDSVTGY QVTPVVGIIP
PDLPYRASED EVSAVFEMPL AQALHLGRYH PLDIYRRGDS HRVWLSWYEQ YFVWGMTAGI
IRELALQIGV KP
