ID NUDL_SALPK Reviewed; 192 AA.
AC B5BHD1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 64.
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}; OrderedLocusNames=SSPA0978;
OS Salmonella paratyphi A (strain AKU_12601).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=554290;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AKU_12601;
RX PubMed=19159446; DOI=10.1186/1471-2164-10-36;
RA Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hasan R., Bhutta Z.A.,
RA Quail M.A., Norbertczak H., Walker D., Simmonds M., White B., Bason N.,
RA Mungall K., Dougan G., Parkhill J.;
RT "Pseudogene accumulation in the evolutionary histories of Salmonella
RT enterica serovars Paratyphi A and Typhi.";
RL BMC Genomics 10:36-36(2009).
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; FM200053; CAR59129.1; -; Genomic_DNA.
DR RefSeq; WP_000381531.1; NC_011147.1.
DR AlphaFoldDB; B5BHD1; -.
DR SMR; B5BHD1; -.
DR KEGG; sek:SSPA0978; -.
DR HOGENOM; CLU_040940_5_2_6; -.
DR Proteomes; UP000001869; Chromosome.
DR GO; GO:0010945; F:coenzyme A diphosphatase 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 Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 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:SF11; MITOCHONDRIAL COENZYME A DIPHOSPHATASE NUDT8; 1.
DR PANTHER; PTHR12992; NUDIX HYDROLASE; 1.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; Nudix; 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_1000147826"
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; 21413 MW; 428D03827DF15F1D CRC64;
MDTSRLTLDH FLSRFQLLRP QITHETLNQR QAAVLIPVVR RPQPGLLLTQ RAIHLRKHAG
QVAFPGGAVD STDASLIAAA LREAQEEVAI PPQAVEVIGV LPPVDSVTGF QVTPVVGIIP
PNLPWRASED EVSAVFEMPL AQALQLGRYH PLDVYRRGNS HRVWLSWYEH YFVWGMTANI
LRELALQIGV KP
//
