NUDL_PHOLL
ID NUDL_PHOLL Reviewed; 187 AA.
AC Q7N3M0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=plu2695;
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01;
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(2003).
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; BX571868; CAE15069.1; -; Genomic_DNA.
DR RefSeq; WP_011146917.1; NC_005126.1.
DR AlphaFoldDB; Q7N3M0; -.
DR SMR; Q7N3M0; -.
DR STRING; 243265.plu2695; -.
DR PRIDE; Q7N3M0; -.
DR EnsemblBacteria; CAE15069; CAE15069; plu2695.
DR GeneID; 24170495; -.
DR KEGG; plu:plu2695; -.
DR eggNOG; COG0494; Bacteria.
DR HOGENOM; CLU_040940_5_2_6; -.
DR OMA; YYIWGAT; -.
DR OrthoDB; 1623169at2; -.
DR BioCyc; PLUM243265:PLU_RS13365-MON; -.
DR Proteomes; UP000002514; 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; Reference proteome.
FT CHAIN 1..187
FT /note="Uncharacterized Nudix hydrolase NudL"
FT /id="PRO_0000315580"
FT DOMAIN 26..157
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01592"
FT MOTIF 64..86
FT /note="Nudix box"
FT BINDING 80
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01592"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01592"
SQ SEQUENCE 187 AA; 20732 MW; EACBE1F8C9FE78B9 CRC64;
MISLSDFVNR FQLQLPPPPK RLSDNNRHAA VLLPIICKPK PTLLLTRRSA TLRSHAGQVA
FPGGVADPKD KSIIATALRE AEEEVNIPHQ KVQVLGQLAP LNSSGGYLVT PIVGLLPPGL
SLHSNPAEVA KIFEVPLSEA LSLSSYHYLD VSRRGQQHRV YFYWYQQHLI WGLTATIIHQ
LAQQVQV
