NUDL_ESCF3
ID NUDL_ESCF3 Reviewed; 192 AA.
AC B7LPN4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=EFER_1263;
OS Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS 14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585054;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 / JCM
RC 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(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; CU928158; CAQ88787.1; -; Genomic_DNA.
DR RefSeq; WP_000456805.1; NC_011740.1.
DR AlphaFoldDB; B7LPN4; -.
DR SMR; B7LPN4; -.
DR EnsemblBacteria; CAQ88787; CAQ88787; EFER_1263.
DR KEGG; efe:EFER_1263; -.
DR HOGENOM; CLU_040940_5_2_6; -.
DR OMA; YYIWGAT; -.
DR OrthoDB; 1623169at2; -.
DR BioCyc; EFER585054:EFER_RS06395-MON; -.
DR Proteomes; UP000000745; 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_1000147820"
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; 21431 MW; 5C44475A83118397 CRC64;
MEYSSLTLDD FLSRFQLLRP QINRETLNHR QAAVLIPIVR RPQPGLLLTQ RSIHLRKHAG
QVAFPGGAVD DTDTSVIAAA LREAEEEVAI PPSSVEVIGV LPPVDSVTGY QVTPVVGIIP
PDLPYHASED EVSAVFEMPL AQALHLGRYH PLDIYRRGDS HRVWLSWYEH YFVWGMTAGI
IRELALQIGV KP