NUDL_CROS8
ID NUDL_CROS8 Reviewed; 192 AA.
AC A7MKE8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=ESA_01440;
OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=290339;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-894;
RX PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA McClelland M., Forsythe S.J.;
RT "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT hybridization analysis with other Cronobacter species.";
RL PLoS ONE 5:E9556-E9556(2010).
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; CP000783; ABU76698.1; -; Genomic_DNA.
DR RefSeq; WP_004387271.1; NC_009778.1.
DR AlphaFoldDB; A7MKE8; -.
DR SMR; A7MKE8; -.
DR EnsemblBacteria; ABU76698; ABU76698; ESA_01440.
DR KEGG; esa:ESA_01440; -.
DR HOGENOM; CLU_040940_5_2_6; -.
DR OMA; YYIWGAT; -.
DR OrthoDB; 1623169at2; -.
DR Proteomes; UP000000260; 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_0000315569"
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; 21273 MW; DC9596B2E1D912B1 CRC64;
MENSPLTLDR FLSRFQLLRP QMSRSSLNQR QAAVLVPVVR RPEPGLLLTK RAATLRKHAG
QVAFPGGAVD DTDASLIAAA LREAQEEVAI PPEAVDVIGV LPPVDSVTGF QVTPVVGIIP
PDLPYHASED EVAAVFEMPL AEALRLGRYH PLDIHRRGNH HRVWLSWYQH YFVWGMTAGI
IRELALQIGE KP
