ID C7BH10_PHOAA Unreviewed; 187 AA.
AC C7BH10;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Nudix hydrolase domain-containing protein {ECO:0000259|PROSITE:PS51462};
GN Name=nudL {ECO:0000313|EMBL:CAQ83932.1};
GN OrderedLocusNames=PAU_01840 {ECO:0000313|EMBL:CAQ83932.1};
OS Photorhabdus asymbiotica subsp. asymbiotica (strain ATCC 43949 / 3105-77)
OS (Xenorhabdus luminescens (strain 2)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=553480 {ECO:0000313|EMBL:CAQ83932.1, ECO:0000313|Proteomes:UP000002747};
RN [1] {ECO:0000313|EMBL:CAQ83932.1, ECO:0000313|Proteomes:UP000002747}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43949 / 3105-77 {ECO:0000313|Proteomes:UP000002747};
RX PubMed=19583835; DOI=10.1186/1471-2164-10-302;
RA Wilkinson P., Waterfield N.R., Crossman L., Corton C.,
RA Sanchez-Contreras M., Vlisidou I., Barron A., Bignell A., Clark L.,
RA Ormond D., Mayho M., Bason N., Smith F., Simmonds M., Churcher C.,
RA Harris D., Thompson N.R., Quail M., Parkhill J., ffrench-Constant R.H.;
RT "Comparative genomics of the emerging human pathogen Photorhabdus
RT asymbiotica with the insect pathogen Photorhabdus luminescens.";
RL BMC Genomics 10:302-302(2009).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. PCD1 subfamily.
CC {ECO:0000256|ARBA:ARBA00006506}.
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DR EMBL; FM162591; CAQ83932.1; -; Genomic_DNA.
DR AlphaFoldDB; C7BH10; -.
DR STRING; 291112.PAU_01840; -.
DR KEGG; pay:PAU_01840; -.
DR eggNOG; COG0494; Bacteria.
DR Proteomes; UP000002747; Chromosome.
DR GO; GO:0010945; F:coenzyme A diphosphatase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
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 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 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 {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAQ83932.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 26..157
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 187 AA; 20879 MW; B7B25D89BB5E8AF7 CRC64;
MILLSDFINR FQLQLPSHPK RPSNNCRHAA VLLPIICKPK PTLLLTQRST TLRSHAGQVA
FPGGAADPED KSIIATALRE AEEEVNIPHH KVQVLGQLVP LDSISGYLVT PVVGLLPPEL
SFHSNPTEVS SIFEVPLSKA LSLSSYYYLD VNRHGQQHRT YFYWYQGKLI WGLTAAIIHQ
LAQQVQI
//
