ID 5NTD_PSEAE Reviewed; 221 AA. AC Q9I767; DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 12-AUG-2020, entry version 103. DE RecName: Full=5'-nucleotidase; DE EC=3.1.3.5; DE AltName: Full=Nucleoside 5'-monophosphate phosphohydrolase; GN OrderedLocusNames=PA0065; OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=208964; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / RC PRS 101 / PAO1; RX PubMed=10984043; DOI=10.1038/35023079; RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic RT pathogen."; RL Nature 406:959-964(2000). RN [2] RP FUNCTION, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=15808744; DOI=10.1016/j.fmrre.2004.12.006; RA Kuznetsova E., Proudfoot M., Sanders S.A., Reinking J., Savchenko A., RA Arrowsmith C.H., Edwards A.M., Yakunin A.F.; RT "Enzyme genomics: application of general enzymatic screens to discover new RT enzymes."; RL FEMS Microbiol. Rev. 29:263-279(2005). CC -!- FUNCTION: Specifically dephosphorylates nucleoside 5'-monophosphates to CC nucleosides and inorganic phosphate. Displays high activity toward 5'- CC UMP and 5'-IMP, significant activity against 5'-XMP and 5'-TMP, and low CC activity against 5'-CMP. {ECO:0000269|PubMed:15808744}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + CC phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:15808744}; CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:15808744}; CC Note=Divalent metal cation. Prefers Mn(2+) over Mg(2+). CC {ECO:0000269|PubMed:15808744}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.39 mM for 5'-UMP {ECO:0000269|PubMed:15808744}; CC Vmax=3.14 umol/min/mg enzyme with 5'-UMP as substrate CC {ECO:0000269|PubMed:15808744}; CC pH dependence: CC Optimum pH is 7.4. {ECO:0000269|PubMed:15808744}; CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE004091; AAG03455.1; -; Genomic_DNA. DR PIR; C83636; C83636. DR RefSeq; NP_248755.1; NC_002516.2. DR RefSeq; WP_003114659.1; NZ_QZGE01000015.1. DR SMR; Q9I767; -. DR PaxDb; Q9I767; -. DR PRIDE; Q9I767; -. DR EnsemblBacteria; AAG03455; AAG03455; PA0065. DR GeneID; 878495; -. DR KEGG; pae:PA0065; -. DR PATRIC; fig|208964.12.peg.68; -. DR PseudoCAP; PA0065; -. DR HOGENOM; CLU_045011_19_4_6; -. DR InParanoid; Q9I767; -. DR KO; K01091; -. DR OMA; IEMGQRA; -. DR PhylomeDB; Q9I767; -. DR BioCyc; PAER208964:G1FZ6-67-MONOMER; -. DR BRENDA; 3.1.3.5; 5087. DR Proteomes; UP000002438; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0008253; F:5'-nucleotidase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0004713; F:protein tyrosine kinase activity; IBA:GO_Central. DR Gene3D; 1.10.150.240; -; 1. DR Gene3D; 3.40.50.1000; -; 1. DR InterPro; IPR036412; HAD-like_sf. DR InterPro; IPR041492; HAD_2. DR InterPro; IPR023214; HAD_sf. DR InterPro; IPR023198; PGP-like_dom2. DR Pfam; PF13419; HAD_2; 1. DR SUPFAM; SSF56784; SSF56784; 1. PE 1: Evidence at protein level; KW Hydrolase; Magnesium; Manganese; Metal-binding; Nucleotide-binding; KW Reference proteome. FT CHAIN 1..221 FT /note="5'-nucleotidase" FT /id="PRO_0000064390" FT ACT_SITE 14 FT /note="Nucleophile" FT /evidence="ECO:0000250" SQ SEQUENCE 221 AA; 24951 MW; 8885AF689CC828B1 CRC64; MRDAALRYPN ILFDLDGTLT DPREGITRSV QFALARLGID EPDLARLEHF IGPPLLQCFM QTYGFDEARA WEAVNHYRER FRVTGLYENR VFDGIPELLE ALVGRGHTLY VATSKPGVFA REIARHFAFD RHFKAIYGSE LDGTRTHKEE LIRHLLDSEG LAAEHCLMIG DRMHDLLGAS RNGVACIGVG YGFGSEDELR AHQPTHYCAD LAALRQVLES H //