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 02-MAR-2010, entry version 47. DE RecName: Full=5'-nucleotidase; DE EC=3.1.3.5; DE AltName: Full=Nucleoside 5'-monophosphate phosphohydrolase; GN OrderedLocusNames=PA0065; OS Pseudomonas aeruginosa. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=287; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228; RX MEDLINE=20437337; 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., RA Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an RT opportunistic pathogen."; RL Nature 406:959-964(2000). RN [2] RP FUNCTION, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=15808744; DOI=10.1016/j.femsre.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 RT new enzymes."; RL FEMS Microbiol. Rev. 29:263-279(2005). CC -!- FUNCTION: Specifically dephosphorylates nucleoside 5'- CC monophosphates to nucleosides and inorganic phosphate. Displays CC high activity toward 5'-UMP and 5'-IMP, significant activity CC against 5'-XMP and 5'-TMP, and low activity against 5'-CMP. CC -!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside CC + phosphate. CC -!- COFACTOR: Divalent metal cation. Prefers manganese over magnesium. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.39 mM for 5'-UMP; CC Vmax=3.14 umol/min/mg enzyme with 5'-UMP as substrate; CC pH dependence: CC Optimum pH is 7.4; CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. 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; -. DR SMR; Q9I767; 7-219. DR GeneID; 878495; -. DR GenomeReviews; AE004091_GR; PA0065. DR KEGG; pae:PA0065; -. DR NMPDR; fig|208964.1.peg.65; -. DR PseudoCAP; PA0065; -. DR HOGENOM; HBG742904; -. DR OMA; DIIGANQ; -. DR ProtClustDB; CLSK865566; -. DR BioCyc; PAER208964:PA0065-MONOMER; -. DR BRENDA; 3.1.3.5; 354. DR GO; GO:0008253; F:5'-nucleotidase activity; IEA:EC. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0008967; F:phosphoglycolate phosphatase activity; IEA:InterPro. DR GO; GO:0008152; P:metabolic process; IEA:InterPro. DR InterPro; IPR005834; Dehalogen-like_hydro. DR InterPro; IPR006439; HAD-SF_hydro_IA_v1. DR Pfam; PF00702; Hydrolase; 1. DR TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1. PE 1: Evidence at protein level; KW Complete proteome; Hydrolase; Magnesium; Manganese; Metal-binding; KW Nucleotide-binding. FT CHAIN 1 221 5'-nucleotidase. FT /FTId=PRO_0000064390. FT ACT_SITE 14 14 Nucleophile (By similarity). 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 //