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   03-AUG-2022, entry version 108.
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}.
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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   AlphaFoldDB; Q9I767; -.
DR   SMR; Q9I767; -.
DR   STRING; 287.DR97_3022; -.
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   OMA; HHFKVIY; -.
DR   PhylomeDB; Q9I767; -.
DR   BioCyc; PAER208964:G1FZ6-67-MON; -.
DR   BRENDA; 3.1.3.5; 5087.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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   GO; GO:0106411; F:XMP 5'-nucleosidase activity; IEA:UniProtKB-EC.
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