{PDOC00627}
{PS00785; 5_NUCLEOTIDASE_1}
{PS00786; 5_NUCLEOTIDASE_2}
{BEGIN}
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* 5'-nucleotidase signatures *
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5'-nucleotidases (EC 3.1.3.5) [1]  are enzymes that catalyze the hydrolysis of
phosphate  esterified at carbon 5' of  the ribose  and deoxyribose portions of
nucleotide molecules.  5'-nucleotidase  is a ubiquitous enzyme found in a wide
variety of  species  and  which  occurs  in  different cellular locations. The
sequences of the following 5'-nucleotidases are currently known:

 - Extracellular 5'-nucleotidase from mammals and electric ray.  This  isozyme
   is a homodimeric disulfide-bonded glycoprotein attached to the  membrane by
   a GPI-anchor. It requires zinc for its activity
 - Vibrio parahaemolyticus 5'-nucleotidase (gene nutA).  This isozyme is bound
   to the membrane by a lipid chain.  NutA  requires  chloride  and magnesium
   ions for   its  activity.  It  is    involved  in  degrading  extracellular
   5'-nucleotides for nutritional needs.
 - Periplasmic bacterial 5'-nucleotidase (gene ushA).  This enzyme, also known
   as UDP-sugar hydrolase (EC 3.6.1.45), can  degrade  UDP-glucose and   other
   nucleotide diphosphate  sugars.  It  produces  sugar-1-phosphate  which can
   then be used by the cell. UshA seems to require cobalt for its activity.

5'-nucleotidases are evolutionary related to the following enzyme:

 - Periplasmic bacterial 2',3'-cyclic-nucleotide 2'-phosphodiesterase (EC 3.1.
   4.16) (gene cpdB).  This  bifunctional  enzyme  catalyzes  two  consecutive
   reactions: it  first converts 2',3'-cyclic-nucleotide  to 3'-nucleotide and
   then acts as a 3'-nucleotidase.
 - Mosquito  apyrase  (EC  3.6.1.5)  (ATP-diphosphohydrolase) [2]. This enzyme
   catalyzes the  hydrolysis  of  ATP  into AMP and facilitates hematophagy by
   preventing ADP-dependent platelet aggregation in the host.

All these  proteins share a number of regions of sequence similarity, of which
we selected  two  as  signature  patterns.  Both regions are located in the N-
terminal section  of  these  enzymes.  The second pattern contains a perfectly
conserved pentapeptide.

-Consensus pattern: [LIVM]-x-[LIVM](2)-[HEA]-[TI]-x-D-x-H-[GSA]-x-[LIVMF]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Consensus pattern: [FYPH]-x(4)-[LIVM]-G-N-H-E-F-[DN]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: December 2004 / Pattern and text revised.

[ 1] Zimmermann H.
     "5'-Nucleotidase: molecular structure and functional aspects."
     Biochem. J. 285:345-365(1992).
     PubMed=1637327
[ 2] Champagne D.E., Smartt C.T., Ribeiro J.M.C., James A.A.
     "The salivary gland-specific apyrase of the mosquito Aedes aegypti is
     a member of the 5'-nucleotidase family."
     Proc. Natl. Acad. Sci. U.S.A. 92:694-698(1995).
     PubMed=7846038

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