Function and Biology

REACTION MECHANISM OF ALKALINE PHOSPHATASE BASED ON CRYSTAL STRUCTURES. TWO METAL ION CATALYSIS

Source organism: Escherichia coli
Biochemical function: metal ion binding
Biological process: dephosphorylation
Cellular component: periplasmic space

EC 3.1.3.1: Alkaline phosphatase

Reaction catalysed:
A phosphate monoester + H(2)O = an alcohol + phosphate
Systematic name:
Phosphate-monoester phosphohydrolase (alkaline optimum)
Alternative Name(s):
  • Alkaline phenyl phosphatase
  • Alkaline phosphohydrolase
  • Alkaline phosphomonoesterase
  • Glycerophosphatase
  • Orthophosphoric-monoester phosphohydrolase (alkaline optimum)
  • Phosphomonoesterase

Sequence family

Pfam Protein family (Pfam)
PF00245
Domain description: Alkaline phosphatase
Occurring in:
  1. Alkaline phosphatase
The deposited structure of PDB entry 1alk contains 4 copies of Pfam domain PF00245 (Alkaline phosphatase) in Alkaline phosphatase. Showing 2 copies in chain A.

InterPro InterPro annotations
IPR001952
Domain description: Alkaline phosphatase
Occurring in:
  1. Alkaline phosphatase
IPR017850
Domain description: Alkaline-phosphatase-like, core domain superfamily
Occurring in:
  1. Alkaline phosphatase
IPR018299
Domain description: Alkaline phosphatase, active site
Occurring in:
  1. Alkaline phosphatase

Structure domain

CATH CATH domain
3.40.720.10
Class: Alpha Beta
Architecture: 3-Layer(aba) Sandwich
Topology: Alkaline Phosphatase, subunit A
Homology: Alkaline Phosphatase, subunit A
Occurring in:
  1. Alkaline phosphatase
The deposited structure of PDB entry 1alk contains 2 copies of CATH domain 3.40.720.10 (Alkaline Phosphatase, subunit A) in Alkaline phosphatase. Showing 1 copy in chain A.
SCOP SCOP annotation
53650
Class: Alpha and beta proteins (a/b)
Fold: Alkaline phosphatase-like
Superfamily: Alkaline phosphatase-like
Occurring in:
  1. Alkaline phosphatase
The deposited structure of PDB entry 1alk contains 2 copies of SCOP domain 53650 (Alkaline phosphatase) in Alkaline phosphatase. Showing 1 copy in chain A.