SMART: Pfam domain PhoD

PhoD

PFAM accession number:	PF09423
Interpro abstract (IPR018946):	Alkaline phosphatase D (PhoD) [ (PUBMED:8760916) ] catalyses the reaction: phosphate monoester + H(2)O = an alcohol + phosphate. PhoD is similar to Ca(2+)-dependent phospholipase D [ (PUBMED:17906150) ], which catalyses the hydrolysis of the ester bond between the phosphatidic acid and alcohol moieties of phospholipids [ (PUBMED:15588701) (PUBMED:12519726) ]. PhoD (also known as alkaline phosphatase D/APaseD in Bacillus subtilis) is a secreted phosphodiesterase encoded by phoD of the Pho regulon in Bacillus subtilis. PhoD homologs are found in prokaryotes, eukaryotes, and archaea. PhoD contains a twin arginine (RR) motif and is transported by the Tat (Twin-arginine translocation) translocation pathway machinery (TatAyCy) [ (PUBMED:8760916) (PUBMED:19180538) (PUBMED:16517638) (PUBMED:11719524) ]. Proteins containing this domain also includes the Fusarium oxysporum Fso1 protein [ (PUBMED:18039941) ]. PhoD belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination [ (PUBMED:25217636) ].

PFAM accession number:

PF09423

Interpro abstract (IPR018946):

Alkaline phosphatase D (PhoD) [ (PUBMED:8760916) ] catalyses the reaction: phosphate monoester + H(2)O = an alcohol + phosphate. PhoD is similar to Ca(2+)-dependent phospholipase D [ (PUBMED:17906150) ], which catalyses the hydrolysis of the ester bond between the phosphatidic acid and alcohol moieties of phospholipids [ (PUBMED:15588701) (PUBMED:12519726) ].

PhoD (also known as alkaline phosphatase D/APaseD in Bacillus subtilis) is a secreted phosphodiesterase encoded by phoD of the Pho regulon in Bacillus subtilis. PhoD homologs are found in prokaryotes, eukaryotes, and archaea. PhoD contains a twin arginine (RR) motif and is transported by the Tat (Twin-arginine translocation) translocation pathway machinery (TatAyCy) [ (PUBMED:8760916) (PUBMED:19180538) (PUBMED:16517638) (PUBMED:11719524) ]. Proteins containing this domain also includes the Fusarium oxysporum Fso1 protein [ (PUBMED:18039941) ].

PhoD belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination [ (PUBMED:25217636) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry PhoD