|
|
||
|
|
|
|
|
UniProt functional annotation for Q96GD0 | ||
|
|
|
|
|
|
||
| UniProt code: Q96GD0. |
|
||
| Organism: | |
Homo sapiens (Human). |
| Taxonomy: | |
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. |
|
||
|
||
| Function: | |
Functions as a pyridoxal phosphate (PLP) phosphatase, which also catalyzes the dephosphorylation of pyridoxine 5'-phosphate (PNP) and pyridoxamine 5'-phosphate (PMP), with order of substrate preference PLP > PNP > PMP and therefore plays a role in vitamin B6 metabolism (PubMed:14522954, PubMed:8132548). Also functions as a protein serine phosphatase that specifically dephosphorylates 'Ser-3' in proteins of the actin-depolymerizing factor (ADF)/cofilin family like CFL1 and DSTN. Thereby, regulates cofilin-dependent actin cytoskeleton reorganization, being required for normal progress through mitosis and normal cytokinesis. Does not dephosphorylate phosphothreonines in LIMK1. Does not dephosphorylate peptides containing phosphotyrosine (PubMed:15580268). {ECO:0000269|PubMed:14522954, ECO:0000269|PubMed:15580268, ECO:0000269|PubMed:8132548}. |
|
||
| Catalytic activity: | |
Reaction=H2O + pyridoxal 5'-phosphate = phosphate + pyridoxal; Xref=Rhea:RHEA:20533, ChEBI:CHEBI:15377, ChEBI:CHEBI:17310, ChEBI:CHEBI:43474, ChEBI:CHEBI:597326; EC=3.1.3.74; Evidence={ECO:0000269|PubMed:14522954}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20534; Evidence={ECO:0000305|PubMed:14522954}; |
| Catalytic activity: | |
Reaction=H2O + pyridoxine 5'-phosphate = phosphate + pyridoxine; Xref=Rhea:RHEA:25112, ChEBI:CHEBI:15377, ChEBI:CHEBI:16709, ChEBI:CHEBI:43474, ChEBI:CHEBI:58589; EC=3.1.3.74; Evidence={ECO:0000269|PubMed:14522954, ECO:0000269|PubMed:8132548}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25113; Evidence={ECO:0000305|PubMed:14522954}; |
| Catalytic activity: | |
Reaction=phosphate + pyridoxamine = H2O + pyridoxamine 5'-phosphate; Xref=Rhea:RHEA:25135, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57761, ChEBI:CHEBI:58451; EC=3.1.3.74; Evidence={ECO:0000269|PubMed:14522954}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25137; Evidence={ECO:0000305|PubMed:14522954}; |
| Catalytic activity: | |
Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000269|PubMed:15580268}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20630; Evidence={ECO:0000269|PubMed:15580268}; |
| Cofactor: | |
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:14522954, ECO:0000269|PubMed:15580268}; Note=Divalent metal ions. Mg(2+) is the most effective. {ECO:0000269|PubMed:14522954, ECO:0000269|PubMed:15580268}; |
| Activity regulation: | |
Inhibited by NaF, Zn(2+), Ca(2+), Mn(2+) and EDTA. {ECO:0000269|PubMed:15580268}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=2.5 uM for pyridoxal 5'-phosphate (at pH 7.4 and 37 degrees Celsius) {ECO:0000269|PubMed:14522954}; KM=43.4 uM for pyridoxine 5'-phosphate (at pH 7.4 and 37 degrees Celsius) {ECO:0000269|PubMed:14522954}; KM=80.6 uM for pyridoxamine 5'-phosphate (at pH 7.4 and 37 degrees Celsius) {ECO:0000269|PubMed:14522954}; Vmax=1.42 umol/min/mg enzyme with pyridoxal 5'-phosphate as substrate {ECO:0000269|PubMed:14522954}; Vmax=1.17 umol/min/mg enzyme with pyridoxine 5'-phosphate as substrate {ECO:0000269|PubMed:14522954}; Vmax=0.42 umol/min/mg enzyme with pyridoxamine 5'-phosphate as substrate {ECO:0000269|PubMed:14522954}; Note=Kcat is 1.52 sec(-1) for the dephosphorylation of pyridoxal 5'- phosphate (at pH 7.4 and 37 degrees Celsius). Kcat is 1.25 sec(-1) for the dephosphorylation of pyridoxine 5'-phosphate (at pH 7.4 and 37 degrees Celsius). Kcat is 0.45 sec(-1) for the dephosphorylation of pyridoxamine 5'-phosphate (at pH 7.4 and 37 degrees Celsius). {ECO:0000269|PubMed:14522954}; |
| Subunit: | |
Homodimer. {ECO:0000269|PubMed:14522954}. |
| Subcellular location: | |
Cytoplasm, cytosol {ECO:0000269|PubMed:15580268}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15580268}. Cell projection, ruffle membrane {ECO:0000269|PubMed:15580268}; Peripheral membrane protein {ECO:0000269|PubMed:15580268}; Cytoplasmic side {ECO:0000269|PubMed:15580268}. Cell projection, lamellipodium membrane {ECO:0000269|PubMed:15580268}; Peripheral membrane protein {ECO:0000269|PubMed:15580268}; Cytoplasmic side {ECO:0000269|PubMed:15580268}. Cell membrane {ECO:0000269|PubMed:15580268}; Peripheral membrane protein {ECO:0000269|PubMed:15580268}; Cytoplasmic side {ECO:0000269|PubMed:15580268}. Note=Colocalizes with the actin cytoskeleton in membrane ruffles and lamellipodia. Diffusely distributed throughout the cytosol during pro-metaphase and metaphase. Detected at the dynamic cell poles during telophase. Detected at the cleavage furrow and contractile ring during cytokinesis. Transiently detected at the plasma membrane in late stages of cytokinesis. Detected at the midbody. {ECO:0000269|PubMed:15580268}. |
| Tissue specificity: | |
Ubiquitously expressed (at protein level) (PubMed:23223568). Highly expressed in all the regions of central nerve system except the spinal cord. Also expressed at high level in liver and testis. In fetus, it is weakly expressed in all organs except brain (PubMed:14522954, PubMed:15580268). {ECO:0000269|PubMed:14522954, ECO:0000269|PubMed:15580268, ECO:0000269|PubMed:23223568}. |
| Similarity: | |
Belongs to the HAD-like hydrolase superfamily. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.