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UniProt functional annotation for Q9I596 | ||
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| UniProt code: Q9I596. |
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| Organism: | |
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1). |
| Taxonomy: | |
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas. |
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| Function: | |
Catalyzes the cleavage of the N-acyl linkage of the ceramides (Cers) to yield sphingosine (Sph) and free fatty acid at an optimal pH of 8-9. Also catalyzes the synthesis of Cers from Sph and fatty acid. {ECO:0000269|PubMed:19088069, ECO:0000269|PubMed:9603946}. |
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| Catalytic activity: | |
Reaction=an N-acylsphing-4-enine + H2O = a fatty acid + sphing-4-enine; Xref=Rhea:RHEA:20856, ChEBI:CHEBI:15377, ChEBI:CHEBI:28868, ChEBI:CHEBI:52639, ChEBI:CHEBI:57756; EC=3.5.1.23; Evidence={ECO:0000269|PubMed:10593963, ECO:0000269|PubMed:12821326, ECO:0000269|PubMed:9603946}; |
| Cofactor: | |
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:19088069}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:19088069}; |
| Cofactor: | |
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:19088069}; |
| Activity regulation: | |
Inhibited by EDTA, EGTA and D/L-sphinganine D- erythro-sphingosine. L-erythro-sphingosine is a less powerful inhibitor. Stimulated by glycerophospholipids: cardiolipin is the most effective, followed by phosphatidic acid, phosphatidylethanolamine and phosphatidylglycerol, whereas phosphatidylcholine, lysophosphatidic acid and diacylglycerol are less effective. {ECO:0000269|PubMed:11879188}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=139 uM for N-palmitoylsphingosine {ECO:0000269|PubMed:12821326, ECO:0000269|PubMed:9603946}; Vmax=5.3 umol/min/mg enzyme with N-palmitoylsphingosine as substrate {ECO:0000269|PubMed:12821326, ECO:0000269|PubMed:9603946}; pH dependence: Optimum pH is 7.5-9.5. {ECO:0000269|PubMed:12821326, ECO:0000269|PubMed:9603946}; |
| Subunit: | |
Homodimer. {ECO:0000269|PubMed:19088069}. |
| Subcellular location: | |
Secreted {ECO:0000305}. |
| Miscellaneous: | |
Alternate N-termini have been proposed by different authors. It either starts from Asp-25 (PubMed:10593963) or from Leu-27 (PubMed:12821326). {ECO:0000305|PubMed:10593963, ECO:0000305|PubMed:12821326}. |
| Similarity: | |
Belongs to the neutral ceramidase family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.