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UniProt functional annotation for Q03529 | ||
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| UniProt code: Q03529. |
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| Organism: | |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). |
| Taxonomy: | |
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. |
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| Function: | |
Ceramide hydroxylase involved in the hydroxylation of sphingolipid-associated very long chain fatty acids (PubMed:9353282, PubMed:9368039, PubMed:26977056, PubMed:9559540, PubMed:16652392, PubMed:19074599). Postulated to hydroxylate the very long chain fatty acid of dihydroceramides and phytoceramides at C-2 (PubMed:9368039, PubMed:26977056). {ECO:0000269|PubMed:16652392, ECO:0000269|PubMed:19074599, ECO:0000269|PubMed:26977056, ECO:0000269|PubMed:9353282, ECO:0000269|PubMed:9368039, ECO:0000269|PubMed:9559540}. |
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| Catalytic activity: | |
Reaction=2 [Fe(II)-cytochrome b5] + an N-(1,2 saturated acyl)-(4R)- hydroxysphinganine + 2 H(+) + O2 = 2 [Fe(III)-cytochrome b5] + an N- (2R-hydroxyacyl)-4R-hydroxysphinganine + H2O; Xref=Rhea:RHEA:46520, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:86274, ChEBI:CHEBI:86275; EC=1.14.18.6; Evidence={ECO:0000305|PubMed:26977056, ECO:0000305|PubMed:9368039}; |
| Catalytic activity: | |
Reaction=2 [Fe(II)-cytochrome b5] + an N-(1,2-saturated acyl)sphinganine + 2 H(+) + O2 = 2 [Fe(III)-cytochrome b5] + an N- [(2'R)-hydroxyacyl]sphinganine + H2O; Xref=Rhea:RHEA:46512, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:86265, ChEBI:CHEBI:86266; EC=1.14.18.7; Evidence={ECO:0000305|PubMed:9368039}; |
| Catalytic activity: | |
Reaction=2 [Fe(II)-cytochrome b5] + 2 H(+) + N-hexacosanoyl-(4R)- hydroxysphinganine + O2 = 2 [Fe(III)-cytochrome b5] + H2O + N-(2- hydroxyhexacosanyl)-(4R)-hydroxysphinganine; Xref=Rhea:RHEA:33663, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:52374, ChEBI:CHEBI:52980; Evidence={ECO:0000269|PubMed:16652392, ECO:0000269|PubMed:9353282, ECO:0000269|PubMed:9368039}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33664; Evidence={ECO:0000305|PubMed:16652392, ECO:0000305|PubMed:9353282, ECO:0000305|PubMed:9368039}; |
| Cofactor: | |
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305|PubMed:26515067}; Note=Binds 2 Zn(2+) ions per subunit that likely form a catalytic dimetal center. {ECO:0000269|PubMed:26515067}; |
| Pathway: | |
Sphingolipid metabolism. {ECO:0000269|PubMed:12006573, ECO:0000269|PubMed:16652392, ECO:0000269|PubMed:19074599, ECO:0000269|PubMed:26977056, ECO:0000269|PubMed:9353282, ECO:0000269|PubMed:9368039, ECO:0000269|PubMed:9559540}. |
| Subcellular location: | |
Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}. |
| Domain: | |
The histidine box domains may contain the active site and/or be involved in metal ion binding. |
| Disruption phenotype: | |
Causes a lack of alpha-hydroxylated very long chain fatty acids in yeast sphingolipids. This confers resistance to syringomycin E, an antifungal cyclic lipodepsinonapeptide produced by Pseudomonas syringae. {ECO:0000269|PubMed:10922463}. |
| Miscellaneous: | |
Present with 3290 molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}. |
| Similarity: | |
Belongs to the sterol desaturase family. SCS7 subfamily. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.