Neutral ceramidase
Details
- Name
- Neutral ceramidase
- Synonyms
- 3.5.1.23
- Acylsphingosine deacylase
- N-acylsphingosine amidohydrolase
- N-CDase
- Gene Name
- Not Available
- Organism
- Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
- Amino acid sequence
>lcl|BSEQ0012628|Neutral ceramidase MSRSAFTALLLSCVLLALSMPARADDLPYRFGLGKADITGEAAEVGMMGYSSLEQKTAGI HMRQWARAFVIEEAASGRRLVYVNTDLGMIFQAVHLKVLARLKAKYPGVYDENNVMLAAT HTHSGPGGFSHYAMYNLSVLGFQEKTFNAIVDGIVRSIERAQARLQPGRLFYGSGELRNA NRNRSLLSHLKNPDIVGYEDGIDPQMSVLSFVDANGELAGAISWFPVHSTSMTNANHLIS PDNKGYASYHWEHDVSRKSGFVAAFAQTNAGNLSPNLNLKPGSGPFDNEFDNTREIGLRQ FAKAYEIAGQAQEEVLGELDSRFRFVDFTRLPIRPEFTDGQPRQLCTAAIGTSLAAGSTE DGPGPLGLEEGNNPFLSALGGLLTGVPPQELVQCQAEKTILADTGNKKPYPWTPTVLPIQ MFRIGQLELLGAPAEFTVMAGVRIRRAVQAASEAAGIRHVVFNGYANAYASYVTTREEYA AQEYEGGSTLYGPWTQAAYQQLFVDMAVALRERLPVETSAIAPDLSCCQMNFQTGVVADD PYIGKSFGDVLQQPRESYRIGDKVTVAFVTGHPKNDLRTEKTFLEVVNIGKDGKQTPETV ATDNDWDTQYRWERVGISASKATISWSIPPGTEPGHYYIRHYGNAKNFWTQKISEIGGST RSFEVLGTTP
- Number of residues
- 670
- Molecular Weight
- 73372.125
- Theoretical pI
- 6.17
- GO Classification
- Functionsceramidase activity / metal ion bindingProcessesceramide catabolic process / long-chain fatty acid biosynthetic process / sphingosine biosynthetic processComponentsextracellular region
- General Function
- Metal ion binding
- Specific 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.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Secreted
- Gene sequence
>lcl|BSEQ0012629|Neutral ceramidase ATGTCACGTTCCGCATTCACCGCGCTCTTGCTGTCCTGCGTCCTGCTGGCGCTCTCCATG CCTGCCAGGGCCGACGACCTGCCCTACCGCTTCGGCCTGGGCAAGGCGGACATCACCGGC GAAGCCGCCGAAGTCGGCATGATGGGTTACTCCTCCCTCGAACAGAAGACCGCCGGCATC CACATGCGCCAGTGGGCGCGTGCCTTCGTGATCGAGGAAGCGGCCAGCGGACGTCGCCTG GTCTACGTCAACACCGACCTGGGGATGATCTTCCAGGCCGTGCACCTGAAGGTCCTGGCC CGGCTCAAGGCGAAGTACCCCGGTGTCTACGACGAGAACAACGTGATGCTCGCCGCCACC CACACCCACTCCGGTCCGGGCGGCTTCTCCCACTACGCGATGTACAACCTGTCGGTGCTC GGCTTCCAGGAAAAGACCTTCAACGCCATCGTCGACGGCATCGTCCGCTCCATCGAGCGG GCCCAGGCCAGGTTGCAGCCCGGCCGCCTGTTCTACGGCAGCGGCGAGCTGCGCAACGCC AACCGCAACCGTTCGCTGCTGTCGCACCTGAAGAATCCGGACATCGTCGGCTACGAGGAT GGCATCGACCCGCAGATGAGCGTGCTCAGCTTCGTCGACGCCAACGGCGAGCTGGCCGGC GCGATCAGTTGGTTCCCGGTGCACAGCACCTCGATGACCAACGCCAATCACCTGATCTCC CCGGACAACAAGGGCTACGCCTCCTATCACTGGGAGCACGACGTCAGCCGCAAGAGCGGT TTCGTCGCCGCCTTCGCCCAGACCAATGCCGGCAACCTGTCGCCCAACCTGAACCTGAAG CCCGGCTCCGGTCCCTTCGACAACGAGTTCGACAACACCCGCGAGATCGGTCTGCGCCAA TTCGCCAAGGCCTACGAGATCGCCGGCCAGGCCCAGGAGGAAGTGCTCGGCGAACTGGAT TCGCGCTTCCGTTTCGTCGACTTCACCCGCCTGCCGATCCGCCCGGAGTTCACCGACGGC CAGCCGCGCCAGTTGTGCACCGCGGCCATCGGCACCAGCCTGGCCGCCGGTAGCACCGAA GACGGTCCAGGCCCGCTGGGGCTGGAGGAAGGCAACAATCCGTTCCTCTCGGCCCTTGGC GGGTTGCTCACCGGCGTGCCGCCGCAGGAACTGGTGCAATGCCAGGCGGAAAAGACCATC CTCGCCGACACCGGCAACAAGAAACCCTACCCCTGGACGCCGACGGTGCTGCCGATCCAG ATGTTCCGCATCGGCCAGTTGGAACTGCTCGGCGCCCCCGCCGAGTTCACCGTGATGGCC GGGGTGCGGATCCGCCGCGCGGTGCAGGCGGCCAGCGAAGCGGCCGGTATCCGCCATGTG GTCTTCAATGGCTACGCGAATGCCTATGCCAGCTACGTCACCACCCGCGAGGAATACGCC GCCCAGGAATACGAAGGCGGCTCGACCCTCTACGGCCCCTGGACCCAGGCCGCCTACCAG CAGTTGTTCGTCGACATGGCGGTGGCGCTGCGCGAACGCCTGCCGGTGGAAACCTCGGCG ATAGCGCCGGACCTGTCCTGCTGCCAGATGAACTTCCAGACCGGAGTAGTGGCCGACGAT CCCTATATCGGCAAGTCCTTCGGCGACGTGTTGCAACAACCCAGGGAAAGTTATCGCATC GGCGACAAGGTGACCGTCGCTTTCGTGACCGGACATCCGAAGAATGACTTGCGCACCGAG AAGACTTTCCTGGAAGTGGTGAATATCGGCAAGGATGGCAAACAGACGCCCGAGACCGTT GCCACCGATAATGACTGGGATACTCAATACCGCTGGGAGAGAGTGGGTATATCTGCCTCG AAAGCGACTATCAGCTGGTCCATTCCACCAGGGACCGAGCCCGGCCATTACTACATCAGG CACTACGGCAACGCGAAGAACTTCTGGACCCAGAAGATCAGCGAAATCGGCGGCTCGACC CGCTCCTTCGAGGTGCTCGGCACCACTCCCTAG
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q9I596 UniProtKB Entry Name NCASE_PSEAE GenBank Protein ID 6594292 GenBank Gene ID AB028646 - General References
- Okino N, Ichinose S, Omori A, Imayama S, Nakamura T, Ito M: Molecular cloning, sequencing, and expression of the gene encoding alkaline ceramidase from Pseudomonas aeruginosa. Cloning of a ceramidase homologue from Mycobacterium tuberculosis. J Biol Chem. 1999 Dec 17;274(51):36616-22. [Article]
- Stover CK, Pham XQ, Erwin AL, Mizoguchi SD, Warrener P, Hickey MJ, Brinkman FS, Hufnagle WO, Kowalik DJ, Lagrou M, Garber RL, Goltry L, Tolentino E, Westbrock-Wadman S, Yuan Y, Brody LL, Coulter SN, Folger KR, Kas A, Larbig K, Lim R, Smith K, Spencer D, Wong GK, Wu Z, Paulsen IT, Reizer J, Saier MH, Hancock RE, Lory S, Olson MV: Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen. Nature. 2000 Aug 31;406(6799):959-64. [Article]
- Nieuwenhuizen WF, van Leeuwen S, Jack RW, Egmond MR, Gotz F: Molecular cloning and characterization of the alkaline ceramidase from Pseudomonas aeruginosa PA01. Protein Expr Purif. 2003 Jul;30(1):94-104. [Article]
- Okino N, Tani M, Imayama S, Ito M: Purification and characterization of a novel ceramidase from Pseudomonas aeruginosa. J Biol Chem. 1998 Jun 5;273(23):14368-73. [Article]
- Kita K, Sueyoshi N, Okino N, Inagaki M, Ishida H, Kiso M, Imayama S, Nakamura T, Ito M: Activation of bacterial ceramidase by anionic glycerophospholipids: possible involvement in ceramide hydrolysis on atopic skin by Pseudomonas ceramidase. Biochem J. 2002 Mar 15;362(Pt 3):619-26. [Article]
- Tani M, Okino N, Sueyoshi N, Ito M: Conserved amino acid residues in the COOH-terminal tail are indispensable for the correct folding and localization and enzyme activity of neutral ceramidase. J Biol Chem. 2004 Jul 9;279(28):29351-8. Epub 2004 May 3. [Article]
- Inoue T, Okino N, Kakuta Y, Hijikata A, Okano H, Goda HM, Tani M, Sueyoshi N, Kambayashi K, Matsumura H, Kai Y, Ito M: Mechanistic insights into the hydrolysis and synthesis of ceramide by neutral ceramidase. J Biol Chem. 2009 Apr 3;284(14):9566-77. doi: 10.1074/jbc.M808232200. Epub 2008 Dec 16. [Article]