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Protein

Neutral ceramidase

Gene

PA0845

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.2 Publications

Miscellaneous

Alternate N-termini have been proposed by different authors. It either starts from Asp-25 (PubMed:10593963) or from Leu-27 (PubMed:12821326).2 Publications

Catalytic activityi

N-acylsphingosine + H2O = a carboxylate + sphingosine.3 Publications

Cofactori

Protein has several cofactor binding sites:

Activity regulationi

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.1 Publication

Kineticsi

  1. KM=139 µM for N-palmitoylsphingosine2 Publications
  1. Vmax=5.3 µmol/min/mg enzyme with N-palmitoylsphingosine as substrate2 Publications

pH dependencei

Optimum pH is 7.5-9.5.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi61Magnesium; via carbonyl oxygenCombined sources1 Publication1
Binding sitei84Substrate1 Publication1
Binding sitei92Substrate1 Publication1
Binding sitei111Substrate1 Publication1
Metal bindingi121Zinc; via tele nitrogenCombined sources1 Publication1
Binding sitei130Substrate1 Publication1
Metal bindingi228Zinc; via tele nitrogenCombined sources1 Publication1
Active sitei274NucleophileBy similarity1
Metal bindingi435ZincCombined sources1 Publication1
Binding sitei469Substrate1 Publication1
Metal bindingi472ZincCombined sources1 Publication1
Metal bindingi603MagnesiumCombined sources1 Publication1
Metal bindingi605Magnesium; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi608MagnesiumCombined sources1 Publication1

GO - Molecular functioni

  • ceramidase activity Source: UniProtKB-EC
  • metal ion binding Source: UniProtKB-KW
  • N-acylsphingosine amidohydrolase activity Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processLipid metabolism
LigandMagnesium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciPAER208964:G1FZ6-860-MONOMER
BRENDAi3.5.1.23 5087

Names & Taxonomyi

Protein namesi
Recommended name:
Neutral ceramidase (EC:3.5.1.23)
Short name:
N-CDase
Short name:
NCDase
Alternative name(s):
Acylsphingosine deacylase
N-acylsphingosine amidohydrolase
Gene namesi
Ordered Locus Names:PA0845
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA0845

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi121H → A: No ceramidase activity; when associated with A-123. 1 Publication1
Mutagenesisi123H → A: No ceramidase activity; when associated with A-121. 1 Publication1
Mutagenesisi184R → A: No ceramidase activity; when associated. 1 Publication1
Mutagenesisi435E → A: Slight ceramidase activity. 1 Publication1
Mutagenesisi472Y → A: No ceramidase activity; when associated. 1 Publication1
Mutagenesisi484Y → A: Slight ceramidase activity. 1 Publication1
Mutagenesisi665V → D: Abolishes enzyme activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 241 PublicationAdd BLAST24
ChainiPRO_000024711125 – 670Neutral ceramidaseAdd BLAST646

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi346 ↔ 3941 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ9I596
PRIDEiQ9I596

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi208964.PA0845

Structurei

Secondary structure

1670
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ9I596
SMRiQ9I596
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9I596

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni644 – 670Required for correct folding and localizationAdd BLAST27

Sequence similaritiesi

Belongs to the neutral ceramidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4107R72 Bacteria
ENOG410XQWE LUCA
HOGENOMiHOG000209915
InParanoidiQ9I596
KOiK12349
OMAiCKPALGH

Family and domain databases

Gene3Di2.60.40.2300, 1 hit
InterProiView protein in InterPro
IPR006823 Ceramidase_alk
IPR038445 NCDase_C_sf
IPR031331 NEUT/ALK_ceramidase_C
IPR031329 NEUT/ALK_ceramidase_N
PANTHERiPTHR12670 PTHR12670, 1 hit
PfamiView protein in Pfam
PF04734 Ceramidase_alk, 1 hit
PF17048 Ceramidse_alk_C, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9I596-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSRSAFTALL LSCVLLALSM PARADDLPYR FGLGKADITG EAAEVGMMGY
60 70 80 90 100
SSLEQKTAGI HMRQWARAFV IEEAASGRRL VYVNTDLGMI FQAVHLKVLA
110 120 130 140 150
RLKAKYPGVY DENNVMLAAT HTHSGPGGFS HYAMYNLSVL GFQEKTFNAI
160 170 180 190 200
VDGIVRSIER AQARLQPGRL FYGSGELRNA NRNRSLLSHL KNPDIVGYED
210 220 230 240 250
GIDPQMSVLS FVDANGELAG AISWFPVHST SMTNANHLIS PDNKGYASYH
260 270 280 290 300
WEHDVSRKSG FVAAFAQTNA GNLSPNLNLK PGSGPFDNEF DNTREIGLRQ
310 320 330 340 350
FAKAYEIAGQ AQEEVLGELD SRFRFVDFTR LPIRPEFTDG QPRQLCTAAI
360 370 380 390 400
GTSLAAGSTE DGPGPLGLEE GNNPFLSALG GLLTGVPPQE LVQCQAEKTI
410 420 430 440 450
LADTGNKKPY PWTPTVLPIQ MFRIGQLELL GAPAEFTVMA GVRIRRAVQA
460 470 480 490 500
ASEAAGIRHV VFNGYANAYA SYVTTREEYA AQEYEGGSTL YGPWTQAAYQ
510 520 530 540 550
QLFVDMAVAL RERLPVETSA IAPDLSCCQM NFQTGVVADD PYIGKSFGDV
560 570 580 590 600
LQQPRESYRI GDKVTVAFVT GHPKNDLRTE KTFLEVVNIG KDGKQTPETV
610 620 630 640 650
ATDNDWDTQY RWERVGISAS KATISWSIPP GTEPGHYYIR HYGNAKNFWT
660 670
QKISEIGGST RSFEVLGTTP
Length:670
Mass (Da):73,373
Last modified:March 1, 2001 - v1
Checksum:iF12C73EAC9CED287
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti90I → T in BAA88409 (PubMed:10593963).Curated1
Sequence conflicti181N → S in BAA88409 (PubMed:10593963).Curated1
Sequence conflicti196V → A in BAA88409 (PubMed:10593963).Curated1
Sequence conflicti598E → V in BAA88409 (PubMed:10593963).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB028646 Genomic DNA Translation: BAA88409.1
AJ315932 Genomic DNA Translation: CAC67511.1
AE004091 Genomic DNA Translation: AAG04234.1
PIRiC83540
RefSeqiNP_249536.1, NC_002516.2
WP_003114226.1, NC_002516.2

Genome annotation databases

EnsemblBacteriaiAAG04234; AAG04234; PA0845
GeneIDi880698
KEGGipae:PA0845
PATRICifig|208964.12.peg.877

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB028646 Genomic DNA Translation: BAA88409.1
AJ315932 Genomic DNA Translation: CAC67511.1
AE004091 Genomic DNA Translation: AAG04234.1
PIRiC83540
RefSeqiNP_249536.1, NC_002516.2
WP_003114226.1, NC_002516.2

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ZWSX-ray1.40A25-670[»]
2ZXCX-ray2.20A/B25-670[»]
ProteinModelPortaliQ9I596
SMRiQ9I596
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA0845

Proteomic databases

PaxDbiQ9I596
PRIDEiQ9I596

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG04234; AAG04234; PA0845
GeneIDi880698
KEGGipae:PA0845
PATRICifig|208964.12.peg.877

Organism-specific databases

PseudoCAPiPA0845

Phylogenomic databases

eggNOGiENOG4107R72 Bacteria
ENOG410XQWE LUCA
HOGENOMiHOG000209915
InParanoidiQ9I596
KOiK12349
OMAiCKPALGH

Enzyme and pathway databases

BioCyciPAER208964:G1FZ6-860-MONOMER
BRENDAi3.5.1.23 5087

Miscellaneous databases

EvolutionaryTraceiQ9I596

Family and domain databases

Gene3Di2.60.40.2300, 1 hit
InterProiView protein in InterPro
IPR006823 Ceramidase_alk
IPR038445 NCDase_C_sf
IPR031331 NEUT/ALK_ceramidase_C
IPR031329 NEUT/ALK_ceramidase_N
PANTHERiPTHR12670 PTHR12670, 1 hit
PfamiView protein in Pfam
PF04734 Ceramidase_alk, 1 hit
PF17048 Ceramidse_alk_C, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiNCASE_PSEAE
AccessioniPrimary (citable) accession number: Q9I596
Secondary accession number(s): Q7AY51, Q9RHQ0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: March 1, 2001
Last modified: November 7, 2018
This is version 95 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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