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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: Annotation score: 5 out of 5-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

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:

Enzyme 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi61 – 611Magnesium; via carbonyl oxygenCombined sources1 Publication
Binding sitei84 – 841Substrate1 Publication
Binding sitei92 – 921Substrate1 Publication
Binding sitei111 – 1111Substrate1 Publication
Metal bindingi121 – 1211Zinc; via tele nitrogenCombined sources1 Publication
Binding sitei130 – 1301Substrate1 Publication
Metal bindingi228 – 2281Zinc; via tele nitrogenCombined sources1 Publication
Active sitei274 – 2741NucleophileBy similarity
Metal bindingi435 – 4351ZincCombined sources1 Publication
Binding sitei469 – 4691Substrate1 Publication
Metal bindingi472 – 4721ZincCombined sources1 Publication
Metal bindingi603 – 6031MagnesiumCombined sources1 Publication
Metal bindingi605 – 6051Magnesium; via carbonyl oxygenCombined sources1 Publication
Metal bindingi608 – 6081MagnesiumCombined sources1 Publication

GO - Molecular functioni

  • ceramidase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • long-chain fatty acid biosynthetic process Source: UniProtKB
  • sphingosine biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid metabolism

Keywords - Ligandi

Magnesium, Metal-binding, Zinc

Enzyme and pathway databases

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

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi121 – 1211H → A: No ceramidase activity; when associated with A-123. 1 Publication
Mutagenesisi123 – 1231H → A: No ceramidase activity; when associated with A-121. 1 Publication
Mutagenesisi184 – 1841R → A: No ceramidase activity; when associated. 1 Publication
Mutagenesisi435 – 4351E → A: Slight ceramidase activity. 1 Publication
Mutagenesisi472 – 4721Y → A: No ceramidase activity; when associated. 1 Publication
Mutagenesisi484 – 4841Y → A: Slight ceramidase activity. 1 Publication
Mutagenesisi665 – 6651V → D: Abolishes enzyme activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 24241 PublicationAdd
BLAST
Chaini25 – 670646Neutral ceramidasePRO_0000247111Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi346 ↔ 3941 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ9I596.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi208964.PA0845.

Structurei

Secondary structure

1
670
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 3710Combined sources
Beta strandi43 – 508Combined sources
Beta strandi56 – 627Combined sources
Beta strandi65 – 7612Combined sources
Beta strandi79 – 8810Combined sources
Helixi92 – 10514Combined sources
Turni107 – 1093Combined sources
Turni112 – 1143Combined sources
Beta strandi115 – 1195Combined sources
Beta strandi122 – 1265Combined sources
Helixi133 – 1364Combined sources
Helixi137 – 1393Combined sources
Helixi144 – 16219Combined sources
Beta strandi166 – 17611Combined sources
Beta strandi179 – 1846Combined sources
Helixi186 – 1894Combined sources
Beta strandi205 – 2139Combined sources
Beta strandi218 – 2247Combined sources
Beta strandi238 – 2403Combined sources
Helixi242 – 25312Combined sources
Beta strandi258 – 2603Combined sources
Beta strandi262 – 2665Combined sources
Beta strandi273 – 2753Combined sources
Beta strandi277 – 2815Combined sources
Beta strandi283 – 2853Combined sources
Helixi289 – 31022Combined sources
Beta strandi313 – 3153Combined sources
Beta strandi319 – 3279Combined sources
Helixi335 – 3373Combined sources
Beta strandi338 – 3414Combined sources
Beta strandi359 – 3635Combined sources
Helixi374 – 3785Combined sources
Helixi389 – 3946Combined sources
Turni395 – 3973Combined sources
Beta strandi400 – 4023Combined sources
Beta strandi408 – 4103Combined sources
Beta strandi415 – 42410Combined sources
Beta strandi427 – 4315Combined sources
Beta strandi433 – 4364Combined sources
Helixi438 – 45215Combined sources
Helixi453 – 4553Combined sources
Beta strandi459 – 4635Combined sources
Beta strandi465 – 4684Combined sources
Helixi476 – 4816Combined sources
Turni484 – 4874Combined sources
Helixi495 – 51218Combined sources
Helixi526 – 5283Combined sources
Beta strandi550 – 5523Combined sources
Beta strandi556 – 5594Combined sources
Beta strandi563 – 5697Combined sources
Helixi573 – 5753Combined sources
Beta strandi583 – 59311Combined sources
Beta strandi598 – 6025Combined sources
Beta strandi608 – 6158Combined sources
Turni616 – 6183Combined sources
Beta strandi619 – 6279Combined sources
Beta strandi634 – 64613Combined sources
Turni648 – 6503Combined sources
Beta strandi653 – 6597Combined sources
Beta strandi663 – 6664Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZWSX-ray1.40A25-670[»]
2ZXCX-ray2.20A/B25-670[»]
ProteinModelPortaliQ9I596.
SMRiQ9I596. Positions 26-668.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9I596.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni644 – 67027Required for correct folding and localizationAdd
BLAST

Sequence similaritiesi

Belongs to the neutral ceramidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4107R72. Bacteria.
ENOG410XQWE. LUCA.
HOGENOMiHOG000209915.
InParanoidiQ9I596.
KOiK12349.
OMAiMGSFDIT.

Family and domain databases

InterProiIPR006823. Ceramidase_alk.
IPR031331. NEUT/ALK_ceramidase_C.
IPR031329. NEUT/ALK_ceramidase_N.
[Graphical view]
PANTHERiPTHR12670. PTHR12670. 1 hit.
PfamiPF04734. Ceramidase_alk. 1 hit.
PF17048. Ceramidse_alk_C. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti90 – 901I → T in BAA88409 (PubMed:10593963).Curated
Sequence conflicti181 – 1811N → S in BAA88409 (PubMed:10593963).Curated
Sequence conflicti196 – 1961V → A in BAA88409 (PubMed:10593963).Curated
Sequence conflicti598 – 5981E → V in BAA88409 (PubMed:10593963).Curated

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. NZ_ASJY01000128.1.

Genome annotation databases

EnsemblBacteriaiAAG04234; AAG04234; PA0845.
GeneIDi880698.
KEGGipae:PA0845.
PATRICi19835970. VBIPseAer58763_0877.

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. NZ_ASJY01000128.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZWSX-ray1.40A25-670[»]
2ZXCX-ray2.20A/B25-670[»]
ProteinModelPortaliQ9I596.
SMRiQ9I596. Positions 26-668.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA0845.

Proteomic databases

PaxDbiQ9I596.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG04234; AAG04234; PA0845.
GeneIDi880698.
KEGGipae:PA0845.
PATRICi19835970. VBIPseAer58763_0877.

Organism-specific databases

PseudoCAPiPA0845.

Phylogenomic databases

eggNOGiENOG4107R72. Bacteria.
ENOG410XQWE. LUCA.
HOGENOMiHOG000209915.
InParanoidiQ9I596.
KOiK12349.
OMAiMGSFDIT.

Enzyme and pathway databases

BRENDAi3.5.1.23. 5087.

Miscellaneous databases

EvolutionaryTraceiQ9I596.

Family and domain databases

InterProiIPR006823. Ceramidase_alk.
IPR031331. NEUT/ALK_ceramidase_C.
IPR031329. NEUT/ALK_ceramidase_N.
[Graphical view]
PANTHERiPTHR12670. PTHR12670. 1 hit.
PfamiPF04734. Ceramidase_alk. 1 hit.
PF17048. Ceramidse_alk_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNCASE_PSEAE
AccessioniPrimary (citable) accession number: Q9I596
Secondary accession number(s): Q7AY51, Q9RHQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: March 1, 2001
Last modified: September 7, 2016
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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

Keywords - Technical termi

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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.