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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)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
  • 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)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.

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
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi28 – 37Combined sources10
Beta strandi43 – 50Combined sources8
Beta strandi56 – 62Combined sources7
Beta strandi65 – 76Combined sources12
Beta strandi79 – 88Combined sources10
Helixi92 – 105Combined sources14
Turni107 – 109Combined sources3
Turni112 – 114Combined sources3
Beta strandi115 – 119Combined sources5
Beta strandi122 – 126Combined sources5
Helixi133 – 136Combined sources4
Helixi137 – 139Combined sources3
Helixi144 – 162Combined sources19
Beta strandi166 – 176Combined sources11
Beta strandi179 – 184Combined sources6
Helixi186 – 189Combined sources4
Beta strandi205 – 213Combined sources9
Beta strandi218 – 224Combined sources7
Beta strandi238 – 240Combined sources3
Helixi242 – 253Combined sources12
Beta strandi258 – 260Combined sources3
Beta strandi262 – 266Combined sources5
Beta strandi273 – 275Combined sources3
Beta strandi277 – 281Combined sources5
Beta strandi283 – 285Combined sources3
Helixi289 – 310Combined sources22
Beta strandi313 – 315Combined sources3
Beta strandi319 – 327Combined sources9
Helixi335 – 337Combined sources3
Beta strandi338 – 341Combined sources4
Beta strandi359 – 363Combined sources5
Helixi374 – 378Combined sources5
Helixi389 – 394Combined sources6
Turni395 – 397Combined sources3
Beta strandi400 – 402Combined sources3
Beta strandi408 – 410Combined sources3
Beta strandi415 – 424Combined sources10
Beta strandi427 – 431Combined sources5
Beta strandi433 – 436Combined sources4
Helixi438 – 452Combined sources15
Helixi453 – 455Combined sources3
Beta strandi459 – 463Combined sources5
Beta strandi465 – 468Combined sources4
Helixi476 – 481Combined sources6
Turni484 – 487Combined sources4
Helixi495 – 512Combined sources18
Helixi526 – 528Combined sources3
Beta strandi550 – 552Combined sources3
Beta strandi556 – 559Combined sources4
Beta strandi563 – 569Combined sources7
Helixi573 – 575Combined sources3
Beta strandi583 – 593Combined sources11
Beta strandi598 – 602Combined sources5
Beta strandi608 – 615Combined sources8
Turni616 – 618Combined sources3
Beta strandi619 – 627Combined sources9
Beta strandi634 – 646Combined sources13
Turni648 – 650Combined sources3
Beta strandi653 – 659Combined sources7
Beta strandi663 – 666Combined sources4

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...

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.
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)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. 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
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.

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: November 2, 2016
This is version 87 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.