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P51691 (ARS_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arylsulfatase

Short name=AS
EC=3.1.6.1
Alternative name(s):
Aryl-sulfate sulphohydrolase
Gene names
Name:atsA
Ordered Locus Names:PA0183
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length536 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

A phenol sulfate + H2O = a phenol + sulfate.

Cofactor

Binds 1 calcium ion per subunit.

Subunit structure

Monomer.

Subcellular location

Cytoplasm Potential.

Post-translational modification

The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity By similarity.

Sequence similarities

Belongs to the sulfatase family.

Biophysicochemical properties

pH dependence:

Optimum pH is 8.9.

Temperature dependence:

Optimum temperature is 57 degrees Celsius. Incubation that exceeds 20 minutes above 50 degrees Celsius leads to enzyme inactivation.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionarylsulfatase activity

Inferred from direct assay Ref.1. Source: PseudoCAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoric diester hydrolase activity

Inferred from direct assay PubMed 19554727. Source: PseudoCAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 536535Arylsulfatase
PRO_0000192683

Sites

Active site1151
Metal binding131Calcium
Metal binding141Calcium
Metal binding511Calcium; via 3-oxoalanine
Metal binding3171Calcium
Metal binding3181Calcium

Amino acid modifications

Modified residue5113-oxoalanine (Cys)

Experimental info

Sequence conflict21S → D AA sequence Ref.1

Secondary structure

................................................................................................ 536
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P51691 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E926EC099E14EA63

FASTA53659,946
        10         20         30         40         50         60 
MSKRPNFLVI VADDLGFSDI GAFGGEIATP NLDALAIAGL RLTDFHTAST CSPTRSMLLT 

        70         80         90        100        110        120 
GTDHHIAGIG TMAEALTPEL EGKPGYEGHL NERVVALPEL LREAGYQTLM AGKWHLGLKP 

       130        140        150        160        170        180 
EQTPHARGFE RSFSLLPGAA NHYGFEPPYD ESTPRILKGT PALYVEDERY LDTLPEGFYS 

       190        200        210        220        230        240 
SDAFGDKLLQ YLKERDQSRP FFAYLPFSAP HWPLQAPREI VEKYRGRYDA GPEALRQERL 

       250        260        270        280        290        300 
ARLKELGLVE ADVEAHPVLA LTREWEALED EERAKSARAM EVYAAMVERM DWNIGRVVDY 

       310        320        330        340        350        360 
LRRQGELDNT FVLFMSDNGA EGALLEAFPK FGPDLLGFLD RHYDNSLENI GRANSYVWYG 

       370        380        390        400        410        420 
PRWAQAATAP SRLYKAFTTQ GGIRVPALVR YPRLSRQGAI SHAFATVMDV TPTLLDLAGV 

       430        440        450        460        470        480 
RHPGKRWRGR EIAEPRGRSW LGWLSGETEA AHDENTVTGW ELFGMRAIRQ GDWKAVYLPA 

       490        500        510        520        530 
PVGPATWQLY DLARDPGEIH DLADSQPGKL AELIEHWKRY VSETGVVEGA SPFLVR 

« Hide

References

« Hide 'large scale' references
[1]"Purification and characterization of the arylsulfatase synthesized by Pseudomonas aeruginosa PAO during growth in sulfate-free medium and cloning of the arylsulfatase gene (atsA)."
Beil S., Kehrli H., James P., Staudenmann W., Cook A.M., Leisinger T., Kertesz M.A.
Eur. J. Biochem. 229:385-394(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[2]Kertesz M.A.
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. expand/collapse author list , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.
Nature 406:959-964(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[4]"1.3 A structure of arylsulfatase from Pseudomonas aeruginosa establishes the catalytic mechanism of sulfate ester cleavage in the sulfatase family."
Boltes I., Czapinska H., Kahnert A., von Buelow R., Dierks T., Schmidt B., von Figura K., Kertesz M.A., Uson I.
Structure 9:483-491(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS), OXOALANINE AT CYS-51.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z48540 Genomic DNA. Translation: CAA88421.2.
AE004091 Genomic DNA. Translation: AAG03573.1.
PIRD83622.
S69336.
RefSeqNP_248873.1. NC_002516.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HDHX-ray1.30A/B1-536[»]
ProteinModelPortalP51691.
SMRP51691. Positions 3-527.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING208964.PA0183.

Chemistry

BindingDBP51691.
ChEMBLCHEMBL5816.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG03573; AAG03573; PA0183.
GeneID879288.
KEGGpae:PA0183.
PATRIC19834574. VBIPseAer58763_0189.

Organism-specific databases

PseudoCAPPA0183.

Phylogenomic databases

eggNOGCOG3119.
HOGENOMHOG000135353.
KOK01130.
OMAVPMRGKS.
OrthoDBEOG61VZ37.
PhylomeDBP51691.

Family and domain databases

Gene3D3.40.720.10. 1 hit.
InterProIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR000917. Sulfatase.
IPR024607. Sulfatase_CS.
[Graphical view]
PfamPF00884. Sulfatase. 1 hit.
[Graphical view]
SUPFAMSSF53649. SSF53649. 1 hit.
PROSITEPS00523. SULFATASE_1. 1 hit.
PS00149. SULFATASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP51691.

Entry information

Entry nameARS_PSEAE
AccessionPrimary (citable) accession number: P51691
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 105 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references