Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P51691

- ARS_PSEAE

UniProt

P51691 - ARS_PSEAE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Arylsulfatase

Gene

atsA

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

A phenol sulfate + H2O = a phenol + sulfate.

Cofactori

Binds 1 calcium ion per subunit.

pH dependencei

Optimum pH is 8.9.

Temperature dependencei

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi13 – 131Calcium
Metal bindingi14 – 141Calcium
Metal bindingi51 – 511Calcium; via 3-oxoalanine
Active sitei115 – 1151
Metal bindingi317 – 3171Calcium
Metal bindingi318 – 3181Calcium

GO - Molecular functioni

  1. arylsulfatase activity Source: PseudoCAP
  2. metal ion binding Source: UniProtKB-KW
  3. phosphoric diester hydrolase activity Source: PseudoCAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Arylsulfatase (EC:3.1.6.1)
Short name:
AS
Alternative name(s):
Aryl-sulfate sulphohydrolase
Gene namesi
Name:atsA
Ordered Locus Names:PA0183
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000002438: Chromosome

Organism-specific databases

PseudoCAPiPA0183.

Subcellular locationi

Cytoplasm Curated

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 536535ArylsulfatasePRO_0000192683Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei51 – 5113-oxoalanine (Cys)1 Publication

Post-translational modificationi

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

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi208964.PA0183.

Structurei

Secondary structure

1
536
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 149Combined sources
Helixi21 – 233Combined sources
Helixi30 – 389Combined sources
Beta strandi39 – 468Combined sources
Helixi51 – 588Combined sources
Helixi64 – 674Combined sources
Helixi73 – 753Combined sources
Turni78 – 825Combined sources
Beta strandi87 – 893Combined sources
Beta strandi92 – 943Combined sources
Helixi97 – 1026Combined sources
Turni103 – 1053Combined sources
Beta strandi107 – 1137Combined sources
Helixi120 – 1223Combined sources
Turni124 – 1285Combined sources
Beta strandi130 – 1356Combined sources
Helixi155 – 1584Combined sources
Beta strandi164 – 1663Combined sources
Helixi180 – 19314Combined sources
Beta strandi201 – 2066Combined sources
Beta strandi211 – 2133Combined sources
Helixi218 – 2214Combined sources
Helixi222 – 2243Combined sources
Turni225 – 2306Combined sources
Helixi231 – 24515Combined sources
Helixi265 – 2673Combined sources
Helixi270 – 30334Combined sources
Helixi307 – 3093Combined sources
Beta strandi310 – 31910Combined sources
Helixi325 – 3273Combined sources
Helixi329 – 3313Combined sources
Helixi335 – 3428Combined sources
Helixi347 – 3493Combined sources
Helixi360 – 3689Combined sources
Beta strandi371 – 3733Combined sources
Beta strandi377 – 3793Combined sources
Helixi380 – 3834Combined sources
Beta strandi387 – 3904Combined sources
Beta strandi398 – 4014Combined sources
Helixi407 – 4093Combined sources
Helixi410 – 4189Combined sources
Beta strandi425 – 4273Combined sources
Helixi441 – 4444Combined sources
Beta strandi447 – 4493Combined sources
Beta strandi457 – 4626Combined sources
Beta strandi465 – 4706Combined sources
Beta strandi473 – 4775Combined sources
Turni480 – 4823Combined sources
Beta strandi485 – 4917Combined sources
Turni492 – 4943Combined sources
Turni503 – 5053Combined sources
Helixi507 – 52418Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HDHX-ray1.30A/B1-536[»]
ProteinModelPortaliP51691.
SMRiP51691. Positions 3-527.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51691.

Family & Domainsi

Sequence similaritiesi

Belongs to the sulfatase family.Curated

Phylogenomic databases

eggNOGiCOG3119.
HOGENOMiHOG000135353.
InParanoidiP51691.
KOiK01130.
OMAiVPMRGKS.
OrthoDBiEOG61VZ37.
PhylomeDBiP51691.

Family and domain databases

Gene3Di3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR000917. Sulfatase.
IPR024607. Sulfatase_CS.
[Graphical view]
PfamiPF00884. Sulfatase. 1 hit.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 1 hit.
PROSITEiPS00523. SULFATASE_1. 1 hit.
PS00149. SULFATASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P51691-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSKRPNFLVI VADDLGFSDI GAFGGEIATP NLDALAIAGL RLTDFHTAST
60 70 80 90 100
CSPTRSMLLT GTDHHIAGIG TMAEALTPEL EGKPGYEGHL NERVVALPEL
110 120 130 140 150
LREAGYQTLM AGKWHLGLKP EQTPHARGFE RSFSLLPGAA NHYGFEPPYD
160 170 180 190 200
ESTPRILKGT PALYVEDERY LDTLPEGFYS SDAFGDKLLQ YLKERDQSRP
210 220 230 240 250
FFAYLPFSAP HWPLQAPREI VEKYRGRYDA GPEALRQERL ARLKELGLVE
260 270 280 290 300
ADVEAHPVLA LTREWEALED EERAKSARAM EVYAAMVERM DWNIGRVVDY
310 320 330 340 350
LRRQGELDNT FVLFMSDNGA EGALLEAFPK FGPDLLGFLD RHYDNSLENI
360 370 380 390 400
GRANSYVWYG PRWAQAATAP SRLYKAFTTQ GGIRVPALVR YPRLSRQGAI
410 420 430 440 450
SHAFATVMDV TPTLLDLAGV RHPGKRWRGR EIAEPRGRSW LGWLSGETEA
460 470 480 490 500
AHDENTVTGW ELFGMRAIRQ GDWKAVYLPA PVGPATWQLY DLARDPGEIH
510 520 530
DLADSQPGKL AELIEHWKRY VSETGVVEGA SPFLVR
Length:536
Mass (Da):59,946
Last modified:January 23, 2007 - v3
Checksum:iE926EC099E14EA63
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21S → D AA sequence (PubMed:7744061)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z48540 Genomic DNA. Translation: CAA88421.2.
AE004091 Genomic DNA. Translation: AAG03573.1.
PIRiD83622.
S69336.
RefSeqiNP_248873.1. NC_002516.2.

Genome annotation databases

EnsemblBacteriaiAAG03573; AAG03573; PA0183.
GeneIDi879288.
KEGGipae:PA0183.
PATRICi19834574. VBIPseAer58763_0189.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z48540 Genomic DNA. Translation: CAA88421.2 .
AE004091 Genomic DNA. Translation: AAG03573.1 .
PIRi D83622.
S69336.
RefSeqi NP_248873.1. NC_002516.2.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HDH X-ray 1.30 A/B 1-536 [» ]
ProteinModelPortali P51691.
SMRi P51691. Positions 3-527.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 208964.PA0183.

Chemistry

BindingDBi P51691.
ChEMBLi CHEMBL5816.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG03573 ; AAG03573 ; PA0183 .
GeneIDi 879288.
KEGGi pae:PA0183.
PATRICi 19834574. VBIPseAer58763_0189.

Organism-specific databases

PseudoCAPi PA0183.

Phylogenomic databases

eggNOGi COG3119.
HOGENOMi HOG000135353.
InParanoidi P51691.
KOi K01130.
OMAi VPMRGKS.
OrthoDBi EOG61VZ37.
PhylomeDBi P51691.

Miscellaneous databases

EvolutionaryTracei P51691.

Family and domain databases

Gene3Di 3.40.720.10. 1 hit.
InterProi IPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR000917. Sulfatase.
IPR024607. Sulfatase_CS.
[Graphical view ]
Pfami PF00884. Sulfatase. 1 hit.
[Graphical view ]
SUPFAMi SSF53649. SSF53649. 1 hit.
PROSITEi PS00523. SULFATASE_1. 1 hit.
PS00149. SULFATASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiARS_PSEAE
AccessioniPrimary (citable) accession number: P51691
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 107 of the entry and version 3 of the sequence. [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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3