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P51691

- ARS_PSEAE

UniProt

P51691 - ARS_PSEAE

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
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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

    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-SubCell

    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)

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

    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.
    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

    MSKRPNFLVI VADDLGFSDI GAFGGEIATP NLDALAIAGL RLTDFHTAST    50
    CSPTRSMLLT GTDHHIAGIG TMAEALTPEL EGKPGYEGHL NERVVALPEL 100
    LREAGYQTLM AGKWHLGLKP EQTPHARGFE RSFSLLPGAA NHYGFEPPYD 150
    ESTPRILKGT PALYVEDERY LDTLPEGFYS SDAFGDKLLQ YLKERDQSRP 200
    FFAYLPFSAP HWPLQAPREI VEKYRGRYDA GPEALRQERL ARLKELGLVE 250
    ADVEAHPVLA LTREWEALED EERAKSARAM EVYAAMVERM DWNIGRVVDY 300
    LRRQGELDNT FVLFMSDNGA EGALLEAFPK FGPDLLGFLD RHYDNSLENI 350
    GRANSYVWYG PRWAQAATAP SRLYKAFTTQ GGIRVPALVR YPRLSRQGAI 400
    SHAFATVMDV TPTLLDLAGV RHPGKRWRGR EIAEPRGRSW LGWLSGETEA 450
    AHDENTVTGW ELFGMRAIRQ GDWKAVYLPA PVGPATWQLY DLARDPGEIH 500
    DLADSQPGKL AELIEHWKRY VSETGVVEGA SPFLVR 536
    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.
    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

    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 1, 2014
    This is version 106 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