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Protein

Arylsulfatase

Gene

atsA

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

Catalytic activityi

A phenol sulfate + H2O = a phenol + sulfate.

Cofactori

Ca2+Note: Binds 1 Ca2+ 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)DescriptionActionsGraphical viewLength
Metal bindingi13Calcium1
Metal bindingi14Calcium1
Metal bindingi51Calcium; via 3-oxoalanine1
Active sitei1151
Metal bindingi317Calcium1
Metal bindingi318Calcium1

GO - Molecular functioni

  • arylsulfatase activity Source: PseudoCAP
  • metal ion binding Source: UniProtKB-KW
  • phosphoric diester hydrolase activity Source: PseudoCAP

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.6.1. 5087.

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 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA0183.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL5816.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00001926832 – 536ArylsulfataseAdd BLAST535

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei513-oxoalanine (Cys)1 Publication1

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

Proteomic databases

PaxDbiP51691.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi208964.PA0183.

Chemistry databases

BindingDBiP51691.

Structurei

Secondary structure

1536
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 14Combined sources9
Helixi21 – 23Combined sources3
Helixi30 – 38Combined sources9
Beta strandi39 – 46Combined sources8
Helixi51 – 58Combined sources8
Helixi64 – 67Combined sources4
Helixi73 – 75Combined sources3
Turni78 – 82Combined sources5
Beta strandi87 – 89Combined sources3
Beta strandi92 – 94Combined sources3
Helixi97 – 102Combined sources6
Turni103 – 105Combined sources3
Beta strandi107 – 113Combined sources7
Helixi120 – 122Combined sources3
Turni124 – 128Combined sources5
Beta strandi130 – 135Combined sources6
Helixi155 – 158Combined sources4
Beta strandi164 – 166Combined sources3
Helixi180 – 193Combined sources14
Beta strandi201 – 206Combined sources6
Beta strandi211 – 213Combined sources3
Helixi218 – 221Combined sources4
Helixi222 – 224Combined sources3
Turni225 – 230Combined sources6
Helixi231 – 245Combined sources15
Helixi265 – 267Combined sources3
Helixi270 – 303Combined sources34
Helixi307 – 309Combined sources3
Beta strandi310 – 319Combined sources10
Helixi325 – 327Combined sources3
Helixi329 – 331Combined sources3
Helixi335 – 342Combined sources8
Helixi347 – 349Combined sources3
Helixi360 – 368Combined sources9
Beta strandi371 – 373Combined sources3
Beta strandi377 – 379Combined sources3
Helixi380 – 383Combined sources4
Beta strandi387 – 390Combined sources4
Beta strandi398 – 401Combined sources4
Helixi407 – 409Combined sources3
Helixi410 – 418Combined sources9
Beta strandi425 – 427Combined sources3
Helixi441 – 444Combined sources4
Beta strandi447 – 449Combined sources3
Beta strandi457 – 462Combined sources6
Beta strandi465 – 470Combined sources6
Beta strandi473 – 477Combined sources5
Turni480 – 482Combined sources3
Beta strandi485 – 491Combined sources7
Turni492 – 494Combined sources3
Turni503 – 505Combined sources3
Helixi507 – 524Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HDHX-ray1.30A/B1-536[»]
4CXKX-ray1.86A/B1-534[»]
4CXSX-ray2.30A/B1-536[»]
4CXUX-ray2.03A/B1-536[»]
4CYRX-ray1.72A/B1-536[»]
4CYSX-ray1.88A/B1-536[»]
5AJ9X-ray2.00A/B1-536[»]
ProteinModelPortaliP51691.
SMRiP51691.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51691.

Family & Domainsi

Sequence similaritiesi

Belongs to the sulfatase family.Curated

Phylogenomic databases

eggNOGiENOG4107QRH. Bacteria.
COG3119. LUCA.
HOGENOMiHOG000135353.
InParanoidiP51691.
KOiK01130.
OMAiNIGRANS.
PhylomeDBiP51691.

Family and domain databases

Gene3Di3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR024607. Sulfatase_CS.
IPR000917. Sulfatase_N.
[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)DescriptionActionsGraphical viewLength
Sequence conflicti2S → D AA sequence (PubMed:7744061).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48540 Genomic DNA. Translation: CAA88421.2.
AE004091 Genomic DNA. Translation: AAG03573.1.
PIRiD83622.
S69336.
RefSeqiNP_248873.1. NC_002516.2.
WP_003106692.1. NZ_ASJY01000040.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48540 Genomic DNA. Translation: CAA88421.2.
AE004091 Genomic DNA. Translation: AAG03573.1.
PIRiD83622.
S69336.
RefSeqiNP_248873.1. NC_002516.2.
WP_003106692.1. NZ_ASJY01000040.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HDHX-ray1.30A/B1-536[»]
4CXKX-ray1.86A/B1-534[»]
4CXSX-ray2.30A/B1-536[»]
4CXUX-ray2.03A/B1-536[»]
4CYRX-ray1.72A/B1-536[»]
4CYSX-ray1.88A/B1-536[»]
5AJ9X-ray2.00A/B1-536[»]
ProteinModelPortaliP51691.
SMRiP51691.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA0183.

Chemistry databases

BindingDBiP51691.
ChEMBLiCHEMBL5816.

Proteomic databases

PaxDbiP51691.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

PseudoCAPiPA0183.

Phylogenomic databases

eggNOGiENOG4107QRH. Bacteria.
COG3119. LUCA.
HOGENOMiHOG000135353.
InParanoidiP51691.
KOiK01130.
OMAiNIGRANS.
PhylomeDBiP51691.

Enzyme and pathway databases

BRENDAi3.1.6.1. 5087.

Miscellaneous databases

EvolutionaryTraceiP51691.
PROiP51691.

Family and domain databases

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

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: November 2, 2016
This is version 123 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

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.