ARS_PSEAE
ID ARS_PSEAE Reviewed; 536 AA.
AC P51691;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Arylsulfatase;
DE Short=AS;
DE EC=3.1.6.1 {ECO:0000269|PubMed:7744061, ECO:0000269|PubMed:9748219};
DE AltName: Full=Aryl-sulfate sulphohydrolase;
GN Name=atsA; OrderedLocusNames=PA0183;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=7744061; DOI=10.1111/j.1432-1033.1995.0385k.x;
RA Beil S., Kehrli H., James P., Staudenmann W., Cook A.M., Leisinger T.,
RA Kertesz M.A.;
RT "Purification and characterization of the arylsulfatase synthesized by
RT Pseudomonas aeruginosa PAO during growth in sulfate-free medium and cloning
RT of the arylsulfatase gene (atsA).";
RL Eur. J. Biochem. 229:385-394(1995).
RN [2]
RP SEQUENCE REVISION.
RA Kertesz M.A.;
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, OXOALANINE AT CYS-51, AND MUTAGENESIS OF
RP CYS-51.
RX PubMed=9748219; DOI=10.1074/jbc.273.40.25560;
RA Dierks T., Miech C., Hummerjohann J., Schmidt B., Kertesz M.A.,
RA von Figura K.;
RT "Posttranslational formation of formylglycine in prokaryotic sulfatases by
RT modification of either cysteine or serine.";
RL J. Biol. Chem. 273:25560-25564(1998).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS), AND OXOALANINE AT CYS-51.
RX PubMed=11435113; DOI=10.1016/s0969-2126(01)00609-8;
RA Boltes I., Czapinska H., Kahnert A., von Buelow R., Dierks T., Schmidt B.,
RA von Figura K., Kertesz M.A., Uson I.;
RT "1.3 A structure of arylsulfatase from Pseudomonas aeruginosa establishes
RT the catalytic mechanism of sulfate ester cleavage in the sulfatase
RT family.";
RL Structure 9:483-491(2001).
CC -!- FUNCTION: Hydrolyzes the bond between sulfate and the aromatic ring in
CC a compound such as 4-nitrocatechol sulfate.
CC {ECO:0000269|PubMed:7744061, ECO:0000269|PubMed:9748219}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aryl sulfate + H2O = a phenol + H(+) + sulfate;
CC Xref=Rhea:RHEA:17261, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16189, ChEBI:CHEBI:33853, ChEBI:CHEBI:140317; EC=3.1.6.1;
CC Evidence={ECO:0000269|PubMed:7744061, ECO:0000269|PubMed:9748219};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:11435113};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:11435113};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.9.;
CC Temperature dependence:
CC Optimum temperature is 57 degrees Celsius. Incubation that exceeds 20
CC minutes above 50 degrees Celsius leads to enzyme inactivation.;
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: The conversion to 3-oxoalanine (also known as C-formylglycine,
CC FGly), of a serine or cysteine residue in prokaryotes and of a cysteine
CC residue in eukaryotes, is critical for catalytic activity.
CC {ECO:0000269|PubMed:11435113, ECO:0000269|PubMed:9748219}.
CC -!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
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DR EMBL; Z48540; CAA88421.2; -; Genomic_DNA.
DR EMBL; AE004091; AAG03573.1; -; Genomic_DNA.
DR PIR; D83622; D83622.
DR PIR; S69336; S69336.
DR RefSeq; NP_248873.1; NC_002516.2.
DR RefSeq; WP_003106692.1; NZ_QZGE01000015.1.
DR PDB; 1HDH; X-ray; 1.30 A; A/B=1-536.
DR PDB; 4CXK; X-ray; 1.86 A; A/B=1-534.
DR PDB; 4CXS; X-ray; 2.30 A; A/B=1-536.
DR PDB; 4CXU; X-ray; 2.03 A; A/B=1-536.
DR PDB; 4CYR; X-ray; 1.72 A; A/B=1-536.
DR PDB; 4CYS; X-ray; 1.88 A; A/B=1-536.
DR PDB; 5AJ9; X-ray; 2.00 A; A/B=1-536.
DR PDBsum; 1HDH; -.
DR PDBsum; 4CXK; -.
DR PDBsum; 4CXS; -.
DR PDBsum; 4CXU; -.
DR PDBsum; 4CYR; -.
DR PDBsum; 4CYS; -.
DR PDBsum; 5AJ9; -.
DR AlphaFoldDB; P51691; -.
DR SMR; P51691; -.
DR STRING; 287.DR97_3139; -.
DR BindingDB; P51691; -.
DR ChEMBL; CHEMBL5816; -.
DR DrugBank; DB02289; 2-Aminopropanedioic Acid.
DR PaxDb; P51691; -.
DR PRIDE; P51691; -.
DR EnsemblBacteria; AAG03573; AAG03573; PA0183.
DR GeneID; 879288; -.
DR KEGG; pae:PA0183; -.
DR PATRIC; fig|208964.12.peg.189; -.
DR PseudoCAP; PA0183; -.
DR HOGENOM; CLU_006332_11_1_6; -.
DR InParanoid; P51691; -.
DR OMA; EAYPMVQ; -.
DR PhylomeDB; P51691; -.
DR BioCyc; MetaCyc:MON-20682; -.
DR BioCyc; PAER208964:G1FZ6-184-MON; -.
DR BRENDA; 3.1.6.1; 5087.
DR BRENDA; 3.1.6.2; 5087.
DR EvolutionaryTrace; P51691; -.
DR PRO; PR:P51691; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004065; F:arylsulfatase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IDA:PseudoCAP.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR024607; Sulfatase_CS.
DR InterPro; IPR000917; Sulfatase_N.
DR Pfam; PF00884; Sulfatase; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
DR PROSITE; PS00523; SULFATASE_1; 1.
DR PROSITE; PS00149; SULFATASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Metal-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7744061"
FT CHAIN 2..536
FT /note="Arylsulfatase"
FT /id="PRO_0000192683"
FT ACT_SITE 51
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:11435113,
FT ECO:0000269|PubMed:9748219"
FT ACT_SITE 115
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 13
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:11435113"
FT BINDING 14
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:11435113"
FT BINDING 51
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000269|PubMed:11435113"
FT BINDING 317
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:11435113"
FT BINDING 318
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:11435113"
FT MOD_RES 51
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000269|PubMed:11435113,
FT ECO:0000269|PubMed:9748219"
FT MUTAGEN 51
FT /note="C->S: Abolishes formation of 3-oxoalanine (also
FT known as C-formylglycine, FGly). Strongly reduced enzyme
FT activity."
FT /evidence="ECO:0000269|PubMed:9748219"
FT CONFLICT 2
FT /note="S -> D (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 6..14
FT /evidence="ECO:0007829|PDB:1HDH"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:1HDH"
FT HELIX 30..38
FT /evidence="ECO:0007829|PDB:1HDH"
FT STRAND 39..46
FT /evidence="ECO:0007829|PDB:1HDH"
FT HELIX 51..58
FT /evidence="ECO:0007829|PDB:1HDH"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:1HDH"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:1HDH"
FT TURN 78..82
FT /evidence="ECO:0007829|PDB:1HDH"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:1HDH"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:1HDH"
FT HELIX 97..102
FT /evidence="ECO:0007829|PDB:1HDH"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:1HDH"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:1HDH"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:1HDH"
FT TURN 124..128
FT /evidence="ECO:0007829|PDB:1HDH"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:1HDH"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:1HDH"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:1HDH"
FT HELIX 180..193
FT /evidence="ECO:0007829|PDB:1HDH"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:1HDH"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:1HDH"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:1HDH"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:1HDH"
FT TURN 225..230
FT /evidence="ECO:0007829|PDB:1HDH"
FT HELIX 231..245
FT /evidence="ECO:0007829|PDB:1HDH"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:1HDH"
FT HELIX 270..303
FT /evidence="ECO:0007829|PDB:1HDH"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:1HDH"
FT STRAND 310..319
FT /evidence="ECO:0007829|PDB:1HDH"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:1HDH"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:1HDH"
FT HELIX 335..342
FT /evidence="ECO:0007829|PDB:1HDH"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:1HDH"
FT HELIX 360..368
FT /evidence="ECO:0007829|PDB:1HDH"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:1HDH"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:1HDH"
FT HELIX 380..383
FT /evidence="ECO:0007829|PDB:1HDH"
FT STRAND 387..390
FT /evidence="ECO:0007829|PDB:1HDH"
FT STRAND 398..401
FT /evidence="ECO:0007829|PDB:1HDH"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:1HDH"
FT HELIX 410..418
FT /evidence="ECO:0007829|PDB:1HDH"
FT STRAND 425..427
FT /evidence="ECO:0007829|PDB:1HDH"
FT HELIX 441..444
FT /evidence="ECO:0007829|PDB:1HDH"
FT STRAND 447..449
FT /evidence="ECO:0007829|PDB:1HDH"
FT STRAND 457..462
FT /evidence="ECO:0007829|PDB:1HDH"
FT STRAND 465..470
FT /evidence="ECO:0007829|PDB:1HDH"
FT STRAND 473..477
FT /evidence="ECO:0007829|PDB:1HDH"
FT TURN 480..482
FT /evidence="ECO:0007829|PDB:1HDH"
FT STRAND 485..491
FT /evidence="ECO:0007829|PDB:1HDH"
FT TURN 492..494
FT /evidence="ECO:0007829|PDB:1HDH"
FT TURN 503..505
FT /evidence="ECO:0007829|PDB:1HDH"
FT HELIX 507..524
FT /evidence="ECO:0007829|PDB:1HDH"
SQ SEQUENCE 536 AA; 59946 MW; E926EC099E14EA63 CRC64;
MSKRPNFLVI VADDLGFSDI GAFGGEIATP NLDALAIAGL RLTDFHTAST CSPTRSMLLT
GTDHHIAGIG TMAEALTPEL EGKPGYEGHL NERVVALPEL LREAGYQTLM AGKWHLGLKP
EQTPHARGFE RSFSLLPGAA NHYGFEPPYD ESTPRILKGT PALYVEDERY LDTLPEGFYS
SDAFGDKLLQ YLKERDQSRP FFAYLPFSAP HWPLQAPREI VEKYRGRYDA GPEALRQERL
ARLKELGLVE ADVEAHPVLA LTREWEALED EERAKSARAM EVYAAMVERM DWNIGRVVDY
LRRQGELDNT FVLFMSDNGA EGALLEAFPK FGPDLLGFLD RHYDNSLENI GRANSYVWYG
PRWAQAATAP SRLYKAFTTQ GGIRVPALVR YPRLSRQGAI SHAFATVMDV TPTLLDLAGV
RHPGKRWRGR EIAEPRGRSW LGWLSGETEA AHDENTVTGW ELFGMRAIRQ GDWKAVYLPA
PVGPATWQLY DLARDPGEIH DLADSQPGKL AELIEHWKRY VSETGVVEGA SPFLVR
