ID   ATSA_KLEAE              Reviewed;         464 AA.
AC   P20713;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Arylsulfatase;
DE            Short=AS;
DE            EC=3.1.6.1;
DE   AltName: Full=Aryl-sulfate sulphohydrolase;
DE   Flags: Precursor;
GN   Name=atsA;
OS   Klebsiella aerogenes (Enterobacter aerogenes).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=548;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 21-33.
RX   PubMed=2180918; DOI=10.1128/jb.172.4.2131-2140.1990;
RA   Murooka Y., Ishibashi K., Yasumoto M., Sasaki M., Sugino H., Azakami H.,
RA   Yamashita M.;
RT   "A sulfur- and tyramine-regulated Klebsiella aerogenes operon containing
RT   the arylsulfatase (atsA) gene and the atsB gene.";
RL   J. Bacteriol. 172:2131-2140(1990).
CC   -!- FUNCTION: Plays an important role in the mineralization of sulfates.
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   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
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:0000250}.
CC   -!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
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DR   EMBL; M31938; AAA25051.1; -; Genomic_DNA.
DR   PIR; B35159; B35159.
DR   AlphaFoldDB; P20713; -.
DR   SMR; P20713; -.
DR   STRING; 548.EAG7_02824; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004065; F:arylsulfatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   Calcium; Direct protein sequencing; Hydrolase; Metal-binding; Periplasm;
KW   Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:2180918"
FT   CHAIN           21..464
FT                   /note="Arylsulfatase"
FT                   /id="PRO_0000033447"
FT   ACT_SITE        72
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   ACT_SITE        134
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   BINDING         34
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         35
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         72
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /note="via 3-oxoalanine"
FT                   /evidence="ECO:0000250"
FT   BINDING         329
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         330
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         72
FT                   /note="3-oxoalanine (Ser)"
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
SQ   SEQUENCE   464 AA;  51471 MW;  C8D09AB9EEF9C627 CRC64;
     MNKKAMAAAV SMILAGGAHA AQQERPNVIV IIADDMGYSD ISPFGGEIPT PNLQAMAEQG
     MRMSQYYTSP MSAPARSMLL TGNSNQQAGM GGMWWYDSTI GKEGYELRLT DRVTTMAERF
     KDAGYNTLMA GKWHLGFVPG ATPKDRGFNH AFAFMGGGTS HFNDAIPLGT VEAFHTYYTR
     DGERVSLPDD FYSSEAYARQ MNSWIKATPK EQPVFAWLAF TAPHDPLQAP DEWIKRFKGQ
     YEQGYAEVYR QRIARLKALG IIHDDTPLPH LELDKEWEAL TPEQQKYTAK VMQVYAAMIA
     NMDAQIGTLM ETLKQTGRDK NTLLVFLTDN GANPAQGFYY ESTPEFWKQF DNSYDNVGRK
     GSFVSYGPHW ANVSNAPYAN YHKTTSAQGG INTDFMISGP GITRHGKIDA STMAVYDVAP
     TLYEFAGIDP NKSLAKKPVL PMIGVSLSAI SPAKYRSRRA ELRG