ID   SULF_CLOPE              Reviewed;         481 AA.
AC   Q8XNV1;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Arylsulfatase;
DE            EC=3.1.6.1;
DE   AltName: Full=Cys-type sulfatase;
GN   OrderedLocusNames=CPE0231;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
CC   -!- FUNCTION: Has sulfatase activity toward para-nitrophenyl sulfate, which
CC       is increased in presence of calcium ion. {ECO:0000250}.
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   -!- 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000016; BAB79937.1; -; Genomic_DNA.
DR   RefSeq; WP_011009688.1; NC_003366.1.
DR   AlphaFoldDB; Q8XNV1; -.
DR   SMR; Q8XNV1; -.
DR   STRING; 195102.gene:10489479; -.
DR   EnsemblBacteria; BAB79937; BAB79937; BAB79937.
DR   KEGG; cpe:CPE0231; -.
DR   HOGENOM; CLU_006332_9_2_9; -.
DR   OMA; DHGELHG; -.
DR   Proteomes; UP000000818; Chromosome.
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; IPR032506; DUF4976.
DR   InterPro; IPR024607; Sulfatase_CS.
DR   InterPro; IPR000917; Sulfatase_N.
DR   Pfam; PF16347; DUF4976; 1.
DR   Pfam; PF00884; Sulfatase; 1.
DR   SUPFAM; SSF53649; SSF53649; 1.
DR   PROSITE; PS00149; SULFATASE_2; 1.
PE   3: Inferred from homology;
KW   Calcium; Hydrolase; Metal-binding; Reference proteome.
FT   CHAIN           1..481
FT                   /note="Arylsulfatase"
FT                   /id="PRO_0000273187"
FT   ACT_SITE        51
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q0TUK6"
FT   ACT_SITE        102
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   BINDING         11
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         12
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         51
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /note="via 3-oxoalanine"
FT                   /evidence="ECO:0000250"
FT   BINDING         302
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         303
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         51
FT                   /note="3-oxoalanine (Cys)"
FT                   /evidence="ECO:0000250|UniProtKB:Q0TUK6"
SQ   SEQUENCE   481 AA;  55796 MW;  18FC4A649862D312 CRC64;
     MKPNIVLIMV DQMRGDCLGV NGNEFIETPN LDMMATEGYN FENAYTAVPS CIASRASILT
     GMSQKSHGRV GYEDGVSWNY ENTIASEFSK AGYHTQCIGK MHVYPERNLC GFHNIMLHDG
     YLHFARNKEG KASTQIEQCD DYLKWFREKK GHNVDLIDIG LDCNSWVSRP WGYEENLHPT
     NWVVNESIDF LRRRDPSKPF FLKMSFVRPH SPLDPPKFYF DMYKDEDLPE PLMGDWANKE
     DEENRGKDIN CVKGIINKKA LKRAKAAYYG SITHIDHQIG RFLIALSEYG KLNNTIFLFV
     SDHGDMMGDH NWFRKGIPYE GSARVPFFIY DPGNLLKGKK GKVFDEVLEL RDIMPTLLDF
     AHISIPDSVE GLSLKDLIEE RNSTWRDYIH GEHSFGEDSN HYIVTKKDKF LWFSQRGEEQ
     YFDLEKDPKE LTNLINSEEY KERIDYLRKI LIKELEGREE GYTDGNKLLK GYPVSTLKHI
     R