ID   ARS_CHLRE               Reviewed;         647 AA.
AC   P14217;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Arylsulfatase;
DE            Short=AS;
DE            EC=3.1.6.1;
DE   AltName: Full=Aryl-sulfate sulphohydrolase;
DE   Flags: Precursor;
GN   Name=AS;
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND PROTEIN SEQUENCE OF 22-55.
RC   STRAIN=cw15;
RX   PubMed=2476654; DOI=10.1007/bf00331273;
RA   de Hostos E.L., Schilling J., Grossman A.R.;
RT   "Structure and expression of the gene encoding the periplasmic
RT   arylsulfatase of Chlamydomonas reinhardtii.";
RL   Mol. Gen. Genet. 218:229-239(1989).
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.
CC   -!- INDUCTION: By sulfur deprivation.
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   -!- SEQUENCE CAUTION:
CC       Sequence=CAA34302.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAA36545.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X16180; CAA34302.1; ALT_FRAME; mRNA.
DR   EMBL; X52304; CAA36545.1; ALT_FRAME; mRNA.
DR   EMBL; X16179; CAA34301.1; -; Genomic_DNA.
DR   PIR; JQ0310; KJKM.
DR   STRING; 3055.EDP04462; -.
DR   eggNOG; KOG3731; Eukaryota.
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   GO; GO:0018958; P:phenol-containing compound metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.720.10; -; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR012083; Arylsulfatase.
DR   InterPro; IPR024607; Sulfatase_CS.
DR   InterPro; IPR000917; Sulfatase_N.
DR   Pfam; PF00884; Sulfatase; 1.
DR   PIRSF; PIRSF000972; Arylsulf_plant; 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; Glycoprotein; Hydrolase; Metal-binding;
KW   Periplasm; Signal; Stress response.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:2476654"
FT   CHAIN           22..647
FT                   /note="Arylsulfatase"
FT                   /id="PRO_0000033444"
FT   ACT_SITE        73
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   BINDING         35
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         36
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         73
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /note="via 3-oxoalanine"
FT                   /evidence="ECO:0000250"
FT   BINDING         323
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         324
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         73
FT                   /note="3-oxoalanine (Cys)"
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   CARBOHYD        42
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        90
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        279
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        444
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        528
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   647 AA;  72106 MW;  7404EA1BF233F0B1 CRC64;
     MGALAVFAVA CLAAVASVAH AADTKKPNFV VIFTDDQDAI QNSTHPHYMP SLHKYIRYPG
     VELSQYFVTT PVCCPSRTNL XRGQFAHNTN FTSVLPPYGG WAKWKGLGID QSYLPLWLKD
     QGYNTYYVGK FLVDYSVSNY QQVPRAGTIS MPXVTPYTFD YNTRLQRNGA TPNIYPGEYS
     TDVIRDKGVA QIKSAVAAGK PFYAQISPIA PHTSTQISTN PATGVTRSYF FPPIPAPPHW
     QLFSDANLPG GSXNKNLYEV DVSDKPAWIR ALPLAQQNNR TYQEEIYRLR LRSLGPDELI
     EQVVKTLDEA GVLDNTYIIY SADNGYHVGA HRFGAGKTTG YEEDLRVPFL IRGPGIKASK
     SDKPQNSKVG LHVDFAPTIL SLAGASHLLG DKGLDGTPLG LYANDDGTLP SDYPRPEQHR
     QQFQGEFWGG WSDELLQNLR SQPNNTWKVV RTYDESSKQG WKLIAQCTNE RELYDLRKDP
     GELYNIYDKA KPAVRSRLEG LLAVLAVCKG ESCSNPWKIL HPDGTVKNFT QALNSKYDRI
     YNAIRPFTYK RCLPYLDWDN EDSQFKTQIR GANPAAGVGH HRLLTAASER AIATRRRAQA
     AVSAELADGP AVFQAKVEEK SVPVPQDILK ADVEKWFAFN NAEYYLA