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Arylsulfatase (AS) (EC 3.1.6.1) (Aryl-sulfate sulphohydrolase)

 ARS_CHLRE               Reviewed;         647 AA.
P14217;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
05-JUL-2017, entry version 88.
RecName: Full=Arylsulfatase;
Short=AS;
EC=3.1.6.1;
AltName: Full=Aryl-sulfate sulphohydrolase;
Flags: Precursor;
Name=AS;
Chlamydomonas reinhardtii (Chlamydomonas smithii).
Eukaryota; Viridiplantae; Chlorophyta; Chlorophyceae;
Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
NCBI_TaxID=3055;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND PROTEIN SEQUENCE OF
22-55.
STRAIN=cw15;
PubMed=2476654; DOI=10.1007/BF00331273;
de Hostos E.L., Schilling J., Grossman A.R.;
"Structure and expression of the gene encoding the periplasmic
arylsulfatase of Chlamydomonas reinhardtii.";
Mol. Gen. Genet. 218:229-239(1989).
-!- CATALYTIC ACTIVITY: A phenol sulfate + H(2)O = a phenol + sulfate.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
-!- SUBCELLULAR LOCATION: Periplasm.
-!- INDUCTION: By sulfur deprivation.
-!- PTM: 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. {ECO:0000250}.
-!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA34302.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
Sequence=CAA36545.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
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EMBL; X16180; CAA34302.1; ALT_FRAME; mRNA.
EMBL; X52304; CAA36545.1; ALT_FRAME; mRNA.
EMBL; X16179; CAA34301.1; -; Genomic_DNA.
PIR; JQ0310; KJKM.
ProteinModelPortal; P14217; -.
PaxDb; P14217; -.
eggNOG; KOG3731; Eukaryota.
eggNOG; COG3119; LUCA.
GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
GO; GO:0004065; F:arylsulfatase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0018958; P:phenol-containing compound metabolic process; IEA:InterPro.
Gene3D; 3.40.720.10; -; 1.
InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
InterPro; IPR017850; Alkaline_phosphatase_core.
InterPro; IPR012083; Arylsulfatase.
InterPro; IPR024607; Sulfatase_CS.
InterPro; IPR000917; Sulfatase_N.
Pfam; PF00884; Sulfatase; 1.
PIRSF; PIRSF000972; Arylsulf_plant; 1.
SUPFAM; SSF53649; SSF53649; 2.
PROSITE; PS00523; SULFATASE_1; 1.
PROSITE; PS00149; SULFATASE_2; 1.
1: Evidence at protein level;
Calcium; Direct protein sequencing; Glycoprotein; Hydrolase;
Metal-binding; Periplasm; Signal; Stress response.
SIGNAL 1 21 {ECO:0000269|PubMed:2476654}.
CHAIN 22 647 Arylsulfatase.
/FTId=PRO_0000033444.
METAL 35 35 Calcium. {ECO:0000250}.
METAL 36 36 Calcium. {ECO:0000250}.
METAL 73 73 Calcium; via 3-oxoalanine. {ECO:0000250}.
METAL 323 323 Calcium. {ECO:0000250}.
METAL 324 324 Calcium. {ECO:0000250}.
MOD_RES 73 73 3-oxoalanine (Cys). {ECO:0000250}.
CARBOHYD 42 42 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 90 90 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 279 279 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 444 444 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 528 528 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
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


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