ARS_VOLCA
ID ARS_VOLCA Reviewed; 649 AA.
AC Q10723;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Arylsulfatase;
DE Short=AS;
DE EC=3.1.6.1;
DE AltName: Full=Aryl-sulfate sulphohydrolase;
DE Flags: Precursor;
OS Volvox carteri (Green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Volvocaceae; Volvox.
OX NCBI_TaxID=3067;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RC STRAIN=f. Nagariensis / HK10;
RX PubMed=8168504; DOI=10.1111/j.1432-1033.1994.tb18723.x;
RA Hallmann A., Sumper M.;
RT "An inducible arylsulfatase of Volvox carteri with properties suitable for
RT a reporter-gene system. Purification, characterization and molecular
RT cloning.";
RL Eur. J. Biochem. 221:143-150(1994).
RN [2]
RP PROTEIN SEQUENCE OF 64-76, ACTIVE SITE, AND OXOALANINE AT CYS-72.
RX PubMed=8681943; DOI=10.1111/j.1432-1033.1996.0341z.x;
RA Selmer T., Hallmann A., Schmidt B., Sumper M., von Figura K.;
RT "The evolutionary conservation of a novel protein modification, the
RT conversion of cysteine to serinesemialdehyde in arylsulfatase from Volvox
RT carteri.";
RL Eur. J. Biochem. 238:341-345(1996).
CC -!- FUNCTION: Is commonly produced by soil microorganisms and plays an
CC 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 -!- ACTIVITY REGULATION: Inhibited by Na(3)BO(3) and KCN. No inhibition by
CC sodium dodecyl sulfate, even at high concentration.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0.;
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius. Thermostable.;
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}.
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DR EMBL; X77214; CAA54426.1; -; mRNA.
DR PIR; S43229; S43229.
DR AlphaFoldDB; Q10723; -.
DR SMR; Q10723; -.
DR BioCyc; MetaCyc:MON-16826; -.
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..22
FT CHAIN 23..649
FT /note="Arylsulfatase"
FT /id="PRO_0000033445"
FT ACT_SITE 72
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:8681943"
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 324
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 325
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 72
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000269|PubMed:8681943"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 224
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 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 489
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 531
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 649 AA; 72287 MW; 0C23EFD77C43F7B9 CRC64;
MLQRLVVALC LLGFAALTAA AAHQRPNFVV IFTDDQDGIQ NSTHPRYQPK LHEHIRYPGI
ELKNYFVTTP VCCPSRTNLW RGQFSHNTNF TDVLGPHGGY AKWKSLGIDK SYLPVWLQNL
GYNTYYVGKF LVDYSVSNYQ NVPAGWTDID ALVTPYTFDY NNPGFSRNGA TPNIYPGFYS
TDVIADKAVA QIKTAVAAGK PFYAQISPIA PHTSTQIYFD PVANATKTFF YPPIPAPRHW
ELFSDATLPE GTSHKNLYEA DVSDKPAWIR ALPLAQQNNR TYLEEVYRLR LRSLASVDEL
IDRVVATLQE AGVLDNTYLI YSADNGYHVG THRFGAGKVT AYDEDLRVPF LIRGPGIRAS
HSDKPANSKV GLHVDFAPTI LTLAGAGDQV GDKALDGTPL GLYANDDGNL LADYPRPANH
RNQFQGEFWG GWSDEVLHHI PRYTNNSWKA VRVYDEDNQQ AWKLIVSCTN ERELYDLKTD
PGELCNIYNK TRAAVRTRLE ALLAVLVVCK GESCTNPWKI LHPEGSVNSW NQSLDRKYDK
YYANVAPFQY RTCLPYQDHN NEVSAFRSTV AAAAAAAAAA AAQQPGRRRM YTWTSAGRQL
SATASAIATS PQPRSEPFVA EVERHSVPVP AEVLQSDVAK WFDNPLALA
