ID Q2U9R3_ASPOR Unreviewed; 586 AA.
AC Q2U9R3;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 24-JAN-2024, entry version 82.
DE RecName: Full=Arylsulfatase {ECO:0000256|PIRNR:PIRNR000972};
DE Short=AS {ECO:0000256|PIRNR:PIRNR000972};
DE EC=3.1.6.1 {ECO:0000256|PIRNR:PIRNR000972};
DE AltName: Full=Aryl-sulfate sulphohydrolase {ECO:0000256|PIRNR:PIRNR000972};
GN ORFNames=AO090166000050 {ECO:0000313|EMBL:BAE61702.1};
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE61702.1, ECO:0000313|Proteomes:UP000006564};
RN [1] {ECO:0000313|EMBL:BAE61702.1, ECO:0000313|Proteomes:UP000006564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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 Evidence={ECO:0000256|PIRNR:PIRNR000972};
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:0000256|PIRSR:PIRSR000972-50}.
CC -!- SIMILARITY: Belongs to the sulfatase family.
CC {ECO:0000256|ARBA:ARBA00008779, ECO:0000256|PIRNR:PIRNR000972}.
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DR EMBL; AP007163; BAE61702.1; -; Genomic_DNA.
DR RefSeq; XP_001822835.1; XM_001822783.1.
DR AlphaFoldDB; Q2U9R3; -.
DR STRING; 510516.Q2U9R3; -.
DR EnsemblFungi; BAE61702; BAE61702; AO090166000050.
DR GeneID; 5994891; -.
DR KEGG; aor:AO090166000050; -.
DR VEuPathDB; FungiDB:AO090166000050; -.
DR HOGENOM; CLU_006332_4_0_1; -.
DR OMA; RCEYAYI; -.
DR OrthoDB; 1365192at2759; -.
DR Proteomes; UP000006564; Chromosome 4.
DR GO; GO:0004065; F:arylsulfatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0018958; P:phenol-containing compound metabolic process; IEA:InterPro.
DR CDD; cd16147; G6S; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR012083; Arylsulfatase.
DR InterPro; IPR024607; Sulfatase_CS.
DR InterPro; IPR000917; Sulfatase_N.
DR PANTHER; PTHR43108; N-ACETYLGLUCOSAMINE-6-SULFATASE FAMILY MEMBER; 1.
DR PANTHER; PTHR43108:SF8; SD21168P; 1.
DR Pfam; PF00884; Sulfatase; 1.
DR PIRSF; PIRSF000972; Arylsulf_plant; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR PROSITE; PS00523; SULFATASE_1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR000972};
KW Reference proteome {ECO:0000313|Proteomes:UP000006564};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..586
FT /note="Arylsulfatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004216957"
FT DOMAIN 41..390
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT MOD_RES 85
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000256|PIRSR:PIRSR000972-50"
SQ SEQUENCE 586 AA; 66383 MW; 32EBDD92D7E30D1F CRC64;
MKFTKKILTT LGLLGVTEAN LGSINTEKHV AQQNAVSKRP PNFLFIMSDD QDLLLDSLSY
TPLTMKHMRD KGTTFNNHFV TTALCCPSRV SLWTGRLAHN TNVTDVHPPW GGYPKFVEGG
FDKNFLPVWL QQAGYDTYYT GKLMNAHSIE NYASPHVSGF NGSDFLLDPY TYDYMNATYQ
RNHDAPVSYL GRHTTEVLTE KAMGFLEDAL SGERPFFMAV SPIAPHSNMN GTYGAGSGPL
WMDEPIPEDR HKHLFPEAKV PRKANFNPKE PTGVSWIHDL PFRNETEVDY NDHYYRQRLR
ALQGVDELVD SLVTRLEQSD KLDNTYIIYT SDNGFHIGQH RLPPGKTCGF EEDIRVPFFI
RGPGIPEGAV EDSVSTHIDL APTFYELAGI PLRDDFDGAP MRILRNNMGT LHEHVTVEYW
GQAMLEGGLS NLGKPTVPNN TYKAVRILSE EYNLYYSVWC NNEHELYDLT NDPYQINNLY
AKVQTDNSQE TRIMGYSLSR VITRLDALLL VLKSCKGTSC IEPWSVLHPG GSVHNLRDAL
NEKYDSFYQA QSKVSFDRCE YAYIIDAEGP QEALAYRNGY SLDAWV
//
