(data stored in ACNUC8465 zone)

SWISSPROT: B6H6V0_PENRW

ID   B6H6V0_PENRW            Unreviewed;       623 AA.
AC   B6H6V0;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   08-MAY-2019, entry version 55.
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=Pc16g00510 {ECO:0000313|EMBL:CAP92721.1}, PCH_Pc16g00510
GN   {ECO:0000313|EMBL:CAP92721.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP92721.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP92721.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a phenyl 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;
CC         EC=3.1.6.1; Evidence={ECO:0000256|PIRNR:PIRNR000972};
CC   -!- PTM: The conversion to 3-oxoalanine (also known as C-
CC       formylglycine, FGly), of a serine or cysteine residue in
CC       prokaryotes and of a cysteine residue in eukaryotes, is critical
CC       for catalytic activity. {ECO:0000256|PIRSR:PIRSR000972-50}.
CC   -!- SIMILARITY: Belongs to the sulfatase family.
CC       {ECO:0000256|PIRNR:PIRNR000972}.
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DR   EMBL; AM920431; CAP92721.1; -; Genomic_DNA.
DR   RefSeq; XP_002560473.1; XM_002560427.1.
DR   EnsemblFungi; CAP92721; CAP92721; PCH_Pc16g00510.
DR   GeneID; 8317629; -.
DR   KEGG; pcs:Pc16g00510; -.
DR   eggNOG; KOG3731; Eukaryota.
DR   eggNOG; COG3119; LUCA.
DR   HOGENOM; HOG000169239; -.
DR   OMA; HVPPGWS; -.
DR   OrthoDB; 1273622at2759; -.
DR   BioCyc; PCHR:PC16G00510-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c16.
DR   GO; GO:0004065; F:arylsulfatase activity; IEA:UniProtKB-UniRule.
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.
PE   3: Inferred from homology;
DR   PRODOM; B6H6V0.
DR   SWISS-2DPAGE; B6H6V0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR000972};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724}.
FT   DOMAIN       82    430       Sulfatase. {ECO:0000259|Pfam:PF00884}.
FT   MOD_RES     126    126       3-oxoalanine (Cys). {ECO:0000256|PIRSR:
FT                                PIRSR000972-50}.
SQ   SEQUENCE   623 AA;  69901 MW;  123B4AA43572A363 CRC64;
     MDGIIRSTFP LSTLDLYNYA LGSAREYVVI DSYLHPSPLH LMKLNTALVG LIAEGVIALN
     LQSMQSALQS VLKHSEAEPR KPNILFIITD DQDLQLDSIS YTPLITKHIR DQGTFFRNHF
     VTTALCCPSR VSLWTGRQAH NTNVTDVHPP YGGYPKFVER GFNDDFLPLW LQGAGYDTYY
     TGKMFNAHTV DNYHSPHING FNASDFLLDP YTYSYRNSTY QRNHEPPVSH EGEHTIDVIT
     GKALGFLDDA LAGERPFFLA VSPVAPHSNV DPGNITSENF YMSAPIPLER HEHLFQDVRI
     PRTANFNSDQ PSGVSWVHDL PLQNQSVVDY HDHFYRSRLR ALQGVDELVD GLVTRLEESG
     QLDNTYIIYT SDNGFHIGQH RLPPGKTCGF EEDIRVPLFI RGPGVTKGYV QDAVTTHVDL
     APTLFHLAGI PARDDFDGTA IPVTPEFEGE RHEHVTVEYW GSAVVEGPGG STMIPNNTYK
     SVRLLGEGYN LYYSVWCNNE HELYDLSTDP YQLNNLYPTT SHAGINETRI LGRSLNQAIN
     RLDALLMVLK SCQGVTCIQP WDVLQPVDPV STLQHALNKE YDGFYGAQPQ VSFDWCDSGY
     IVEAEGAQVP LTSRHGVSWD VWV
//

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