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Database: UniProt
Entry: K6Y8Y2_9ALTE
LinkDB: K6Y8Y2_9ALTE
Original site: K6Y8Y2_9ALTE 
ID   K6Y8Y2_9ALTE            Unreviewed;       799 AA.
AC   K6Y8Y2;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Arylsulfatase {ECO:0000313|EMBL:GAC13118.1};
DE            EC=3.1.6.1 {ECO:0000313|EMBL:GAC13118.1};
GN   Name=aslA {ECO:0000313|EMBL:GAC13118.1};
GN   ORFNames=GLIP_0472 {ECO:0000313|EMBL:GAC13118.1};
OS   Aliiglaciecola lipolytica E3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Aliiglaciecola.
OX   NCBI_TaxID=1127673 {ECO:0000313|EMBL:GAC13118.1, ECO:0000313|Proteomes:UP000006334};
RN   [1] {ECO:0000313|EMBL:GAC13118.1, ECO:0000313|Proteomes:UP000006334}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E3 {ECO:0000313|EMBL:GAC13118.1,
RC   ECO:0000313|Proteomes:UP000006334};
RX   PubMed=25009843;
RA   Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA   Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT   "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT   high degree of genomic diversity and genomic characteristic for cold
RT   adaptation.";
RL   Environ. Microbiol. 16:1642-1653(2014).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC       {ECO:0000256|ARBA:ARBA00009865}.
CC   -!- SIMILARITY: Belongs to the sulfatase family.
CC       {ECO:0000256|ARBA:ARBA00008779}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAC13118.1}.
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DR   EMBL; BAEN01000014; GAC13118.1; -; Genomic_DNA.
DR   RefSeq; WP_008842938.1; NZ_BAEN01000014.1.
DR   AlphaFoldDB; K6Y8Y2; -.
DR   STRING; 1127673.GLIP_0472; -.
DR   eggNOG; COG1621; Bacteria.
DR   eggNOG; COG3119; Bacteria.
DR   OrthoDB; 9803751at2; -.
DR   Proteomes; UP000006334; Unassembled WGS sequence.
DR   GO; GO:0004065; F:arylsulfatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd16144; ARS_like; 1.
DR   Gene3D; 3.30.1120.10; -; 1.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   InterPro; IPR024607; Sulfatase_CS.
DR   InterPro; IPR000917; Sulfatase_N.
DR   PANTHER; PTHR42693:SF33; ARYLSULFATASE; 1.
DR   PANTHER; PTHR42693; ARYLSULFATASE FAMILY MEMBER; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   Pfam; PF00884; Sulfatase; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS00523; SULFATASE_1; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:GAC13118.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006334};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..799
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003897226"
FT   DOMAIN          31..379
FT                   /note="Sulfatase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00884"
FT   SITE            649
FT                   /note="Important for catalytic activity, responsible for
FT                   pKa modulation of the active site Glu and correct
FT                   orientation of both the proton donor and substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ   SEQUENCE   799 AA;  88766 MW;  0356662BA9B36AD6 CRC64;
     MKVLSIVAVM VLSICMLSAC NSTNSDKKKL NVLLILVDDL GWADVAAFNP NTNYSTPNMD
     KLANQGLLFT DGYAASPVCS PTRASLLTGQ HPTRLSTTDF FRDQSRKHRY REGKFKPAQF
     EEQLPTNIST IASVLGDDGY QTAFLGKWHL GQTEDGWPEH FGFDVNIGGH VAGAPRGGYF
     SPYNNPRLES GPDGEYLTER LTSEAINLLE GYAQGESPFF MMMSYYSVHT PLDAPKETID
     KYASKFAGTD PESEFVQVEQ IWPTDKPRLN RVKQTHATYA AMVEKVDENI GRLVDSLKAQ
     NLAEDTIVIL LSDNGGLSTA EGLPTSNLPL RGGKGWLYEG GIRVPFVISV PGSKSMGTST
     SVPATSTDIA ATLYDILGIN DNNIKQLDGD SLKAVINGES NVAERPLYFH YPHYSNQGGF
     PGAAIRLGDW KLLERFEDGK VQLFNLAQDR EESNDLALEY PQRVAKMKEM LHRWYEDQDA
     KFLRPNPTLP EYGQPWKPAQ DASQKIVISH SDLNGIGIEE NVMRRDPSDI IKVGDLYYVW
     YSKGKVSTGY DATVWYATSE DGRHWTEKGE ALGKGTKGSW EGASVFTPNI LVAEGKYWLF
     YTGTSKTYKQ PFSPDSKIGI VVSDSPDGPW QRFSNAPVLV NSENKDDFDS HLVDDSSLII
     RDGKYWLYYK GRQLGKSPKH TQMGLAIAEN PEGPYIKVPN NPVIPGNHEV FVWPQGTGVA
     AMIGERAPEE IQDSIMYAED GMNFIKTHEV INHPWAAGAY RPEAFTDSDL GEMPLWGVEI
     GRAKKALPFI HRFDVTKEN
//
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