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LOCUS WP_000828465 497 aa linear BCT 26-FEB-2025 ACCESSION WP_000828465 VERSION WP_000828465.1 KEYWORDS RefSeq. SOURCE Escherichia coli ORGANISM Escherichia coli Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. REFERENCE 1 (residues 1 to 497) AUTHORS Lukatela,G., Krauss,N., Theis,K., Selmer,T., Gieselmann,V., von Figura,K. and Saenger,W. TITLE Crystal structure of human arylsulfatase A: the aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis JOURNAL Biochemistry 37 (11), 3654-3664 (1998) PUBMED 9521684 COMMENT REFSEQ: This record represents a single, non-redundant, protein sequence which may be annotated on many different RefSeq genomes from the same, or different, species. ##Evidence-For-Name-Assignment-START## Evidence Category :: HMM Evidence Accession :: NF013080.6 Evidence Source :: EMBL-EBI Source Identifier :: PF00884.28 ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..497 /organism="Escherichia coli" /db_xref="taxon:562" Protein 1..497 /product="sulfatase-like hydrolase/transferase" /GO_function="GO:0008484 - sulfuric ester hydrolase activity [Evidence IEA]" /calculated_mol_wt=57126 Region 4..469 /region_name="sulfatase_like" /note="uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; cd16156" /db_xref="CDD:293775" Site order(12..13,52,100,102,194,284..285) /site_type="active" /note="putative active site [active]" /db_xref="CDD:293775" Site order(12..13,52,100,102,194,285) /site_type="other" /note="putative substrate binding site [chemical binding]" /db_xref="CDD:293775" ORIGIN 1 mkrpnflfim tdtqapnmvg cysgkplntq nidslaaegi rfnsaytcsp vctparaglf 61 tgiyanqsgp wtnnvapgkn istmgryfkd agyhtcyigk whldghdyfg tgecppewda 121 dywfdganyl seltekeisl wrnglnsved lqanhidetf twahrisnra vdflqqpara 181 eepflmvvsy dephhpftcp veylekyadf yyelgekaqd dlankpehhr lwaqampspv 241 gddglyhhpl yfacndfvdd qigrvinalk peqrentwvi ytsdhgemmg ahkliskgaa 301 mydditripl iirspqgerr qvdtpvshid llptmmalad iekpeilpge nilavkeprg 361 vmvefnryei ehdsfggfip vrcwvtddfk lvlnlftsde lydrrndpne mhnliddahf 421 advrskmhda lldymdkird pfrsyqwslr pwrkdaqprw mgafrprpqd gyspvvrdyd 481 tglptqgvkv eekkqkf