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LOCUS WP_003092055 483 aa linear BCT 18-FEB-2025 [Pseudomonas]. ACCESSION WP_003092055 VERSION WP_003092055.1 KEYWORDS RefSeq. SOURCE Pseudomonas ORGANISM Pseudomonas Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae. REFERENCE 1 (residues 1 to 483) AUTHORS Yang,J., Wang,Y., Woolridge,E.M., Arora,V., Petsko,G.A., Kozarich,J.W. and Ringe,D. TITLE Crystal structure of 3-carboxy-cis,cis-muconate lactonizing enzyme from Pseudomonas putida, a fumarase class II type cycloisomerase: enzyme evolution in parallel pathways JOURNAL Biochemistry 43 (32), 10424-10434 (2004) PUBMED 15301541 REFERENCE 2 (residues 1 to 483) AUTHORS Fujii,T., Sakai,H., Kawata,Y. and Hata,Y. TITLE Crystal structure of thermostable aspartase from Bacillus sp. YM55-1: structure-based exploration of functional sites in the aspartase family JOURNAL J Mol Biol 328 (3), 635-654 (2003) PUBMED 12706722 REFERENCE 3 (residues 1 to 483) AUTHORS Williams,S.E., Woolridge,E.M., Ransom,S.C., Landro,J.A., Babbitt,P.C. and Kozarich,J.W. TITLE 3-Carboxy-cis,cis-muconate lactonizing enzyme from Pseudomonas putida is homologous to the class II fumarase family: a new reaction in the evolution of a mechanistic motif JOURNAL Biochemistry 31 (40), 9768-9776 (1992) PUBMED 1390752 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 :: Conserved Domain (CDD) Evidence Accession :: Domain architecture ID 10107773 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..483 /organism="Pseudomonas" /db_xref="taxon:286" Protein 1..483 /product="class-II fumarase/aspartase family protein" /calculated_mol_wt=52797 Region 42..478 /region_name="pCLME" /note="prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; cd01597" /db_xref="CDD:176469" Site order(56..58,61..62,105,108..109,132..133,185..187, 189..190,192..193,199,201,206,209,212..213,216,230..232, 235,240..241,256..257,262..263,265..266,268..269,272, 275..276,283,286..287,292..293,295,317..318,323,330..331, 336,340,345..349,355..356,358,360,399,466..467,471,474) /site_type="other" /note="tetramer interface [polypeptide binding]" /db_xref="CDD:176469" Site order(113..114,139..141,186..187,229,315..316,318,349) /site_type="active" /db_xref="CDD:176469" ORIGIN 1 mdaeslemla rssctahpqs fggapaessc khehshivds kthgggyagp vsrrifcshc 61 rlqrwldvea alalaqadvg vippeaalei akaarlsavd lqqiadgvas tghslmpllg 121 alqrncspsa reyvhfgatt qdiqdtaqsl emrdvldete raldilldrl svlasgtrna 181 lmvarthsip alpttfglkv agwidellrh rerlgearkr ilvvqlfggv gtmaafgdea 241 mlllesfarr lsldvplagw hvsrdrvtef vstlamvtas lariadeirt lnrweigele 301 vgwtqqqigs stmphkrnpe gceqvvvlar lakaqvllal damileherd yrgtrlewca 361 vadvshyalm alslltdtid gltvhdetma rtanaysdai cteafvfema kqlgkssaye 421 iifeitqacq rkripmrqal esdprvgavm pketlarlfe prthlgmagt ivdkvldkva 481 shh