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MULTISPECIES: 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase


LOCUS       WP_002894357             180 aa            linear   BCT 01-JAN-2025
            [Klebsiella].
ACCESSION   WP_002894357
VERSION     WP_002894357.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Ju,T., Goldsmith,R.B., Chai,S.C., Maroney,M.J., Pochapsky,S.S. and
            Pochapsky,T.C.
  TITLE     One protein, two enzymes revisited: a structural entropy switch
            interconverts the two isoforms of acireductone dioxygenase
  JOURNAL   J Mol Biol 363 (4), 823-834 (2006)
   PUBMED   16989860
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 180)
  AUTHORS   Dai,Y., Wensink,P.C. and Abeles,R.H.
  TITLE     One protein, two enzymes
  JOURNAL   J Biol Chem 274 (3), 1193-1195 (1999)
   PUBMED   9880484
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 10004526
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..180
                     /product="1,2-dihydroxy-3-keto-5-methylthiopentene
                     dioxygenase"
                     /EC_number="1.13.11.53"
                     /EC_number="1.13.11.54"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0010308 - acireductone dioxygenase
                     (Ni2+-requiring) activity [Evidence IEA]"
                     /GO_function="GO:0010309 - acireductone dioxygenase
                     [iron(II)-requiring] activity [Evidence IEA]"
                     /GO_function="GO:0016151 - nickel cation binding [Evidence
                     IEA]"
                     /GO_process="GO:0019509 - L-methionine salvage from
                     methylthioadenosine [Evidence IEA]"
                     /calculated_mol_wt=20138
     Region          1..180
                     /region_name="Adi1"
                     /note="Acireductone dioxygenase (methionine salvage),
                     cupin superfamily [Amino acid transport and metabolism];
                     COG1791"
                     /db_xref="CDD:441396"
ORIGIN      
        1 msaltlfsvt dpqtpvwhst dakaiqdqln akgvrferwq adrdlganps petviaayqh
       61 aidklvaekg yqswdvislr adnpqkealr ekflnehthg edevrffveg aglfclhigd
      121 evfqvlcekn dlisvpahtp hwfdmgsepn ftairifdnp egwiaqftgd diasayprla