Unfortunately due to lack of commercial feasibility, the SkyBLAST service has been suspended from December 1st, 2025.
All subscriptions for paid accounts have been paused. For further information or enquiries, please email [email protected]

MULTISPECIES: aldehyde dehydrogenase family protein [Klebsiella].


LOCUS       WP_004151587             499 aa            linear   BCT 26-FEB-2025
ACCESSION   WP_004151587
VERSION     WP_004151587.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Steinmetz,C.G., Xie,P., Weiner,H. and Hurley,T.D.
  TITLE     Structure of mitochondrial aldehyde dehydrogenase: the genetic
            component of ethanol aversion
  JOURNAL   Structure 5 (5), 701-711 (1997)
   PUBMED   9195888
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 :: NF012398.6
            Evidence Source    :: EMBL-EBI
            Source Identifier  :: PF00171.27
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..499
                     /product="aldehyde dehydrogenase family protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=53448
     Region          21..499
                     /region_name="ALDH-SF"
                     /note="NAD(P)+-dependent aldehyde dehydrogenase
                     superfamily; cl11961"
                     /db_xref="CDD:448367"
     Site            order(170..174,182,197,199..200,248..251,254,257..258,
                     272..274,306,403,405,431,469)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:143431"
     Site            order(174,272,303,306)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143431"
ORIGIN      
        1 mstsqialla svqqflyrqh glyidgapca aqsenrltvw dpatgqaiat tadaspadvd
       61 ravmsawraf vdrrwagrtp adrerillrf adlveqhgee laqletleqg ksiaisrafe
      121 vgctlnwmry taglttkisg rtldvsipfp qgaryqawtk kepvgvvagi vpwnfplmig
      181 mwkvmpalaa gcsivikpse ttpltllrva elatqagipd gvfnvvtgsg agcgaaltah
      241 pqvakvsftg statgkqiar vaadrltrvt lelggknpai vlkdadpqwv ieglmtgsfl
      301 nqgqvcaass riyieaplfd tlvsgfeqav kslqvgpgmq etaqinpvvs rahcdkvaay
      361 leearqqkae lisgsagpda ggyyipptlv vnpdaglrls reevfgpvvn lvrvadgeea
      421 lrlandsdfg ltasvwtrdl tqalnytdrl qagtvwvnsh tlidanlpfg gmkqsgtgrd
      481 fgpdwldgwc etksvcvry