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: S-(hydroxymethyl)glutathione dehydrogenase/class III


LOCUS       WP_004189749             372 aa            linear   BCT 06-NOV-2024
            alcohol dehydrogenase [Klebsiella].
ACCESSION   WP_004189749
VERSION     WP_004189749.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
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 :: TIGR02818.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..372
                     /product="S-(hydroxymethyl)glutathione dehydrogenase/class
                     III alcohol dehydrogenase"
                     /GO_function="GO:0004022 - alcohol dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051903 - S-(hydroxymethyl)glutathione
                     dehydrogenase [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=39153
     Region          1..368
                     /region_name="alcohol_DH_class_III"
                     /note="class III alcohol dehydrogenases; cd08300"
                     /db_xref="CDD:176260"
     Site            order(40,42,51..53,62,88..89,169,289,313)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:176260"
     Site            order(40,62..63,169)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176260"
     Site            order(41..42,169,173,194..198,218..219,223,263..264,
                     268..269,287..288,312..314,364)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:176260"
     Site            order(92,95,98,106)
                     /site_type="other"
                     /note="structural Zn binding site [ion binding]"
                     /db_xref="CDD:176260"
     Site            order(96..97,100,102..103,105,107,254,259,270..271,
                     278..281,290,293..300,303..305,308..313)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176260"
ORIGIN      
        1 mksraavafg pgqplkivei dvappkkgev lvkithtgvc htdaftlsgd dpegvfpavl
       61 ghegggivve vgegvtslkp gdhviplyta ecgeckfcks gktnlcqavr atqgkglmpd
      121 gttrfsynge piyhymgtst fseytvcaei slakvnpqap ldkvcllgcg vttgigavhn
      181 takvkagdtv avfglggigl aviqgavqaq agrilavdtn pdkftlakem gatdfinpnd
      241 ydkpiqdviv eltdggvdfs fecignvnvm raalecchkg wgesviigva gagqeiktrp
      301 fqlvtgrvwr gsafggvkgr sqlpgmveda magkirldpf ithrlpleqi neafdlmheg
      361 ksirtvihfg dq