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: 1-propanol dehydrogenase PduQ [Klebsiella].


LOCUS       WP_004151973             370 aa            linear   BCT 13-MAY-2021
ACCESSION   WP_004151973
VERSION     WP_004151973.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Cheng,S., Fan,C., Sinha,S. and Bobik,T.A.
  TITLE     The PduQ enzyme is an alcohol dehydrogenase used to recycle NAD+
            internally within the Pdu microcompartment of Salmonella enterica
  JOURNAL   PLoS ONE 7 (10), e47144 (2012)
   PUBMED   23077559
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  :: BlastRule
            Evidence Accession :: NBR006391
            Evidence Source    :: NCBI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     gene            1..370
                     /gene="pduQ"
     Protein         1..370
                     /product="1-propanol dehydrogenase PduQ"
                     /calculated_mol_wt=39180
     Region          4..367
                     /region_name="PDD"
                     /note="1,3-propanediol dehydrogenase (PPD) catalyzes the
                     reduction of 3-hydroxypropionaldehyde (3-HPA) to
                     1,3-propanediol in glycerol metabolism; cd08180"
                     /db_xref="CDD:341459"
     Site            order(33,90..92,95,98,119..120,122,141..142,160,168,175,
                     179,244,248,258)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341459"
     Site            order(175,179,244,258)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:341459"
ORIGIN      
        1 mhtfslqtrl ysgpgslaal qrfshqhiwi vcdgflarsp lldrlraalp asnrvsvfsd
       61 itpdptihtv akgiaqmqal rpqvvigfgg gsamdaakai vwfsqqgglp vdtcvaiptt
      121 sgtgsevtsa cvisdpekgi kyplfhealc pdmaiidptl vvsvpptita htgldaltha
      181 leawvspqat dftdalaeka vrlvfralpv airqgdciat rskmhnastl agmafsqagl
      241 glnhaiahql ggqfhlphgl anallltavi rfnagepraa kryarlarac rfcppeageq
      301 eafqalltav etlkqqcaip tlkgalqeky plflsripam vpaaladatl rtnprpvdga
      361 aiaqlleslq