1-propanol dehydrogenase PduQ [Listeria monocytogenes].

LOCUS       WP_010989700             379 aa            linear   BCT 20-MAR-2023
ACCESSION   WP_010989700
VERSION     WP_010989700.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Shanbhag,A.P., Ghatak,A. and Rajagopal,S.
  TITLE     Industrial light at the end of the iron-containing (group III)
            alcohol dehydrogenase tunnel
  JOURNAL   Biotechnol Appl Biochem (2022) In press
   PUBMED   35751426
  REMARK    Publication Status: Available-Online prior to print
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Carpenter,E.P., Hawkins,A.R., Frost,J.W. and Brown,K.A.
  TITLE     Structure of dehydroquinate synthase reveals an active site capable
            of multistep catalysis
  JOURNAL   Nature 394 (6690), 299-302 (1998)
   PUBMED   9685163
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 10169374
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..379
                     /product="1-propanol dehydrogenase PduQ"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0004022 - alcohol dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /GO_process="GO:0051144 - propanediol catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=40750
     Region          5..375
                     /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..92,95,98,120..121,123,142..143,161,169,176,
                     180,245,249,259)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341459"
     Site            order(176,180,245,259)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:341459"
ORIGIN      
        1 mqkvsfktdl yigqgatdrl ldfkdkqifi vtdpfmvssg minaitdkid qsntytifse
       61 iipdppienv vagievlnec danlmiaigg gsaidaakam kffgqklgtv rampfivipt
      121 tsgtgsevts fsvitnkeka ikyplitdai lpdeaildad lvksvppait adtgmdvlth
      181 aleayvstka ndysdamaek viqlvftyle raykdgndle arekmhnasc lagmafnits
      241 lglnhgiaht agakfkiphg rmntlllphv isynagitsd fgnnpdnraa erytaiakll
      301 kmpasntrlg vrslinaikq lqkklnmptt ltecgisrtd lneniaqiae galndgctat
      361 nprtptetdv sailekmla