bifunctional L-1,2-propanediol dehydrogenase/glycerol dehydrogenase

LOCUS       WP_000374012             367 aa            linear   BCT 20-JAN-2025
            [Escherichia coli].
ACCESSION   WP_000374012
VERSION     WP_000374012.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Gonzalez,R., Murarka,A., Dharmadi,Y. and Yazdani,S.S.
  TITLE     A new model for the anaerobic fermentation of glycerol in enteric
            bacteria: trunk and auxiliary pathways in Escherichia coli
  JOURNAL   Metab Eng 10 (5), 234-245 (2008)
   PUBMED   18632294
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Subedi,K.P., Kim,I., Kim,J., Min,B. and Park,C.
  TITLE     Role of GldA in dihydroxyacetone and methylglyoxal metabolism of
            Escherichia coli K12
  JOURNAL   FEMS Microbiol Lett 279 (2), 180-187 (2008)
   PUBMED   18179582
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Truniger,V. and Boos,W.
  TITLE     Mapping and cloning of gldA, the structural gene of the Escherichia
            coli glycerol dehydrogenase
  JOURNAL   J Bacteriol 176 (6), 1796-1800 (1994)
   PUBMED   8132480
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 :: NF047954.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..367
                     /gene="gldA"
     Protein         1..367
                     /product="bifunctional L-1,2-propanediol
                     dehydrogenase/glycerol dehydrogenase"
                     /EC_number="1.1.1.6"
                     /EC_number="1.1.1.75"
                     /GO_function="GO:0008888 - glycerol dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_function="GO:0019147 - (R)-aminopropanol dehydrogenase
                     activity [Evidence IEA]"
                     /GO_process="GO:0019588 - anaerobic glycerol catabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0051596 - methylglyoxal catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38597
     Region          1..366
                     /region_name="gldA"
                     /note="glycerol dehydrogenase; Provisional; PRK09423"
                     /db_xref="CDD:181843"
     Site            order(9..11,13..14,205,208,231..232,235)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:341449"
     Site            order(37,93..95,98,101,116..117,119,138..139,156,164,171,
                     175,254,258,271)
                     /site_type="active"
                     /db_xref="CDD:341449"
     Site            order(171,254,271)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:341449"
ORIGIN      
        1 mdriiqspgk yiqgadvinr lgeylkplae rwlvvgdkfv lgfaqstvek sfkdaglvve
       61 iapfggecsq neidrlrgia etaqcgailg igggktldta kalahfmgvp vaiaptiast
      121 dapcsalsvi ytdegefdry lllpnnpnmv ivdtkivaga parllaagig dalatwfear
      181 acsrsgattm aggkctqaal alaelcyntl leegekamla aeqhvvtpal ervieantyl
      241 sgvgfesggl aaahavhngl taipdahhyy hgekvafgtl tqlvlenspv eeietvaals
      301 havglpitla qldikedvpa kmrivaeaac aegetihnmp ggatpdqvya allvadqygq
      361 rflqewe