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]

zinc-dependent alcohol dehydrogenase [Escherichia coli].


LOCUS       WP_000737329             350 aa            linear   BCT 24-DEC-2024
ACCESSION   WP_000737329
VERSION     WP_000737329.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 350)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 350)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
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 10169599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..350
                     /product="zinc-dependent alcohol dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=38100
     Region          79..350
                     /region_name="2-desacetyl-2-
                     hydroxyethyl_bacteriochlorophyllide_"
                     /note="2-desacetyl-2-hydroxyethyl bacteriochlorophyllide
                     and other MDR family members; cd08255"
                     /db_xref="CDD:176217"
     Site            order(141,145,165..170,189..190,194,212,233..234,236,
                     256..257,283..285)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176217"
ORIGIN      
        1 mkklvatapr vaalveyedr ailanevkir vrfgapkhgt evvdfraasp fidedfngew
       61 qmftprpada prgiefgkfq lgnmvvgdii ecgsdvtdya vgdsvcgygp lsetiiinav
      121 nnyklrkmpe gsswknavcy dpaqfamsgv rdanvrvgdf vvvvglgaig qiaiqlakra
      181 gasvvigvdp iahrcdiarr hgadfclnpi gtdvgkeikt ltgkqgadvi ietsgyadal
      241 qsalrglayg gtisyvafak pfaegfnlgr eahfnnakiv fsracsepnp dyprwsrkri
      301 eetcwkllmn gylncedlid pvvtfanspe symqyvdqhp eqsikmgvtf