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LOCUS WP_004140529 397 aa linear BCT 01-JAN-2025 ACCESSION WP_004140529 VERSION WP_004140529.1 KEYWORDS RefSeq. SOURCE Klebsiella ORGANISM Klebsiella Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group. REFERENCE 1 (residues 1 to 397) 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 397) 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 397) 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 397) 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 397) 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 10169674 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..397 /organism="Klebsiella" /db_xref="taxon:570" Protein 1..397 /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=42608 Region 1..388 /region_name="FDH_like_1" /note="Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; cd08283" /db_xref="CDD:176243" Site order(38..40,43,86,170,174,193..194,196..198,217..219,223, 238,264..266,290,307..309,332..334,374) /site_type="other" /note="NAD binding site [chemical binding]" /db_xref="CDD:176243" Site order(38,40,60,170) /site_type="other" /note="catalytic Zn binding site [ion binding]" /db_xref="CDD:176243" Site order(90..91,93,96,104) /site_type="other" /note="structural Zn binding site [ion binding]" /db_xref="CDD:176243" ORIGIN 1 mkaltyhgph hvsvdtmpdp aleaaddiil rvtataicgs dlhlyrgkip gthhgdifgh 61 efmgevveag sevtavrkgd rvvipfviac gdcffcrlqq yaacestnsg qgatlnrkgi 121 sppaalfgys dlyggipggq aeyvrvpkan tgpfkvpdtl pdekvlflsd ilptawqavk 181 naevkpgssv aifgagpvgl lcascarlng aeqifiidhn dyrldfaqqr ygaipinfdh 241 hddpaqwiid ntpghrgvda vidavgfeak gsltetvlst lkiegssgka lrqciaavrr 301 ggivsvpgvy agfihgfmfg dafdkgltfr mgqthvhawl pdllalieqg lltpeeivth 361 hmpleeaarg yqifekreea crkvilvpgm qpgkatl