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LOCUS WP_000646113 412 aa linear BCT 01-JAN-2025 ACCESSION WP_000646113 VERSION WP_000646113.1 KEYWORDS RefSeq. SOURCE Salmonella ORGANISM Salmonella Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae. REFERENCE 1 (residues 1 to 412) 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 412) 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 412) 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 412) 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 412) 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..412 /organism="Salmonella" /db_xref="taxon:590" Protein 1..412 /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=44445 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 hvkvenvpdp gieqpddiil rvtataicgs dlhlyrgkip qvkhgdifgh 61 efmgevvetg hdvknirkgd rvvipfviac gdcffcrlqq ysacentndg hgaamnkkqi 121 pppaalfgys hlyggvpggq aeyvrvpkgn vgpfkvppll sddkalflsd ilptawqaak 181 naqiqqgfsv avfgagpvgl ltiacarllg aeqifvvdhh awrlrfaeer ygaipinfdd 241 endpaekiie qtaghrgvda vidavgfeak gsltetvltn lklegssgka lrqciaavrr 301 ggvvsvpgvy agfihgflfg dafdkgltfk mgqthvhawl gellpliekg llkpeeivth 361 ympfeeaarg yeifekreee crkvilvpga tsaqaaqkqa tgvvnpmpgg vv