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LOCUS WP_003088939 415 aa linear BCT 31-DEC-2024 ACCESSION WP_003088939 VERSION WP_003088939.1 KEYWORDS RefSeq. SOURCE Pseudomonas ORGANISM Pseudomonas Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae. REFERENCE 1 (residues 1 to 415) 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 415) 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 415) 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 415) 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 415) 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..415 /organism="Pseudomonas" /db_xref="taxon:286" Protein 1..415 /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=44165 Region 1..383 /region_name="FDH_like_1" /note="Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; cd08283" /db_xref="CDD:176243" Site order(38..40,43,86,162,166,185..186,188..190,209..211,215, 229,253..255,285,302..304,327..329,369) /site_type="other" /note="NAD binding site [chemical binding]" /db_xref="CDD:176243" Site order(38,40,60,162) /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 mkavvfhdig dirledvaep rlqeptdaiv rltasaicgt dlhfvrgsvg gmrpgtilgh 61 egvgivealg devrnlqvgd rvvipstiac gncvycragy yaqcdvanpg gsqagtaffg 121 gpranggfhg lqaekaripy aniglirlps sisddqaill sdifptgyfg aelagiapgn 181 tvavfgcgpv gqfaiasall lgaarvfaid rhpdrlhmar qqgaevidfe redpvqalrw 241 ltagigvdra idavgvdaeh shgtatpapr qegtswspgn apaqalewav qglakagtls 301 iigvyaedsr qfpiglamnr nltirmgnch hrkyipllle hvlsgridpa kiltqvkpig 361 daieafeafd rretgwikve lvpqkrqveg seerlderav delarrptpe sgarg