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LOCUS WP_000152563 339 aa linear BCT 13-JAN-2025 ACCESSION WP_000152563 VERSION WP_000152563.1 KEYWORDS RefSeq. SOURCE Salmonella ORGANISM Salmonella Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae. REFERENCE 1 (residues 1 to 339) AUTHORS Pick,A., Ruhmann,B., Schmid,J. and Sieber,V. TITLE Novel CAD-like enzymes from Escherichia coli K-12 as additional tools in chemical production JOURNAL Appl Microbiol Biotechnol 97 (13), 5815-5824 (2013) PUBMED 23093176 REFERENCE 2 (residues 1 to 339) AUTHORS Akhtar,M.K., Turner,N.J. and Jones,P.R. TITLE Carboxylic acid reductase is a versatile enzyme for the conversion of fatty acids into fuels and chemical commodities JOURNAL Proc Natl Acad Sci U S A 110 (1), 87-92 (2013) PUBMED 23248280 REFERENCE 3 (residues 1 to 339) AUTHORS Rodriguez,G.M. and Atsumi,S. TITLE Isobutyraldehyde production from Escherichia coli by removing aldehyde reductase activity JOURNAL Microb Cell Fact 11, 90 (2012) PUBMED 22731523 REMARK Publication Status: Online-Only 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 :: NF047908.1 Evidence Source :: NCBIFAM ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..339 /organism="Salmonella" /db_xref="taxon:590" gene 1..339 /gene="ahr" /GO_function="GO:0016491 - oxidoreductase activity [Evidence IEA]" Protein 1..339 /product="NADPH-dependent aldehyde reductase Ahr" /EC_number="1.1.1.2" /GO_function="GO:0008106 - alcohol dehydrogenase (NADP+) activity [Evidence IEA]" /GO_function="GO:0016616 - oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [Evidence IEA]" /GO_process="GO:0006631 - fatty acid metabolic process [Evidence IEA]" /calculated_mol_wt=36239 Region 5..336 /region_name="CAD1" /note="Cinnamyl alcohol dehydrogenases (CAD); cd05283" /db_xref="CDD:176186" Site order(41..43,46,152,156,176..181,199..200,204,219, 238..239,241,261..262,285..287) /site_type="other" /note="putative NAD(P) binding site [chemical binding]" /db_xref="CDD:176186" Site order(41,43,63,91,152,287) /site_type="other" /note="putative substrate binding site [chemical binding]" /db_xref="CDD:176186" Site order(41,63,152) /site_type="other" /note="catalytic Zn binding site [ion binding]" /db_xref="CDD:176186" Site order(96,99,102,110) /site_type="other" /note="structural Zn binding site [ion binding]" /db_xref="CDD:176186" Site order(109,159,163,255,260..262,264,273,275..276,279..286) /site_type="other" /note="dimer interface [polypeptide binding]" /db_xref="CDD:176186" ORIGIN 1 mtiiksyaak eaggelelye ydagelqped vevrvdycgi chsdlsmidn ewgfsqyplv 61 aghevigrva algsaaqdkg lkvgqrvgig wtarscghcd acisgnqinc qegavptiln 121 rggfaeklra gwqwviplpe nidmasagpl lcggitvfkp llmhhitats rvgvigiggl 181 ghiaikllha mgcevtafss npskeqevla mgannvvnsr dpealkalag qfdliintvn 241 vdldwqpyfe altyggnfht vgavlkplpv paftliagdr sisgsatgtp yelrklmkfa 301 grskvaptte lfamsqinea iqhvrdgkar yrvvlkadf