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LOCUS WP_000967417 353 aa linear BCT 14-JAN-2025 ACCESSION WP_000967417 VERSION WP_000967417.1 KEYWORDS RefSeq. SOURCE Shigella flexneri ORGANISM Shigella flexneri Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Shigella. REFERENCE 1 (residues 1 to 353) 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 353) 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 353) 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..353 /organism="Shigella flexneri" /db_xref="taxon:623" gene 1..353 /gene="ahr" Protein 1..353 /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=37950 Region 19..350 /region_name="CAD1" /note="Cinnamyl alcohol dehydrogenases (CAD); cd05283" /db_xref="CDD:176186" Site order(55..57,60,166,170,190..195,213..214,218,233, 252..253,255,275..276,299..301) /site_type="other" /note="putative NAD(P) binding site [chemical binding]" /db_xref="CDD:176186" Site order(55,57,77,105,166,301) /site_type="other" /note="putative substrate binding site [chemical binding]" /db_xref="CDD:176186" Site order(55,77,166) /site_type="other" /note="catalytic Zn binding site [ion binding]" /db_xref="CDD:176186" Site order(110,113,116,124) /site_type="other" /note="structural Zn binding site [ion binding]" /db_xref="CDD:176186" Site order(123,173,177,269,274..276,278,287,289..290,293..300) /site_type="other" /note="dimer interface [polypeptide binding]" /db_xref="CDD:176186" ORIGIN 1 mlytsqttpe kapkmsmiks yaakeaggel evyeydpgel kpqdvevqvd ycgichsdls 61 midnewgfsq yplvaghevi grvvalgsaa qdkglqvgqr vgigwtarsc ghcdacisgn 121 qinceqgavp timnrggfae klradwqwvi plpenidies agpllcggit vfkpllmhhi 181 tatsrvgvig igglghiaik llhamgcevt afssnpakeq evlamgadkv vnsrdpqalk 241 alsgqfdlii ntvnvsldwq pyfealtygg nfhtvgavlt plsvpaftli agdrsisgsa 301 tgtpyelrkl mrfaarskva pttelfpmsk indaiqhvrd gkaryrvvlk adf