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LOCUS WP_000189187 240 aa linear BCT 10-JUL-2019 ACCESSION WP_000189187 VERSION WP_000189187.1 KEYWORDS RefSeq. SOURCE Escherichia coli ORGANISM Escherichia coli Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. REFERENCE 1 (residues 1 to 240) AUTHORS Shanmugam,D., Esak,S.B. and Narayanaswamy,A. TITLE Molecular Characterisation of nfsA Gene in Nitrofurantoin Resistant Uropathogens JOURNAL J Clin Diagn Res 10 (6), DC05-DC09 (2016) PUBMED 27504284 REFERENCE 2 (residues 1 to 240) AUTHORS Nokhbeh,M.R., Boroumandi,S., Pokorny,N., Koziarz,P., Paterson,E.S. and Lambert,I.B. TITLE Identification and characterization of SnrA, an inducible oxygen-insensitive nitroreductase in Salmonella enterica serovar Typhimurium TA1535 JOURNAL Mutat. Res. 508 (1-2), 59-70 (2002) PUBMED 12379462 REFERENCE 3 (residues 1 to 240) AUTHORS Zenno,S., Koike,H., Kumar,A.N., Jayaraman,R., Tanokura,M. and Saigo,K. TITLE Biochemical characterization of NfsA, the Escherichia coli major nitroreductase exhibiting a high amino acid sequence homology to Frp, a Vibrio harveyi flavin oxidoreductase JOURNAL J. Bacteriol. 178 (15), 4508-4514 (1996) PUBMED 8755878 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 :: BlastRule Evidence Accession :: NBR006554 Evidence Source :: NCBI ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..240 /organism="Escherichia coli" /db_xref="taxon:562" gene 1..240 /gene="nfsA" Protein 1..240 /product="nitroreductase NfsA" /EC_number="1.5.1.38" /calculated_mol_wt=26720 Region 1..240 /region_name="PRK10765" /note="oxygen-insensitive NADPH nitroreductase" /db_xref="CDD:182710" Site order(4..5,7..9,11,29,31..33,35..38,41..44,46..53,56,82, 101..103,105..106,109..110,113..114,117,121..122,128,133, 143..144,146,153,167..170,172,174..177,192,212..213,216, 220..225) /site_type="other" /note="homodimer interface [polypeptide binding]" /db_xref="CDD:380322" Site order(11..13,15,38..40,42,67,69,106..107,110,127..131,167, 169) /site_type="other" /note="FMN binding site [chemical binding]" /db_xref="CDD:380322" Site order(15,42,133..134,165,167,199..200,203) /site_type="other" /note="NADP binding site [chemical binding]" /db_xref="CDD:380322" ORIGIN 1 mtptieltcg hrsirhftde piseaqreai insaratsss sflqcssiir itdkalreel 61 vtltggqkhv aqaaefwvfc adfnrhlqic pdaqlglaeq lllgvvdtam maqnaltaae 121 slglggvyig glrnnieavt kllklpqhvl plfglclgwp adnpdlkprl pssilvhens 181 yqpldkdala qydeqlaeyy ltrgsnnrrd twsdhirrti ikesrpfild ylhkqgwatr