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LOCUS WP_010990109 358 aa linear BCT 03-JUN-2024 monocytogenes]. ACCESSION WP_010990109 VERSION WP_010990109.1 KEYWORDS RefSeq. SOURCE Listeria monocytogenes ORGANISM Listeria monocytogenes Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria. REFERENCE 1 (residues 1 to 358) AUTHORS Janczak,M.W. and Poulter,C.D. TITLE Kinetic and Binding Studies of Streptococcus pneumoniae Type 2 Isopentenyl Diphosphate:Dimethylallyl Diphosphate Isomerase JOURNAL Biochemistry 55 (15), 2260-2268 (2016) PUBMED 27003727 REFERENCE 2 (residues 1 to 358) AUTHORS Dutoit,R., de Ruyck,J., Durisotti,V., Legrain,C., Jacobs,E. and Wouters,J. TITLE Overexpression, physicochemical characterization, and modeling of a hyperthermophilic pyrococcus furiosus type 2 IPP isomerase JOURNAL Proteins 71 (4), 1699-1707 (2008) PUBMED 18076031 REFERENCE 3 (residues 1 to 358) AUTHORS Takagi,M., Kaneda,K., Shimizu,T., Hayakawa,Y., Seto,H. and Kuzuyama,T. TITLE Bacillus subtilis ypgA gene is fni, a nonessential gene encoding type 2 isopentenyl diphosphate isomerase JOURNAL Biosci Biotechnol Biochem 68 (1), 132-137 (2004) PUBMED 14745175 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 :: TIGR02151.1 Evidence Source :: JCVI ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..358 /organism="Listeria monocytogenes" /db_xref="taxon:1639" gene 1..358 /gene="fni" Protein 1..358 /product="type 2 isopentenyl-diphosphate Delta-isomerase" /EC_number="5.3.3.2" /GO_function="GO:0004452 - isopentenyl-diphosphate delta-isomerase activity [Evidence IEA]" /GO_function="GO:0010181 - FMN binding [Evidence IEA]" /GO_process="GO:0008299 - isoprenoid biosynthetic process [Evidence IEA]" /calculated_mol_wt=39359 Region 11..338 /region_name="IPP_isom_2" /note="isopentenyl-diphosphate delta-isomerase, type 2; TIGR02151" /db_xref="CDD:273999" Site order(38..41,44,154,191,194..195,199,243,251,272..273,309, 312) /site_type="other" /note="homotetramer interface [polypeptide binding]" /db_xref="CDD:239205" Site order(70..73,99,128,153,190,265..267,289) /site_type="other" /note="FMN binding site [chemical binding]" /db_xref="CDD:239205" Site order(72,79..80) /site_type="other" /note="homodimer contacts [polypeptide binding]" /db_xref="CDD:239205" Site order(99,128,153,190,265,288..289) /site_type="active" /note="putative active site [active]" /db_xref="CDD:239205" Site order(128,130,153) /site_type="other" /note="putative substrate binding site [chemical binding]" /db_xref="CDD:239205" ORIGIN 1 mqknddllre rrkdehvalg vkqneqlaps slkdiqligt siprynvkdi dltttifgkn 61 vpfpfyinam tggsrhtkki naelaeiare vaipmavgsq saalknssli dtynivrein 121 pngmilanvs pevaiqdglq aiemleanal qihinpaqel vmqegdrsfs hwltrieeyv 181 klspvpivvk evgfgmtret vktladigvq tvdlagkggt nfaqiendrr rdqaydflld 241 wgistgqali dmqhqdapki aylasggirn pldiikalal gadsvgmagq iiyslkkegv 301 tktieklelw keqlrglfvl anakniaelk ttplivsgel akwgtlrein lvklanrk