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LOCUS NP_462133 672 aa linear CON 08-SEP-2022 serovar Typhimurium str. LT2]. ACCESSION NP_462133 VERSION NP_462133.1 DBLINK BioProject: PRJNA57799 BioSample: SAMN02604315 DBSOURCE REFSEQ: accession NC_003197.2 KEYWORDS RefSeq. SOURCE Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 ORGANISM Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Salmonella. REFERENCE 1 (residues 1 to 672) AUTHORS McClelland,M., Sanderson,K.E., Spieth,J., Clifton,S.W., Latreille,P., Courtney,L., Porwollik,S., Ali,J., Dante,M., Du,F., Hou,S., Layman,D., Leonard,S., Nguyen,C., Scott,K., Holmes,A., Grewal,N., Mulvaney,E., Ryan,E., Sun,H., Florea,L., Miller,W., Stoneking,T., Nhan,M., Waterston,R. and Wilson,R.K. TITLE Complete genome sequence of Salmonella enterica serovar Typhimurium LT2 JOURNAL Nature 413 (6858), 852-856 (2001) PUBMED 11677609 REFERENCE 2 (residues 1 to 672) CONSRTM NCBI Genome Project TITLE Direct Submission JOURNAL Submitted (08-SEP-2022) National Center for Biotechnology Information, NIH, Bethesda, MD 20894, USA REFERENCE 3 (residues 1 to 672) AUTHORS McClelland,M., Jain,A., Saraogi,P., Mendelson,R., Westerman,R., SanMiguel,P. and Csonka,L. TITLE Direct Submission JOURNAL Submitted (13-JAN-2016) Department of Microbiology and Molecular Genetics, University of California, Irvine, CA 92697, USA REMARK Sequence update by submitter REFERENCE 4 (residues 1 to 672) CONSRTM The Salmonella typhimurium Genome Sequencing Project TITLE Direct Submission JOURNAL Submitted (29-MAR-2001) Genome Sequencing Center, Department of Genetics, Washington University School of Medicine, 4444 Forest Park Boulevard, St. Louis, MO 63108, USA COMMENT PROVISIONAL REFSEQ: This record has not yet been subject to final NCBI review. The reference sequence is identical to AAL22092. Supported by NIH grant 5U 01 AI43283 Coding sequences below are predicted from manually evaluated computer analysis, using similarity information and the programs; GLIMMER; http://www.tigr.org/softlab/glimmer/glimmer.html and GeneMark; http://opal.biology.gatech.edu/GeneMark/ EC numbers were kindly provided by Junko Yabuzaki and the Kyoto Encyclopedia of Genes and Genomes; http://www.genome.ad.jp/kegg/, and Pedro Romero and Peter Karp at EcoCyc; http://ecocyc.PangeaSystems.com/ecocyc/ The analyses of ribosome binding sites and promoter binding sites were kindly provided by Heladia Salgado, Julio Collado-Vides and ReguonDB; http://kinich.cifn.unam.mx:8850/db/regulondb_intro.frameset This sequence was finished as follows unless otherwise noted: all regions were double stranded, sequenced with an alternate chemistries or covered by high quality data (i.e., phred quality >= 30); an attempt was made to resolve all sequencing problems, such as compressions and repeats; all regions were covered by sequence from more than one m13 subclone. Method: conceptual translation. FEATURES Location/Qualifiers source 1..672 /organism="Salmonella enterica subsp. enterica serovar Typhimurium str. LT2" /strain="LT2" /serovar="Typhimurium" /sub_species="enterica" /culture_collection="ATCC:700720" /culture_collection="SGSC:1412" /type_material="type strain of Salmonella enterica" /db_xref="taxon:99287" /focus Protein 1..672 /product="2,4-dieonyl-coa reductase" /EC_number="1.3.1.34" /calculated_mol_wt=72999 Region 6..358 /region_name="DCR_FMN" /note="2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur flavoenzyme which contains FMN, FAD, and a 4Fe-4S cluster. It is also a monomer, unlike that of its eukaryotic counterparts which form homotetramers and lack the...; cd02930" /db_xref="CDD:239240" Site order(25,27,59,101,165,167,176,215,253,256,311..312,335, 338,342,354) /site_type="active" /db_xref="CDD:239240" Site order(25,27,59,101,215,311..312) /site_type="other" /note="FMN binding site [chemical binding]" /db_xref="CDD:239240" Site order(165,167,176,253,256) /site_type="other" /note="2,4-decadienoyl-CoA binding site" /db_xref="CDD:239240" Site 167 /site_type="active" /note="catalytic residue [active]" /db_xref="CDD:239240" Site order(335,338,342,354) /site_type="other" /note="4Fe-4S cluster binding site [ion binding]" /db_xref="CDD:239240" Region <367..>512 /region_name="GltD" /note="NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; COG0493" /db_xref="CDD:440259" Region 400..>652 /region_name="FadH2" /note="NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism]; COG0446" /db_xref="CDD:440215" CDS 1..672 /gene="fadH" /locus_tag="STM3219" /coded_by="NC_003197.2:3386262..3388280" /note="similar to E. coli putative NADPH dehydrogenase (AAC76116.1); Blastp hit to AAC76116.1 (672 aa), 85% identity in aa 1 - 672" /transl_table=11 /db_xref="GeneID:1254742" CONTIG join(WP_000121523.1:1..672) ORIGIN 1 msypslfapl dlgfttlrnr vlmgsmhtgl eehpdgaerl aafyaerarh gvalivtggi 61 apvpsgvvmt ggamlndasq ltphrvvtda vhaqggkial qilhtgrysy qphlvapsai 121 qapinrfmph elthdeilql iddfahcaql areagydgve vmgsegylin efltrrtnhr 181 ddewggdyas rmrfavevvr avrqrvgndf iiiyrlsmld lvenggtfde tvqlaqaiea 241 agaslintgi gwhearipti atpvprgafs wvtrklkghv svpliatnri ndpqvaetil 301 trgdadmvsm arpfladaef ltkaqsgrad eintcigcnq acldrifigk vtsclvnpra 361 chethmpitp airkknlavv gagpaglafa inaasrghhv tlfdaqseig gqftiarqip 421 gkeefyetlr yyrrmidvtg vtlklnqrvn aedlqpfdea ilacgivprr ppidgidhpk 481 altylevlrd kapvgkrvai igcggigfdt amylsqhges tsqniaefct ewgidtslqq 541 agglrpegpr larsprqivm lqrktskpge glgkttgwih ratllargvk mipavsyqki 601 dddglhllig gepqllevdh vvicagqepr reladplraa gktvhliggc dvameldarr 661 aiaqgtrlal ei