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LOCUS WP_002894467 321 aa linear BCT 20-NOV-2023 ACCESSION WP_002894467 VERSION WP_002894467.1 KEYWORDS RefSeq. SOURCE Klebsiella ORGANISM Klebsiella Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group. REFERENCE 1 (residues 1 to 321) AUTHORS Ollagnier-de Choudens,S. and Fontecave,M. TITLE The lipoate synthase from Escherichia coli is an iron-sulfur protein JOURNAL FEBS Lett. 453 (1-2), 25-28 (1999) PUBMED 10403368 REFERENCE 2 (residues 1 to 321) AUTHORS Sulo,P. and Martin,N.C. TITLE Isolation and characterization of LIP5. A lipoate biosynthetic locus of Saccharomyces cerevisiae JOURNAL J. Biol. Chem. 268 (23), 17634-17639 (1993) PUBMED 8349643 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 :: TIGR00510.1 Evidence Source :: JCVI ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..321 /organism="Klebsiella" /db_xref="taxon:570" gene 1..321 /gene="lipA" Protein 1..321 /product="lipoyl synthase" /EC_number="2.8.1.8" /GO_function="GO:0016992 - lipoate synthase activity [Evidence IEA]" /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster binding [Evidence IEA]" /GO_function="GO:1904047 - S-adenosyl-L-methionine binding [Evidence IEA]" /GO_process="GO:0009107 - lipoate biosynthetic process [Evidence IEA]" /calculated_mol_wt=35960 Region 22..321 /region_name="LipA" /note="Lipoate synthase [Coenzyme transport and metabolism]; COG0320" /db_xref="CDD:440089" ORIGIN 1 mskpivmerg vkyrdadkma lipvknvate reallrkpew mkiklpadss riqgikaamr 61 knglhsvcee ascpnlaecf nhgtatfmil gaictrrcpf cdvahgrpva pdanepqkla 121 qtiadmglry vvvtsvdrdd lrdggaqhfa dcisairekn psikietlvp dfrgrmdral 181 diltvtppdv fnhnlenvpr lyrqvrpgad ynwslkller fkeahpeipt ksglmvglge 241 tndeiievmr dlrrhgvtml tlgqylqpsr hhlpvqryvs peefeemkae amamgfthaa 301 cgpfvrssyh adlqakgmev k