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LOCUS WP_002898924 214 aa linear BCT 02-MAR-2025 ACCESSION WP_002898924 VERSION WP_002898924.1 KEYWORDS RefSeq. SOURCE Klebsiella ORGANISM Klebsiella Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group. REFERENCE 1 (residues 1 to 214) AUTHORS Laurie,A.D. and Lloyd-Jones,G. TITLE The phn genes of Burkholderia sp. strain RP007 constitute a divergent gene cluster for polycyclic aromatic hydrocarbon catabolism JOURNAL J Bacteriol 181 (2), 531-540 (1999) PUBMED 9882667 REFERENCE 2 (residues 1 to 214) AUTHORS Hu,S.H., Peek,J.A., Rattigan,E., Taylor,R.K. and Martin,J.L. TITLE Structure of TcpG, the DsbA protein folding catalyst from Vibrio cholerae JOURNAL J Mol Biol 268 (1), 137-146 (1997) PUBMED 9149147 REFERENCE 3 (residues 1 to 214) AUTHORS Brito,B., Palacios,J.M., Ruiz-Argueso,T. and Imperial,J. TITLE Identification of a gene for a chemoreceptor of the methyl-accepting type in the symbiotic plasmid of Rhizobium leguminosarum bv. viciae UPM791 JOURNAL Biochim Biophys Acta 1308 (1), 7-11 (1996) PUBMED 8765742 REFERENCE 4 (residues 1 to 214) AUTHORS Eaton,R.W. TITLE Organization and evolution of naphthalene catabolic pathways: sequence of the DNA encoding 2-hydroxychromene-2-carboxylate isomerase and trans-o-hydroxybenzylidenepyruvate hydratase-aldolase from the NAH7 plasmid JOURNAL J Bacteriol 176 (24), 7757-7762 (1994) PUBMED 8002605 REFERENCE 5 (residues 1 to 214) AUTHORS Denome,S.A., Stanley,D.C., Olson,E.S. and Young,K.D. TITLE Metabolism of dibenzothiophene and naphthalene in Pseudomonas strains: complete DNA sequence of an upper naphthalene catabolic pathway JOURNAL J Bacteriol 175 (21), 6890-6901 (1993) PUBMED 8226631 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 :: NF013488.6 Evidence Source :: EMBL-EBI Source Identifier :: PF01323.26 ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..214 /organism="Klebsiella" /db_xref="taxon:570" Protein 1..214 /product="DsbA family protein" /GO_function="GO:0015035 - protein-disulfide reductase activity [Evidence IEA]" /calculated_mol_wt=23849 Region 11..213 /region_name="Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold" /note="The thioredoxin (TRX)-like superfamily is a large, diverse group of proteins containing a TRX fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox...; cl00388" /db_xref="CDD:469754" Site order(55,57..58,175) /site_type="active" /note="catalytic residues [active]" /db_xref="CDD:239317" Site 88..90 /site_type="other" /note="hinge region" /db_xref="CDD:239317" Site order(95..103,108..127,130..138,144..153) /site_type="other" /note="alpha helical domain" /db_xref="CDD:239317" ORIGIN 1 mvlhgkvikl litilmvgls saayskdyqa gknftvihst vkqppplvef fsfycgpcya 61 faerinvdta irkrlpddmk lekyhvsqmg plgpalteaw avaqyagvdg kvekllfegl 121 qvkrdiktaa divmvfnqlg itsekyaemq snfmvkalia rqdnlvekmk vhgtpsfyvs 181 gkyhinntsl aqddydtyae dmanlvlfll nkpl