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LOCUS WP_002885150 139 aa linear BCT 02-MAR-2025 ACCESSION WP_002885150 VERSION WP_002885150.1 KEYWORDS RefSeq. SOURCE Klebsiella pneumoniae ORGANISM Klebsiella pneumoniae Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella; Klebsiella pneumoniae complex. REFERENCE 1 (residues 1 to 139) AUTHORS Schneider,F., Lowe,J., Huber,R., Schindelin,H., Kisker,C. and Knablein,J. TITLE Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1.88 A resolution JOURNAL J Mol Biol 263 (1), 53-69 (1996) PUBMED 8890912 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 :: NF012602.6 Evidence Source :: EMBL-EBI Source Identifier :: PF00384.27 ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..139 /organism="Klebsiella pneumoniae" /db_xref="taxon:573" Protein 1..139 /product="molybdopterin-dependent oxidoreductase" /GO_function="GO:0016491 - oxidoreductase activity [Evidence IEA]" /calculated_mol_wt=15067 Region 6..>139 /region_name="Molybdopterin-Binding" /note="Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and...; cl09928" /db_xref="CDD:447860" ORIGIN 1 mkkvvtvcpy casgckinlv vdngkivrae aaqgktnqgt lclkgyygwd findtqiltp 61 rlktpmirrq rggkleavsw dealdyvatr lsaikakygp daiqttgssr gtgnetnyvm 121 qkfaravigt nnvdccarv