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LOCUS WP_002903618 316 aa linear BCT 01-JAN-2025 ACCESSION WP_002903618 VERSION WP_002903618.1 KEYWORDS RefSeq. SOURCE Klebsiella ORGANISM Klebsiella Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group. REFERENCE 1 (residues 1 to 316) AUTHORS Bertsova,Y.V., Fadeeva,M.S., Kostyrko,V.A., Serebryakova,M.V., Baykov,A.A. and Bogachev,A.V. TITLE Alternative pyrimidine biosynthesis protein ApbE is a flavin transferase catalyzing covalent attachment of FMN to a threonine residue in bacterial flavoproteins JOURNAL J Biol Chem 288 (20), 14276-14286 (2013) PUBMED 23558683 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 :: Conserved Domain (CDD) Evidence Accession :: Domain architecture ID 10003878 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..316 /organism="Klebsiella" /db_xref="taxon:570" Protein 1..316 /product="FAD:protein FMN transferase" /EC_number="2.7.1.180" /GO_component="GO:0005886 - plasma membrane [Evidence IEA]" /GO_function="GO:0016740 - transferase activity [Evidence IEA]" /GO_function="GO:0046872 - metal ion binding [Evidence IEA]" /GO_process="GO:0017013 - protein flavinylation [Evidence IEA]" /calculated_mol_wt=34836 Region 14..296 /region_name="ApbE" /note="FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational modification, protein turnover, chaperones]; COG1477" /db_xref="CDD:441086" ORIGIN 1 msdnrvysys avlmgspill klcshdeama srvfqlikry edlltvnrae sqvmdinhaa 61 grhpvtvsrp vfqliqcaka asmvrdsafn laigplvklw rigfhghsvp daadirarla 121 ltrpqevild eatcsvflqq pgmeldlgai akgyiadrvr dflrqqqvek alinlggnvh 181 tlgewaiglk kpfadaqali gsltvngqsv vtsgtyeryf eqdgkrwhhi ldprsgypld 241 neldsvtvis adsldgdiwt tllfglgvek gcaalrqrqd idaifvtknr diilsspqrl 301 rfasldsgyr vidcta