Unfortunately due to lack of commercial feasibility, the SkyBLAST service has been suspended from December 1st, 2025.
All subscriptions for paid accounts have been paused. For further information or enquiries, please email [email protected]
LOCUS WP_003722416 331 aa linear BCT 01-JAN-2025 ACCESSION WP_003722416 VERSION WP_003722416.1 KEYWORDS RefSeq. SOURCE Listeria monocytogenes ORGANISM Listeria monocytogenes Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria. REFERENCE 1 (residues 1 to 331) AUTHORS Hammerstad,M. and Hersleth,H.P. TITLE Overview of structurally homologous flavoprotein oxidoreductases containing the low Mr thioredoxin reductase-like fold - A functionally diverse group JOURNAL Arch Biochem Biophys 702, 108826 (2021) PUBMED 33684359 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 11422994 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..331 /organism="Listeria monocytogenes" /db_xref="taxon:1639" Protein 1..331 /product="NAD(P)/FAD-dependent oxidoreductase" /EC_number="1.-.-.-" /GO_function="GO:0016491 - oxidoreductase activity [Evidence IEA]" /GO_function="GO:0050660 - flavin adenine dinucleotide binding [Evidence IEA]" /calculated_mol_wt=36295 Region 8..318 /region_name="TrxB" /note="Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; COG0492" /db_xref="CDD:440258" ORIGIN 1 mdektkiydi tiigggpvgl faafyagmrn asvkiieslp qlggqlstly pekyiydipg 61 ypsvraqelv nnliqqmkpf dptvaleeav qsvekqvdgt feiitkkdth yskaiiitag 121 ngafeprrld lpeaeqyegt nihyfindls rfsgrrvavc gggdsavdwa lmlekvassv 181 aivhrrnafr ahehsvnnle kssiaiktpf iptevlgngd klthitlqev kgdttetlei 241 ddfiinygfv sslgpiknwg lelernsivv nskmetsipg iycagdicty dgkvkliatg 301 fgeaptavnn amnfidpktr vqpmhstslf e