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Information on EC 1.5.1.37 - FAD reductase (NADH) and Organism(s) Burkholderia cepacia and UniProt Accession O87008

for references in articles please use BRENDA:EC1.5.1.37
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EC Tree
     1 Oxidoreductases
         1.5 Acting on the CH-NH group of donors
             1.5.1 With NAD+ or NADP+ as acceptor
                1.5.1.37 FAD reductase (NADH)
IUBMB Comments
The enzyme from Burkholderia phenoliruptrix can reduce either FAD or flavin mononucleotide (FMN) but prefers FAD. Unlike EC 1.5.1.36, flavin reductase (NADH), the enzyme can not reduce riboflavin. The enzyme does not use NADPH as acceptor.
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This record set is specific for:
Burkholderia cepacia
UNIPROT: O87008
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Word Map
The taxonomic range for the selected organisms is: Burkholderia cepacia
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
sgce6, nadh-fad reductase, nadh:fad oxidoreductase, fad:nadh reductase, nad(p)h:fad reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NADH:FAD oxidoreductase
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NADH-dependent FAD reductase
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-
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NADH-FAD reductase
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-
-
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NADH:FAD oxidoreductase
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-
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NADH:flavin adenine dinucleotide oxidoreductase
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
FADH2:NAD+ oxidoreductase
The enzyme from Burkholderia phenoliruptrix can reduce either FAD or flavin mononucleotide (FMN) but prefers FAD. Unlike EC 1.5.1.36, flavin reductase (NADH), the enzyme can not reduce riboflavin. The enzyme does not use NADPH as acceptor.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
free FADH2 is generated by NADH:FAD oxidoreductase (TftC), and FADH2-dependent monooxygenase (TftD) uses FADH2 to separately transform 2,4,5-trichlorophenol and 2,5-dichloro-p-hydroquinone
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TFTC_BURCE
179
0
19028
Swiss-Prot
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apo-form crystals of TftC, TftC-FAD complex and TftC-FAD-NADH complex are grown at 4°C using the hanging drop vapor diffusion method. Crystal structures of dimeric TftC is determined at 2.5 A resolution
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Webb, B.N.; Ballinger, J.W.; Kim, E.; Belchik, S.M.; Lam, K.S.; Youn, B.; Nissen, M.S.; Xun, L.; Kang, C.
Characterization of chlorophenol 4-monooxygenase (TftD) and NADH:FAD oxidoreductase (TftC) of Burkholderia cepacia AC1100
J. Biol. Chem.
285
2014-202
2010
Burkholderia cepacia (O87008)
Manually annotated by BRENDA team