fprA
- Type
- protein_coding
- Name
- fprA
- Locus Name
-
Rv3106
- Product
-
NADPH:adrenodoxin oxidoreductase FprA (NADPH-ferredoxin reductase)
- Functional Category
-
Intermediary metabolism and respiration
- Location
- 3474007..3475377 (+ strand)
- Gene Length
- 1370 bp
- Nucleotides
-
TGCGTCCCTATTACATCGCCATCGTGGGCTCCGGGCCGTCGGCGTTCTTCGCCGCGGCATCCTTGCTGAAGGCCGCCGACACGACCGAGGACCTCGACATGGCCGTCGACATGCTGGAGATGTTGCCGACTCCCTGGGGGCTGGTGCGCTCCGGGGTCGCGCCGGATCACCCCAAGATCAAGTCGATCAGCAAGCAATTCGAAAAGACGGCCGAGGACCCCCGCTTCCGCTTCTTCGGCAATGTGGTCGTCGGCGAACACGTCCAGCCCGGCGAGCTCTCCGAGCGCTACGACGCCGTGATCTACGCCGTCGGCGCGCAGTCCGATCGCATGTTGAACATCCCCGGTGAGGACCTGCCGGGCAGTATCGCCGCCGTCGATTTCGTCGGCTGGTACAACGCACATCCACACTTCGAGCAGGTATCACCCGATCTGTCGGGCGCCCGGGCCGTAGTTATCGGCAATGGAAACGTCGCGCTAGACGTGGCACGGATTCTGCTCACCGATCCCGACGTGTTGGCACGCACCGATATCGCCGATCACGCTTTGGAATCGCTACGCCCACGCGGTATCCAGGAGGTGGTGATCGTCGGGCGCCGAGGTCCGCTGCAGGCCGCGTTCACCACGTTGGAGTTGCGCGAGCTGGCCGACCTCGACGGGGTTGACGTGGTGATCGATCCGGCGGAGCTGGACGGCATTACCGACGAGGACGCGGCCGCGGTGGGCAAGGTCTGCAAGCAGAACATCAAGGTGCTGCGTGGCTATGCGGACCGCGAACCCCGCCCGGGACACCGCCGCATGGTGTTCCGGTTCTTGACCTCTCCGATCGAGATCAAGGGCAAGCGCAAAGTGGAGCGGATCGTGCTGGGCCGCAACGAGCTGGTCTCCGACGGCAGCGGGCGAGTGGCGGCCAAGGACACCGGCGAGCGCGAGGAGCTGCCAGCTCAGCTGGTCGTGCGGTCGGTCGGCTACCGCGGGGTGCCCACGCCCGGGCTGCCGTTCGACGACCAGAGCGGGACCATCCCCAACGTCGGCGGCCGAATCAACGGCAGCCCCAACGAATACGTCGTCGGGTGGATCAAGCGCGGGCCGACCGGGGTGATCGGGACCAACAAGAAGGACGCCCAAGACACCGTCGACACCTTGATCAAGAATCTTGGCAACGCCAAGGAGGGCGCCGAGTGCAAGAGCTTTCCGGAAGATCATGCCGACCAGGTGGCCGACTGGCTAGCAGCACGCCAGCCGAAGCTGGTCACGTCGGCCCACTGGCAGGTGATCGACGCTTTCGAGCGGGCCGCCGGCGAGCCGCACGGGCGTCCCCGGGTCAAGTTGGCCAGCCTGGCCGAGCTGTTGCGGATTGGGCTCGGCTGA
- Drug Resistance
- Mutations
- Function
- May serve as electron transfer protein and supply electrons to P450 systems.
- Family
-
Ferredoxin--NADP reductase type 1 family
- GO
-
- cell wall GO:0005618 cellular_component
- flavin adenine dinucleotide binding GO:0050660 molecular_function
- NADP+ binding GO:0070401 molecular_function
- oxidation-reduction process GO:0055114 biological_process
- ferredoxin-NAD+ reductase activity GO:0008860 molecular_function
- ferredoxin-NADP+ reductase activity GO:0004324 molecular_function
- InterPro
1LQT
- Name
- NADPH-ferredoxin reductase FprA (NFR) (EC 1.18.1.2)
- Family
- Ferredoxin--NADP reductase type 1 family
- Protein Sequence
-
MRPYYIAIVGSGPSAFFAAASLLKAADTTEDLDMAVDMLEMLPTPWGLVRSGVAPDHPKIKSISKQFEKTAEDPRFRFFGNVVVGEHVQPGELSERYDAVIYAVGAQSDRMLNIPGEDLPGSIAAVDFVGWYNAHPHFEQVSPDLSGARAVVIGNGNVALDVARILLTDPDVLARTDIADHALESLRPRGIQEVVIVGRRGPLQAAFTTLELRELADLDGVDVVIDPAELDGITDEDAAAVGKVCKQNIKVLRGYADREPRPGHRRMVFRFLTSPIEIKGKRKVERIVLGRNELVSDGSGRVAAKDTGEREELPAQLVVRSVGYRGVPTPGLPFDDQSGTIPNVGGRINGSPNEYVVGWIKRGPTGVIGTNKKDAQDTVDTLIKNLGNAKEGAECKSFPEDHADQVADWLAARQPKLVTSAHWQVIDAFERAAGEPHGRPRVKLASLAELLRIGLG
- Mass
- 49,341 Da
- Length
- 456 Aa
Summary
- Flavin adenine dinucleotide DB03147
-
Adenosine 5'-(trihydrogen pyrophosphate), 5'-5'-ester with riboflavine | Adenosine 5'-[3-(riboflavin-5'-yl) dihydrogen diphosphate] | FAD | Flavin adenine dinucleotide | FLAVIN-adenine dinucleotide | Flavine adenine dinucleotide | Riboflavin 5'-(trihydrogen diphosphate), 5'-5'-ester with adenosine | Riboflavin 5'-adenosine diphosphate
Rv3106 doesn't seem to be involved in any pathway.
- Role of the His57-Glu214 ionic couple located in the active site of Mycobacterium tuberculosis FprA.
- Biochemistry. 2006 Jul 25;45(29):8712-20. doi: 10.1021/bi060369m.
- A covalent modification of NADP+ revealed by the atomic resolution structure of FprA, a Mycobacterium tuberculosis oxidoreductase.
- Biochemistry. 2002 Jul 16;41(28):8807-18. doi: 10.1021/bi025858a.
- Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry.
- Mol Cell Proteomics. 2011 Dec;10(12):M111.011627. doi: 10.1074/mcp.M111.011445. Epub 2011 Oct 3.
- Kinetic, spectroscopic and thermodynamic characterization of the Mycobacterium tuberculosis adrenodoxin reductase homologue FprA.
- Biochem J. 2003 Jun 1;372(Pt 2):317-27. doi: 10.1042/BJ20021692.
- Mycobacterium tuberculosis FprA, a novel bacterial NADPH-ferredoxin reductase.
- Eur J Biochem. 2002 Jun;269(12):3005-13. doi: 10.1046/j.1432-1033.2002.02989.x.
- Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.
- Nature. 1998 Jun 11;393(6685):537-44. doi: 10.1038/31159.