Difference between revisions of "Part:BBa K1796006"

Line 2: Line 2:
 
<partinfo>BBa_K1796006 short</partinfo>
 
<partinfo>BBa_K1796006 short</partinfo>
  
Dinitrogenase reductase, important in nitrogen fixation.  
+
The nifH encoding dinitrogenase reductase(also called Fe protein) is an important gene in nitrogen fixation. The protein is a homodimer bridged by an intersubunit [4Fe-4S] cluster that serves as the obligate electron donor to the MoFe protein.
 
+
 
<!-- Add more about the biology of this part here
 
<!-- Add more about the biology of this part here
 
===Usage and Biology===
 
===Usage and Biology===

Revision as of 21:29, 18 September 2015

Dinitrogenase reductase(nifH)

The nifH encoding dinitrogenase reductase(also called Fe protein) is an important gene in nitrogen fixation. The protein is a homodimer bridged by an intersubunit [4Fe-4S] cluster that serves as the obligate electron donor to the MoFe protein. Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


Parametre of Protein

Number of amino acids: 294

Molecular weight: 32136.5

Theoretical pI: 4.79

Amino acid composition: 

Ala (A) 26 8.8%

Arg (R) 13 4.4%

Asn (N) 16 5.4%

Asp (D) 14 4.8%

Cys (C) 6 2.0%

Gln (Q) 13 4.4%

Glu (E) 29 9.9%

Gly (G) 30 10.2%

His (H) 5 1.7%

Ile (I) 22 7.5%

Leu (L) 27 9.2%

Lys (K) 14 4.8%

Met (M) 11 3.7%

Phe (F) 9 3.1%

Pro (P) 8 2.7%

Ser (S) 9 3.1%

Thr (T) 17 5.8%

Trp (W) 0 0.0%

Tyr (Y) 8 2.7%

Val (V) 17 5.8%

Pyl (O) 0 0.0%

Sec (U) 0 0.0%

(B) 0 0.0%

(Z) 0 0.0%

(X) 0 0.0%

Total number of negatively charged residues (Asp + Glu): 43

Total number of positively charged residues (Arg + Lys): 27

Atomic composition:Carbon C 1400

Hydrogen H 2248

Nitrogen N 386

Oxygen O 444

Sulfur S 17

Formula: C1400H2248N386O444S17Total number of atoms: 4495

Extinction coefficients:This protein does not contain any Trp residues. Experience shows that

this could result in more than 10% error in the computed extinction coefficient.

Extinction coefficients are in units of M-1 cm-1, at 280 nm measured in water.

Ext. coefficient 12295

Abs 0.1% (=1 g/l) 0.383, assuming all pairs of Cys residues form cystines

Ext. coefficient 11920

Abs 0.1% (=1 g/l) 0.371, assuming all Cys residues are reduced

Estimated half-life:The N-terminal of the sequence considered is H (His).

The estimated half-life is: 3.5 hours (mammalian reticulocytes, in vitro).

10 min (yeast, in vivo).

>10 hours (Escherichia coli, in vivo).

Instability index:The instability index (II) is computed to be 38.27

This classifies the protein as stable.

Aliphatic index: 90.61

Grand average of hydropathicity (GRAVY): -0.185