Basic Search | Intermediate Search | Advanced SQL Search | Gene Image Map |  Home

Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR0582.1 IGR0580 IGR0581 IGR0576 IGR0577 IGR0579 IGR0578 IGR0582 IGR0582.2 NG0690 NG0691.1 NG0691 fenR, - NG0687 NG0688 thrC, - NG0689 NG0686 hlfX, - NG0684 NG0683 NG0685 NG0690 NG0691.1 NG0691 fenR, - NG0687 NG0688 thrC, - NG0689 NG0686 hlfX, - NG0684 NG0683 NG0685 NG0690 NG0691 fenR, - NG0687 NG0688 thrC, - NG0689 NG0691.1 NG0686 hlfX, - NG0684 NG0683 NG0685
* Calculated from Protein Sequence

Gene ID: NG0687

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
fenR  

Definition:
ferredoxin-NADP reductase

Gene Start:
678446

Gene Stop:
677673

Gene Length:
774

Molecular Weight*:
29317

pI*:
6.10

Net Charge*:
-4.20

EC:
1.18.1.2  

Functional Class:
Energy metabolism; Electron transport  

Pathway: pathway table
Porphyrin and chlorophyll metabolism

Secondary Evidence:
Bianchi,V., Reichard,P., Eliasson,R., Pontis,E., Krook,M.,Jornvall,H. and Haggard-Ljungquist,E. Escherichia coli ferredoxin NADP+ reductase: activation of E. coli anaerobic ribonucleotide reduction, cloning of the gene (fpr), andoverexpression of the protein. J. Bacteriol. 175 (6): 1590-1595 (1993) [Medline: 93194782].

Jenkins,C.M. and Waterman,M.R. Flavodoxin and NADPH-flavodoxin reductase from Escherichia coli support bovine cytochrome P450c17 hydroxylase activities. J. Biol. Chem. 269 (44): 27401-27408 (1994) [Medline: 95050480].

Ingelman,M., Bianchi,V. and Eklund,H. The three-dimensional structure of flavodoxin reductase from Escherichia coli at 1.7 A resolution. J. Mol. Biol. 268 (1): 147-157 (1997) [Medline: 97293095].

Comment:
From GenBANK (gi:399486): In E. coli, ferredoxin NADP reductase transports electrons between flavodoxin or ferredoxin and NADPH. It is involved in the reductive activation of cobalamin-independent methionine synthase, pyruvate formate lyase
and anaerobic ribonucleotide reductase. It also protects against superoxide radicals due to methyl viologen in the presence of oxygen. The protein catayzes this reaction: reduced ferredoxin + NADP(+) = oxidized ferredoxin + NADPH, requiring a cofactor, FAD. Note that some previously incorrectly assigned the protein to be part of FPR, the C-terminal of GlpX.

Oklahoma ID: NGO.687c

Blast Summary:  PSI-Blast Search
Numerous significant hits in gapped BLAST to ferredoxin NADP+ reductases; e.g. residues 1-258 are 68% similar to L36319 of Azotobacter vinelandii.

Residues 1-258 have 98% similarity to AE002455, N. meningitidis MC58 ferredoxin--NADP reductase (11353901).

COGS Summary:  COGS Search
BeTs to 3 clades of COG1018
COG name: Flavodoxin reductases (ferredoxin-NADPH reductases) family 1
Functional Class:  C
The phylogenetic pattern of COG1018 is ----y---EbR----------
Number of proteins in this genome belonging to this COG is 2

Blocks Summary:  Blocks Search
***** PR00410 (Phenol hydroxylase reductase family signature) with a combined E-value of 3.2e-06.
    PR00410B    51-58
    PR00410D    111-130
    PR00410F    215-223
***** PR00371 (Flavoprotein pyridine nucleotide cytochrome reductase signature) with a combined E-value of 7.6e-06.
    PR00371B    51-58
    PR00371D    111-130
    PR00371H    215-223


ProDom Summary:  Protein Domain Search
Residues 51-121 are 80% similar to a (REDUCTASE OXIDOREDUCTASE FAD FLAVOPROTEIN NADP HEME NAD) protein domain (PD000183) which is seen in FENR_AZOVI.

Residues 5-50 are 65% similar to a (FERREDOXIN--NADP REDUCTASE EC 1.18.1.2) protein domain (PD155002) which is seen in FENR_AZOVI.

Residues 122-232 are 65% similar to a (REDUCTASE FERREDOXIN--NADP FNR PROTEIN OXIDOREDUCTASE) protein domain (PD109340) which is seen in FENR_AZOVI.



Paralogs:  Local Blast Search


NG0687 is paralogously related to NG0734 (ferredoxin-NADP reductase, FenR) (2e-39) and NG1418 (sodium-translocating NADH-ubiquinone reductase subunit F (NqrF)) (8e-08).


Pfam Summary:  Pfam Search
Residues 107 to 231 (E-value = 1.5e-06) place NG0687 in the NAD_binding_1 family which is described as Oxidoreductase NAD-binding domain (PF00175)

Structural Feature(s):
Feature Type  Start  Stop
No predicted structural features.  
  

PDB Hit:
pdb|1A8P|1A8P FERREDOXIN REDUCTASE FROM AZOTOBACTER VINELANDII 388.0 0e+00
pdb|1FDR|1FDR FLAVODOXIN REDUCTASE FROM E. COLI 143.0 3e-35
pdb|1KRH|1KRH-A X-RAY STUCTURE OF BENZOATE DIOXYGENASE REDUCTASE 45.7 9e-06
pdb|1QFY|1QFY-A PEA

Gene Protein Sequence:
MAAFNTQKVLSVHHWTDAYFTFTCIRDESLRFENGQFVMVGLMADGKPLM
RAYSVASANWEEHLEFFSIKVQDGPLTSRLQHLKVGDEVLISKKPTGTLV
AGDLNPGKHLYLLSTGTGIAPFLSITKDPEIYEQFEKIILVHGVRYKKDL
AYYDRFTKELPEHEYLGDLVKEKLIYYPIVSREEFEHRGRLTDLMVSGKL
FEDIGLPKINPQDDRAMLCGSPAMLKDTCKVLDDFGLTVSPKTGVRGDYL
IERAFVDQ

Gene Nucleotide Sequence:  Sequence Viewer
ATGGCAGCATTCAATACCCAAAAAGTATTGTCCGTACACCACTGGACAGA
CGCATATTTTACCTTTACCTGCATCCGCGACGAATCGTTGCGCTTTGAAA
ACGGACAGTTCGTCATGGTCGGGCTGATGGCGGACGGCAAGCCGCTGATG
CGCGCATACAGCGTCGCCTCCGCCAACTGGGAAGAACACCTCGAATTTTT
CAGCATTAAAGTCCAAGACGGCCCGCTGACCAGCCGCCTGCAACACCTCA
AAGTCGGCGACGAAGTGTTAATCAGCAAAAAACCGACCGGAACTCTGGTT
GCCGGCGACCTGAATCCGGGCAAACACCTTTACTTGTTGAGCACCGGTAC
CGGCATCGCCCCTTTCTTGAGCATCACCAAAGACCCCGAGATTTACGAGC
AATTTGAAAAAATCATCCTCGTACACGGCGTGCGCTACAAAAAAGATTTG
GCGTACTACGACCGCTTTACCAAAGAATTGCCCGAACACGAATACCTCGG
CGACTTGGTTAAAGAAAAACTGATTTACTACCCGATTGTTTCCCGAGAAG
AATTCGAACACCGCGGCCGCCTGACCGACCTGATGGTAAGCGGCAAACTG
TTTGAAGACATCGGCCTGCCCAAAATCAACCCGCAAGACGACCGCGCGAT
GCTGTGCGGCAGCCCCGCGATGCTGAAAGATACCTGCAAAGTTTTGGACG
ATTTCGGTCTGACAGTCTCCCCGAAAACCGGCGTGCGCGGCGACTACCTG
ATTGAGCGCGCATTTGTGGATCAA


Los Alamos National Laboratory     
Operated by the University of California for the National Nuclear Security Administration,
of the US Department of Energy.     Copyright © 2001 UC | Disclaimer/Privacy