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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap rRNA-5S-3 rRNA-23S-3 IGR1381 IGR1382 IGR1380 IGR1383 IGR1378 IGR1379 IGR1379.1 IGR1384 IGR1385 IGR1379.2 IGR1384.1 IGR1385.1 NG1697 NG1690 vapA, - NG1689 NG1689.1 comE, - NG1698 folA, - NG1694 aroG, - NG1695 NG1688 NG1696 NG1692 NG1693 NG1687 NG1697 NG1690 vapA, - NG1689 NG1689.1 comE, - NG1698 folA, - NG1694 aroG, - NG1695 NG1688 NG1696 NG1692 NG1693 NG1687 Type: direct, Name:  - 102 Type: direct, Name:  - 108 Type: direct, Name:  - 124 NG1697 NG1690 NG1689.1 comE, - NG1698 folA, - NG1694 aroG, - NG1695 NG1688 vapA, - NG1689 NG1696 NG1693 NG1687 NG1691 NG1692 NG1691
* Calculated from Protein Sequence

Gene ID: NG1694

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
folA  

Definition:
dihydrofolate reductase (FolA)

Gene Start:
1646175

Gene Stop:
1645690

Gene Length:
486

Molecular Weight*:
17687

pI*:
6.30

Net Charge*:
-1.47

EC:
1.5.1.3  

Functional Class:
Biosynthesis of cofactors, prosthetic groups, and carriers; Folic acid  

Pathway: pathway table
Folate biosynthesis
One carbon pool by folate

Primary Evidence:
Baccanari,D.P., Tansik,R.L., Paterson,S.J. and Stone,D.,
Characterization and amino acid sequence of Neisseria gonorrhoeae
dihydrofolate reductase,
Medline: 85006974



Secondary Evidence:
Bystroff,C. and Kraut,J.
Crystal structure of unliganded Escherichia coli dihydrofolate
reductase. Ligand-induced conformational changes and cooperativity
in binding
Biochemistry 30 (8), 2227-2239 (1991)
Medline: 91152037

Bystroff,C., Oatley,S.J. and Kraut,J.
Crystal structures of Escherichia coli dihydrofolate reductase: the NADP+ holoenzyme and the folate.NADP+ ternary complex. Substrate binding and a model for the transition state
Biochemistry 29 (13), 3263-3277 (1990)
Medline: 90241903

Flensburg,J. and Skold,O.
Massive overproduction of dihydrofolate reductase in bacteria as a
response to the use of trimethoprim
Eur. J. Biochem. 162 (3), 473-476 (1987)
Medline: 87161813

Baccanari,D.P., Stone,D. and Kuyper,L.
Effect of a single amino acid substitution on Escherichia coli
dihydrofolate reductase catalysis and ligand binding
J. Biol. Chem. 256 (4), 1738-1747 (1981)
Medline: 81117257

Smith,D.R. and Calvo,J.M.
Nucleotide sequence of the E coli gene coding for dihydrofolate
reductase
Nucleic Acids Res. 8 (10), 2255-2274 (1980)
Medline: 81053692

Stone,D., Phillips,A.W. and Burchall,J.J.
The amino-acid sequence of the dihydrofolate reductase of a
trimethoprim-resistant strain of Escherichia coli
Eur. J. Biochem. 72 (3), 613-624 (1977)
Medline: 77115802


Comment:
Oklahoma ID: NGO.1694c

For other 'fol' genes, see NG0267 (folI), NG0323 (folK), NG0857 (folB), NG1342 (folP), NG0266 (folA), NG1999 (folD).

Blast Summary:  PSI-Blast Search
NG1694 is 99% identical to a previously sequenced N.gonorrhoeae protein in GenBank, 118996.

Residues 1-161 are 94% similar to dihydrofolate reductase in Neisseria meningitidis Z2491 (11252924|).

Numerous hits in gapped BLAST to dihydrofolate reductase sequences, e.g. residues 4-144 are 53% similar to dihydrofolate reductase in Pseudomonas aeruginosa strain PAO1 (11348423|). Residues 4-137 are 45% similar to dihydrofolate reductase in Escherichia coli (1311372|).




COGS Summary:  COGS Search
BeTs to 7 clades of COG0262
COG name: Dihydrofolate reductase
Functional Class:  H
The phylogenetic pattern of COG0262 is ----y-v-eBrh--GP--in-
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
***** IPB001796 (Dihydrofolate reductase) with a combined E-value of 1.4e-39.
    IPB001796A    7-18
    IPB001796B    23-37
    IPB001796C    40-52
    IPB001796D    55-67
    IPB001796E    95-104
    IPB001796F    114-130


ProDom Summary:  Protein Domain Search
Residues 7-133 are 99% similar to a (DIHYDROFOLATE REDUCTASE OXIDOREDUCTASE NADP ONE-CARBON) protein domain (PD000692) which is seen in DYR_NEIGO.

Residues 134-160 are identical to a (DIHYDROFOLATE REDUCTASE EC 1.5.1.3) protein domain (PD091243) which is seen in DYR_NEIGO.



Paralogs:  Local Blast Search


NG1694 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.


Pfam Summary:  Pfam Search
Residues 3 to 161 (E-value = 4.5e-86) place NG1694 in the DiHfolate_red family which is described as Dihydrofolate reductase (PF00186)

Structural Feature(s):
Feature Type  Start  Stop
uncleavable N-terminal sequence N-terminal sequence  
1  
21
non-globular  
64  
127

PDB Hit:
pdb|1DF7|1DF7-A DIHYDROFOLATE REDUCTASE OF MYCOBACTERIUM 136.0 3e-33
pdb|1DDR|1DDR-A MOLECULE: DIHYDROFOLATE REDUCTASE (E.C.1.5.1.3) 121.0 7e-29
pdb|1TDR|1TDR-A MOLECULE: TELLUROMETHIONYL DIHYDROFOLATE 121.0 9e-29
pdb|1DRE|1DRE DIHYD

Gene Protein Sequence:
MLKITIIAACAENLCIGAGNAMPWHIPEDFAFFKAYTLGKPVIMGRKTWE
SLPVKPLPGRRNIVISRQADYCAAGAETVASLEVALALCAGAEEAVIMGG
AQIYGQAMPLATDLRITEVDLSVEGDAFFPEIDRTHWREAERTERRVSSK
GVAYTFVHYLKG

Gene Nucleotide Sequence:  Sequence Viewer
ATGCTCAAAATAACCATAATTGCGGCGTGTGCGGAAAACCTGTGCATCGG
GGCGGGCAATGCTATGCCTTGGCACATCCCCGAAGATTTCGCATTTTTCA
AAGCCTATACCTTGGGCAAACCCGTCATTATGGGGCGGAAAACGTGGGAA
TCCCTGCCCGTCAAACCCCTGCCCGGACGGAGGAACATCGTCATCAGCCG
GCAGGCGGATTATTGCGCGGCAGGCGCGGAAACGGTGGCAAGTTTGGAGG
TGGCATTGGCATTGTGCGCCGGCGCGGAAGAAGCCGTCATTATGGGCGGC
GCGCAGATATACGGACAAGCGATGCCATTAGCGACCGATTTGCGGATAAC
CGAAGTGGATTTGTCTGTGGAAGGAGATGCATTTTTCCCAGAAATAGACC
GGACGCATTGGAGAGAAGCAGAGCGGACGGAACGCCGTGTCAGCAGCAAA
GGCGTTGCATATACATTCGTGCATTACCTCAAGGGA


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