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

Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR0568 IGR0566 IGR0567 IGR0570 IGR0574 IGR0571 IGR0565 IGR0573 IGR0569 IGR0572 NG0678 leuD, - NG0677 rngoV, - NG0675 leu3, - NG0674 mtb5,mngoV, - NG0676 leuC,leu3, - NG0679 NG0672 tpn, - NG0673 radC, - NG0681 NG0682 suhB, - NG0671 gshA, - NG0680 NG0678 leuD, - NG0677 rngoV, - NG0675 leu3, - NG0674 mtb5,mngoV, - NG0676 leuC,leu3, - NG0679 NG0672 tpn, - NG0673 radC, - NG0681 NG0682 suhB, - NG0671 gshA, - NG0680 NG0678 leuD, - NG0677 rngoV, - NG0675 leu3, - NG0674 mtb5,mngoV, - NG0676 leuC,leu3, - NG0679 tpn, - NG0673 radC, - NG0681 NG0682 suhB, - NG0671 gshA, - NG0680 NG0672
* Calculated from Protein Sequence

Gene ID: NG0677

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
leuD  

Definition:
3-isopropylmalate dehydratase small subunit (isopropylmalate isomerase) (alpha-IPM isomerase) (IPMI)

Gene Start:
666914

Gene Stop:
666276

Gene Length:
639

Molecular Weight*:
24193

pI*:
6.40

Net Charge*:
-1.93

EC:
4.2.1.33  

Functional Class:
Amino acid biosynthesis; Branched chain amino acid family  

Pathway: pathway table
Valine, leucine and isoleucine biosynthesis

Primary Evidence:
Lau,P.C., Forghani,F., Labbe,D., Bergeron,H., Brousseau,R. and Holtke,H.J.
The NlaIV restriction and modification genes of Neisseria lactamica are flanked by leucine biosynthesis genes.
Mol. Gen. Genet. 243 (1): 24-31 (1994)
[Medline: 94247353].

Secondary Evidence:
Manna,A.C. and Das,H.K.
Characterization and mutagenesis of the leucine biosynthetic genes of Azotobacter vinelandii: an analysis of the rarity of amino acid auxotrophs.
Mol. Gen. Genet. 254 (2): 207-217 (1997)
[Medline: 97261869].

Friedberg,D., Rosenthal,E.R., Jones,J.W. and Calvo,J.M. Characterization of the 3' end of the leucine operon of Salmonella typhimurium.
Mol. Gen. Genet. 199 (3): 486-494 (1985)
[Medline: 85295470].

Comment:
From GenBANK (gi:2498515): The enzyme complex catalyzes two reactions: 1) 3-isopropylmalate = 2-isopropylmaleate + H2O and 2) 2-isopropylmaleate + H2O = 3-hydroxy-4-methyl-3-carboxypentanone). This is involved in the second step in leucine biosynthesis. The complex consists of two different subunits: leuC and leuD.

See leuC, large subunit, NG0679.

Oklahoma ID: NGO.677c

Blast Summary:  PSI-Blast Search
The central region (aa 135-213) of NG0677 is 98% identical to a previously sequenced Neisseria gonorrhoeae protein, isopropylmalate isomerase, in GenBank, 1165241.

Numerous significant hits in gapped BLAST to 3-isopropylmalate dehydratase, small chain; e.g. residues 1-211 are 74% similar to AE004736 of Pseudomonas aeruginosa.

Residues 1-213 have 97% similarity to AL162756, N. meningitidis Z2491 3-isopropylmalate dehydratase small subunit (11269414), and 96% similarity to AE002454, 3-isopropylmalate dehydratase, small subunit of N.meningitidis MC58 (11269418).

COGS Summary:  COGS Search
BeTs to 11 clades of COG0066
COG name: 3-isopropylmalate dehydratase small subunit
Functional Class:  E
The phylogenetic pattern of COG0066 is AMTkyqVcEbrh---------
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
***** IPB000573 (Aconitase C-terminal domain) with a combined E-value of 1.4e-37.
    IPB000573    79-128


ProDom Summary:  Protein Domain Search
Residues 86-204 are 69% similar to a (LYASE DEHYDRATASE 3-ISOPROPYLMALATE) protein domain (PD001077) which is seen in LEUD_AZOVI.

Residues 1-85 are 74% similar to a (3-ISOPROPYLMALATE DEHYDRATASE ISOMERASE ISOPROPYLMALATE) protein domain (PD018132) which is seen in LEUD_AZOVI.



Paralogs:  Local Blast Search


NG0677 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.


Pfam Summary:  Pfam Search
Residues 1 to 133 (E-value = 1.2e-55) place NG0677 in the Aconitase_C family which is described as Aconitase C-terminal domain (PF00694)

Structural Feature(s):
Feature Type  Start  Stop
uncleavable N-terminal sequence N-terminal sequence  
1  
44

PDB Hit:
pdb|5ACN|5ACN ACONITASE (E.C.4.2.1.3) (INACTIVE (3FE-4S) 43.4 4e-05
pdb|1ACO|1ACO ACONITASE (MITOCHONDRIAL) (E.C.4.2.1.3) COMPLEX 42.6 6e-05
pdb|1AMI|1AMI ACONITASE (E.C.4.2.1.3) COMPLEXED WITH 42.6 6e-05
pdb|1B0J|1B0J-A CRYS

Gene Protein Sequence:
MKAFTKITAIVAPLDRSNVDTDAIIPKQFLKSIKRSGFGPNAFDEWRYLD
HGEPGMDNGKRPLNPDFSLNQPRYQGAQILLTRKNFGCGSSREHAPWALD
DYGFRAIIAPSFADIFFNNCYKNGLLPIVLTEEQVDRLFKEVEANEGYRL
SIDLAEQTLTTPGGETFTFDITEHRKHCLLNGLDEIGLTLQHADKIKAFE
EKRRQSQPWLFNG

Gene Nucleotide Sequence:  Sequence Viewer
ATGAAAGCCTTTACCAAAATCACCGCCATCGTCGCCCCGCTCGACCGCAG
CAACGTCGATACCGATGCCATCATCCCCAAACAATTTCTGAAATCCATCA
AACGCAGCGGCTTCGGCCCCAACGCCTTTGACGAATGGCGTTACCTCGAC
CACGGCGAACCGGGCATGGACAACGGCAAACGCCCGTTGAACCCCGATTT
TTCCCTGAACCAGCCGCGTTACCAAGGCGCGCAAATCCTGTTGACGCGTA
AAAACTTCGGTTGCGGCTCTTCACGCGAACATGCCCCTTGGGCATTGGAC
GACTACGGCTTCCGCGCCATTATCGCCCCCAGCTTCGCCGACATCTTCTT
TAACAACTGCTACAAAAACGGCCTTTTGCCCATCGTGTTGACCGAAGAAC
AAGTCGACCGGCTTTTCAAAGAAGTCGAAGCCAACGAAGGCTATCGGCTC
TCCATCGACCTTGCCGAGCAAACCCTGACCACCCCGGGCGGCGAAACATT
CACATTCGACATTACCGAACACCGCAAACACTGCCTCTTAAACGGCTTGG
ACGAAATCGGACTGACCCTGCAACACGCCGACAAAATTAAAGCCTTTGAA
GAAAAACGCCGCCAAAGCCAGCCTTGGCTGTTTAACGGT


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