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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR0766 IGR0764 IGR0771 IGR0768 IGR0767 IGR0765 IGR0770 IGR0763 IGR0772 IGR0769 NG0927 NG0924 NG0919 dhsC, - NG0923 sdhB,dhsB, - NG0920 prxII, - NG0926 metF, - NG0929 cisY,gltA, - NG0918 dldH, - NG0925 dhsA,sdhA, - NG0921 metE, - NG0928 NG0927 NG0924 NG0919 dhsC, - NG0923 sdhB,dhsB, - NG0920 prxII, - NG0926 metF, - NG0929 cisY,gltA, - NG0918 dldH, - NG0925 dhsA,sdhA, - NG0921 metE, - NG0928 NG0927 sdhB,dhsB, - NG0920 prxII, - NG0926 metF, - NG0929 cisY,gltA, - NG0918 dldH, - NG0925 dhsA,sdhA, - NG0921 metE, - NG0928 dhsD, - NG0922 dhsC, - NG0923 NG0919 dhsD, - NG0922 NG0924
* Calculated from Protein Sequence

Gene ID: NG0925

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
dldH  

Definition:
dihydrolipoamide dehydrogenase (E3 component of the pyruvate complex)

Gene Start:
905825

Gene Stop:
904425

Gene Length:
1401

Molecular Weight*:
50822

pI*:
6.40

Net Charge*:
-5.97

EC:
1.8.1.4  

Functional Class:
Energy metabolism; Pyruvate dehydrogenase  

Pathway: pathway table
Citrate cycle (TCA cycle)
Glycine, serine and threonine metabolism
Glycolysis / Gluconeogenesis
Pyruvate metabolism

Secondary Evidence:
Packman,L.C. and Perham,R.N.
An amino acid sequence in the active site of lipoamide dehydrogenase from Bacillus stearothermophilus.
FEBS Lett. 139 (2): 155-158 (1982)
[Medline: 82187191].

Mande,S.S., Sarfaty,S., Allen,M.D., Perham,R.N. and Hol,W.G. Protein-protein interactions in the pyruvate dehydrogenase multienzyme complex: dihydrolipoamide dehydrogenase complexed withthe binding domain of dihydrolipoamide acetyltransferase. Structure 4 (3): 277-286 (1996)
[Medline: 96398614].

Comment:
From GenBANK (gi:7531099): The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). The reaction: dihydrolipoamide + NAD(+) = lipoamide + NADH, with a cofactor, FAD. This cytoplasmic protein has an active site, a redox-active disulfide bond, and
belongs to the pyridine nucleotide-disulfide oxidoreductases class-I.

See other E3 components: NG0915 and NG0562. See E2 components: NG0564, NG0916, and NG0917. See also E1 component: NG0565.

Oklahoma ID: NGO.925c

Blast Summary:  PSI-Blast Search
NG0925 is orthologous to AL162755, N. meningitidis Z2491 putative dihydrolipoamide dehydrogenase: residues 1-467 have 97% similarity to residues 1-467 in NG0925.

Numerous significant hits in gapped BLAST to dihydrolipoamide dehydrogenases; e.g. residues 4-452 are 28% similar to 118672 of Bacillus subtilis.

COGS Summary:  COGS Search
BeTs to 11 clades of COG1249
COG name: Dihydrolipoamide dehydrogenase/glutathione oxidoreductase and related enzymes
Functional Class:  C
The phylogenetic pattern of COG1249 is amt-YqvCEBRH--gp--inX
Number of proteins in this genome belonging to this COG is 3

Blocks Summary:  Blocks Search
***** PR00368 (FAD-dependent pyridine nucleotide reductase signature) with a combined E-value of 5e-23.
    PR00368A    7-29
    PR00368B    139-148
    PR00368C    175-200
    PR00368D    262-276
    PR00368E    306-313
***** IPB000103 (Pyridine nucleotide-disulphide oxidoreductase class-II) with a combined E-value of 1.9e-13.
    IPB000103A    7-27
    IPB000103C    164-212
    IPB000103D    263-274
    IPB000103E    301-338


ProDom Summary:  Protein Domain Search
Residues 8-458 are 27% similar to a (OXIDOREDUCTASE FLAVOPROTEIN FAD REDUCTASE REDOX-ACTIVE) protein domain (PD000139) which is seen in O34324_BACSU.



Paralogs:  Local Blast Search


NG0925 is paralogously related to NG0915 (dihydrolipoamide dehydrogenase E3 component) (3e-38) and NG0562 (dihydrolipoamide dehydrogenase (pyruvate dehydrogenase, E3 component, lipoamide dehydrogenase) (glycine cleavage system L protein)) (3e-30).


Pfam Summary:  Pfam Search
Residues 7 to 321 (E-value = 2.6e-46) place NG0925 in the Pyr_redox family which is described as Pyridine nucleotide-disulphide oxidoreductase (PF00070)
Residues 347 to 458 (E-value = 2.2e-18) place NG0925 in the Pyr_redox_dim family which is described as Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain (PF02852)

Structural Feature(s):
Feature Type  Start  Stop
cleavable N-terminal sequence  
1  
60
non-globular  
176  
269
transmembrane  
195  
211

PDB Hit:
pdb|1EBD|1EBD-A DIHYDROLIPOAMIDE DEHYDROGENASE COMPLEXED WITH 170.0 5e-43
pdb|1JEH|1JEH-A CRYSTAL STRUCTURE OF YEAST E3, LIPOAMIDE 145.0 1e-35
pdb|1LPF|1LPF-A DIHYDROLIPOAMIDE DEHYDROGENASE (E.C.1.8.1.4) 138.0 2e-33
pdb|1DXL|1DXL-A DIHY

Gene Protein Sequence:
MKKIQADIVVIGGGTAGMGAFRNARLHSDNVYLIENNVFGTTCARVGCMP
SKLLIAAAEARHHALHTDPFGVHLDKDSIVVNGEEVMRRVKSERDRFVGF
VVTDVEEWPADKRIMGSAKFIDEHTVQIDDHIQIAAKSFVIATGSRPVIL
PQWQSLGDRLIINDDVFSWDTLPKRVAVFGPGVIGLELGQALHRLGVKVE
IFGLGGIIGGISDPVVSDEAKAVFGEELKLHLDAKTEVKLDADGNVEVHW
EQDGEKGVFVAEYMLAAVGRRPNVDNIGLENINIDKDARGVPVADPLTMQ
TSIPHIFIAGDASNQLPLLHEAADQGKIAGDNAGRYPNIGSGLRRSTIGV
VFTSPQIGFVGLKYAQVAAQYQADEFVIGEVSFKNQGRSRVMLVNKGHMR
LYAEKATGRFIGAEIVGPAAEHLAHLLAWAHQMKMTVPQMLDMPFYHPVI
EEGLRTALRDADAKLKA

Gene Nucleotide Sequence:  Sequence Viewer
ATGAAAAAAATTCAAGCGGATATCGTCGTAATCGGCGGCGGTACTGCCGG
TATGGGTGCGTTTCGCAATGCCCGTTTACATTCGGATAATGTTTACCTGA
TTGAAAACAATGTGTTCGGCACAACCTGCGCGCGCGTGGGCTGTATGCCT
TCCAAACTCTTGATTGCCGCCGCAGAAGCGCGTCACCACGCATTGCATAC
CGACCCCTTCGGCGTGCATTTGGACAAAGACAGCATCGTCGTCAACGGAG
AAGAGGTTATGCGGCGCGTCAAATCCGAGCGCGACCGTTTTGTCGGCTTT
GTCGTTACCGATGTGGAAGAATGGCCTGCCGACAAGCGCATCATGGGCTC
GGCTAAATTCATCGACGAGCATACCGTCCAAATCGACGACCATATCCAAA
TTGCGGCAAAAAGTTTCGTGATTGCTACCGGTTCGCGTCCCGTCATCCTG
CCGCAGTGGCAGTCTTTGGGCGACCGTTTGATTATCAACGACGACGTTTT
CTCGTGGGATACGCTGCCTAAGCGCGTTGCCGTGTTCGGGCCGGGCGTTA
TCGGTTTGGAACTGGGTCAGGCATTGCACCGTTTGGGTGTGAAAGTTGAA
ATTTTCGGTTTGGGCGGAATCATCGGCGGCATTTCCGACCCCGTTGTTTC
AGACGAGGCGAAAGCCGTGTTCGGAGAAGAATTGAAACTGCATCTGGATG
CTAAAACCGAGGTCAAACTCGACGCAGACGGCAATGTAGAAGTCCATTGG
GAGCAGGATGGCGAAAAAGGCGTATTTGTTGCCGAATATATGTTGGCAGC
CGTAGGTCGCCGTCCGAACGTTGACAATATCGGTTTGGAAAACATCAATA
TCGACAAAGACGCGCGCGGCGTACCCGTTGCCGATCCGCTGACCATGCAG
ACCAGCATTCCGCATATCTTTATTGCGGGCGACGCGTCCAACCAACTGCC
CCTGCTGCATGAAGCCGCCGACCAAGGTAAGATTGCCGGCGATAACGCGG
GCCGCTACCCGAATATCGGCAGCGGTTTGCGCCGCAGCACCATTGGCGTG
GTGTTTACCAGTCCGCAAATCGGCTTTGTCGGTTTGAAATACGCGCAGGT
TGCCGCGCAATACCAAGCCGACGAATTTGTCATCGGCGAAGTATCGTTCA
AAAATCAAGGTCGCAGCCGCGTGATGCTGGTAAACAAAGGCCATATGCGC
CTGTATGCCGAAAAAGCCACCGGCCGCTTTATCGGCGCGGAAATCGTAGG
CCCTGCCGCCGAACATTTGGCTCACTTGTTGGCATGGGCGCATCAAATGA
AGATGACCGTTCCGCAAATGCTGGATATGCCGTTCTACCATCCTGTTATC
GAGGAAGGTCTGCGTACCGCGTTGCGCGATGCCGATGCGAAATTGAAAGC
C


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