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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR0756 IGR0757 IGR0758 IGR0761 IGR0759 IGR0756.1 IGR0760 IGR0756.2 NG0914 NG0910 tpn, - NG0909 sucD, - NG0912 sucC, - NG0913 sucB, - NG0916 dldH, - NG0915 sucA, - NG0917 NG0911 NG0914 NG0910 tpn, - NG0909 sucD, - NG0912 sucC, - NG0913 sucB, - NG0916 dldH, - NG0915 sucA, - NG0917 NG0911 Type: direct, Name:  - 117 NG0914 tpn, - NG0909 sucD, - NG0912 sucC, - NG0913 sucB, - NG0916 dldH, - NG0915 sucA, - NG0917 NG0910 NG0911
* Calculated from Protein Sequence

Gene ID: NG0915

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
dldH  

Definition:
dihydrolipoamide dehydrogenase E3 component

Gene Start:
894608

Gene Stop:
893178

Gene Length:
1431

Molecular Weight*:
50068

pI*:
6.30

Net Charge*:
-5.26

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

Primary Evidence:
Porcella,S.F., Belland,R.J. and Judd,R.C.,
The sucAB-lpd operon of Neisseria gonorrhoeae,
Unpublished

Secondary Evidence:
Hein,S. and Steinbuchel,A. Cloning and characterization of the Alcaligenes eutrophus 2-oxoglutarate dehydrogenase complex. FEMS Microbiol. Lett. 136 (3): 231-238 (1996) [Medline: 97021018].

Palmer,J.A., Hatter,K. and Sokatch,J.R. Cloning and sequence analysis of the LPD-glc structural gene of Pseudomonas putida. J. Bacteriol. 173 (10): 3109-3116 (1991) [Medline: 91216982].

Burns,G., Sykes,P.J., Hatter,K. and Sokatch,J.R. Isolation of a third lipoamide dehydrogenase from Pseudomonas putida. J. Bacteriol. 171 (2): 665-668 (1989) [Medline: 89123137].

Comment:
Oklahoma ID: NGO.915c

The glycine cleavage system comprises four proteins: P,T,L and H.
The P protein is NG1325, the T protein is NG1406 and the H protein is NG1404. The L component may be NG0915.

From GenBANK (gi:1706443): 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). It performs by the reaction: dihydrolipoamide + NAD(+) = lipoamide + NADH, with a cofactor, FAD. The active site is a redox-active disulfide bond. It belongs to the pyridine nucleotide-disulfide oxidoreductases class-I.

Blast Summary:  PSI-Blast Search
NG0915 is 97% identical to a previously sequenced Neisseria gonorrhoeae protein in GenBank, 790864, submitted as L36381, "putative" by Porcella,S.F., Belland,R.J. and Judd,R.C.

Numerous significant hits in gapped BLAST to dihydrolipoamide dehydrogenases; e.g. residues 3-473 are 62% similar to 1588696 of Ralstonia eutropha.

NG0915 is orthologous to AE002447, N. meningitidis MC58 2-oxoglutarate dehydrogenase, E3 component, lipoamide dehydrogenase : residues 1-477 have 99% similarity to residues 1-477 in NG0915.

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 4.4e-47.
    PR00368A    5-27
    PR00368B    150-159
    PR00368C    186-211
    PR00368D    276-290
    PR00368E    319-326
    PR00368C    5-30
***** IPB000103 (Pyridine nucleotide-disulphide oxidoreductase class-II) with a combined E-value of 5.8e-18.
    IPB000103A    5-25
    IPB000103D    277-288
    IPB000103E    314-351
***** IPB001100 (Pyridine nucleotide-disulphide oxidoreductase, class I) with a combined E-value of 1.3e-10.
    IPB001100    46-60
***** IPB000171 (Bacterial-type phytoene dehydrogenase) with a combined E-value of 2e-08.
    IPB000171A    7-37
    IPB000171A    188-218


ProDom Summary:  Protein Domain Search
No significant hit to the ProDom database.

Paralogs:  Local Blast Search


NG0915 is paralogously related to NG0562 (dihydrolipoamide dehydrogenase (pyruvate dehydrogenase, E3 component, lipoamide dehydrogenase) (glycine cleavage system L protein)) (6e-89), NG0925 (dihydrolipoamide dehydrogenase (E3 component of the pyruvate complex)) (3e-38) and NG0580 (thioredoxin reductase) (1e-05).


Pfam Summary:  Pfam Search
Residues 5 to 334 (E-value = 1.4e-100) place NG0915 in the Pyr_redox family which is described as Pyridine nucleotide-disulphide oxidoreductase (PF00070)
Residues 358 to 467 (E-value = 6.4e-54) place NG0915 in the Pyr_redox_dim family which is described as Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain (PF02852)

Structural Feature(s):
Feature Type  Start  Stop
non-globular  
1  
59
cleavable N-terminal sequence  
1  
19

PDB Hit:
pdb|1LPF|1LPF-A DIHYDROLIPOAMIDE DEHYDROGENASE (E.C.1.8.1.4) 499.0 0e+00
pdb|3LAD|3LAD-A DIHYDROLIPOAMIDE DEHYDROGENASE (E.C.1.8.1.4) 481.0 0e+00
pdb|1DXL|1DXL-A DIHYDROLIPOAMIDE DEHYDROGENASE OF GLYCINE 459.0 0e+00
pdb|1JEH|1JEH-A CRYS

Gene Protein Sequence:
MSQYDVVVIGAGPGGYVAAIRAAQLGFKTACVDAGVNKAGNAPALGGTCL
NVGCIPSKALLQSSEHFHAAQHDFAEHGITVGDVKFDAAKMIERKDAIVT
KLTGGVKFLFQKNKVTSLFGTASFAGKNGDAYQIEVDNKGEKTVIEAKHV
IVATGSVPRPLPQVAIDNVNVLDNEGALNLTEVPAKLGVIGSGVIGLEMG
SVWNRVGAEVTILEAAPTFLAAADQQIAKEAFKYFTKEQGLSIELGVKIG
DIKSEGKGVSVAYETAAGEAKTEVFDKLIVAIGRIPNTKGLNAEAVGLEK
DERGFIKVDGECRTNLPNVWAIGDVVRGPMLAHKASDEGVAVAERIAGQK
PHIDFNNVPFVIYTDPEIAWVGKTEEQLKAEGVEYKKGTSGFGANGRALA
MGKAKGTVKVLADAKTDRILGVHMIGPVVSELVTEGVTALEFFASSEDIA
RIIHAHPTLSEVVHEAALAADKRALHG

Gene Nucleotide Sequence:  Sequence Viewer
ATGTCTCAATATGATGTAGTAGTGATTGGTGCAGGTCCGGGCGGATACGT
TGCCGCCATCCGTGCCGCACAACTGGGTTTCAAAACTGCCTGTGTCGATG
CAGGCGTTAACAAAGCAGGCAATGCCCCTGCATTGGGCGGTACTTGCTTG
AACGTAGGCTGTATCCCTTCTAAAGCCCTGTTGCAATCCAGCGAACATTT
CCACGCTGCGCAACACGATTTTGCCGAACACGGTATCACTGTCGGCGACG
TAAAATTCGACGCGGCCAAAATGATTGAGCGCAAAGATGCCATCGTGACC
AAACTGACCGGCGGCGTGAAATTCCTGTTCCAAAAAAACAAAGTAACCAG
CCTGTTCGGTACTGCTTCCTTTGCCGGTAAAAATGGCGATGCTTACCAAA
TTGAAGTCGATAACAAAGGCGAGAAAACCGTTATCGAAGCCAAACACGTC
ATCGTAGCAACCGGTTCCGTACCGCGTCCGTTGCCGCAAGTCGCTATCGA
CAACGTGAACGTATTGGACAACGAAGGCGCATTGAACCTGACTGAAGTAC
CTGCCAAACTCGGCGTAATCGGTTCCGGTGTGATTGGTTTGGAAATGGGT
TCCGTATGGAACCGCGTGGGTGCGGAAGTTACCATTCTTGAAGCCGCGCC
GACCTTCCTGGCTGCCGCCGACCAACAAATCGCCAAAGAAGCCTTCAAAT
ACTTCACCAAAGAGCAAGGTCTGAGCATCGAATTGGGTGTGAAAATCGGC
GACATCAAGTCTGAAGGCAAAGGTGTTTCCGTTGCTTACGAAACTGCTGC
CGGCGAAGCCAAAACCGAAGTATTCGACAAACTGATCGTTGCCATCGGCC
GTATTCCAAACACCAAAGGCCTGAACGCTGAAGCCGTAGGCTTGGAAAAA
GACGAGCGCGGCTTTATCAAAGTGGATGGCGAATGCCGTACCAACCTGCC
TAACGTATGGGCAATCGGCGACGTGGTTCGCGGCCCGATGTTGGCACACA
AAGCCAGCGACGAAGGCGTTGCCGTTGCCGAGCGCATTGCCGGTCAAAAA
CCGCATATCGACTTCAACAACGTACCGTTTGTGATTTACACCGACCCTGA
AATCGCTTGGGTGGGTAAAACCGAAGAGCAGCTCAAAGCCGAAGGCGTGG
AGTACAAAAAAGGTACTTCAGGTTTCGGTGCAAACGGCCGTGCATTGGCA
ATGGGCAAAGCCAAAGGTACGGTTAAAGTGTTGGCAGATGCCAAAACCGA
CCGTATCTTGGGCGTACACATGATCGGCCCGGTTGTCAGCGAATTGGTTA
CCGAAGGCGTGACTGCGCTCGAATTCTTCGCCAGCAGCGAAGACATCGCC
CGTATTATCCATGCCCACCCAACCTTGTCCGAAGTGGTTCACGAAGCTGC
ATTGGCGGCCGACAAACGCGCTTTGCACGGT


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