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Haemophilus ducreyi Search Results

Record: 1 of 1  
MiniMap tRNA-Cys-1 tRNA-Gly-4 IGR1183 IGR1184 IGR1181 IGR1180 IGR1182 HD1621 lpdA, - HD1623 HD1619 aceF,acoC, - HD1624 aceE, - HD1625 HD1621 lpdA, - HD1623 HD1619 aceF,acoC, - HD1624 aceE, - HD1625 HD1621 lpdA, - HD1623 HD1619 aceF,acoC, - HD1624 aceE, - HD1625 HD1622 HD1622
* Calculated from Protein Sequence

Gene ID: HD1623

DNA Molecule Name:
1  

Genbank ID:
0

Gene Name:
lpdA  

Definition:
pyruvate dehydrogenase multienzyme complex, E3/lipoamide dehydrogenase

Gene Start:
1342050

Gene Stop:
1340626

Gene Length:
1425

Molecular Weight*:
50773

pI*:
6.50

Net Charge*:
-4.16

EC:
1.8.1.4  

Functional Class:
Energy metabolism; Pyruvate dehydrogenase  

Pathway: pathway table
Carbohydrate Metabolism; Glycolysis / Gluconeogenesis
Carbohydrate Metabolism; Pyruvate metabolism

Secondary Evidence:
Stephens,P.E., Lewis,H.M., Darlison,M.G. and Guest,J.R.
Nucleotide sequence of the lipoamide dehydrogenase gene of Escherichia coli K12.
Eur. J. Biochem. 135(3): 519-527, 1983.
Medline: 84004369.

Cunningham L, Georgellis D, Green J, Guest JR.
Co-regulation of lipoamide dehydrogenase and 2-oxoglutarate dehydrogenase synthesis in Escherichia coli: characterisation of an ArcA binding site in the lpd promoter.
FEMS Microbiol Lett. 1998 Dec 15;169(2):403-8.
PMID: 9868788

Guillen G, Alvarez A, Silva R, Morera V, Gonzalez S, Musacchio A, Besada V, Coizeau E, Caballero E, Nazabal C, Carmenate T, Gonzalez LJ, Estrada R, Tambara Y, Padron G, Herrera L.
Expression in Escherichia coli of the lpdA gene, protein sequence analysis and immunological characterization of the P64k protein from Neisseria meningitidis.
Biotechnol Appl Biochem. 1998 Jun;27 ( Pt 3):189-96.
PMID: 9664678


Comment:
0

Blast Summary:  PSI-Blast Search
Several significant hits using gapped BLAST to dihydrolipoamide dehydrogenases from H. influenzae (1169352), E. coli (118673) and V. parahaemolyticus (7531098), among others.

HD1623 is similar a pyruvate dehydrogenase E3 component from C. trachomatis (CT557), a lipoamide dehydrogenase from C. pneumoniae (CPn0833), a dihydrolipoamide dehydrogenase component E3 from M. genitalium (MG271), a dihydrolipoamide dehydrogenase from M. pneumoniae (MP0448), a thioredoxin reductase from T. pallidum (TP0814), a NADH oxidase/NADH peroxidase from T. pallidum (TP0921), a NADH oxidase from M. pneumoniae (MP0444), a NADPH thioredoxin reductase from C. trachomatis (CT099) and C. pneumoniae (CPn0314), and a glutamate synthase from T. pallidum (TP0735). No similarity to sequences from U. urealyticum.

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 2

Blocks Summary:  Blocks Search
***** PR00368 (FAD-dependent pyridine nucleotide reductase signature) with a combined E-value of 8.3e-34.
    PR00368A    8-30
    PR00368B    142-151
    PR00368C    178-203
    PR00368D    265-279
    PR00368E    308-315
***** IPB000103 (Pyridine nucleotide-disulphide oxidoreductase class-II) with a combined E-value of 1.1e-15.
    IPB000103A    8-28
    IPB000103D    266-277
    IPB000103E    303-340
***** IPB001100 (Pyridine nucleotide-disulphide oxidoreductase, class I) with a combined E-value of 2.3e-10.
    IPB001100    42-56
***** IPB000171 (Bacterial-type phytoene dehydrogenase) with a combined E-value of 2.3e-08.
    IPB000171A    10-40
    IPB000171A    180-210


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

Paralogs:  Local Blast Search
HD1623 is paralogously related to HD0354 (6e-43) and HD0333 (2e-04).


Pfam Summary:  Pfam Search
Residues 8 to 323 (E-value = 1e-96) place HD1623 in the Pyr_redox family which is described as Pyridine nucleotide-disulphide oxidoreductase (PF00070)
Residues 347 to 456 (E-value = 1.1e-50) place HD1623 in the Pyr_redox_dim family which is described as Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain (PF02852)

PDB Hit:
pdb|1BHY| Low Temperature Middle Resolution Structure Of P64... 493 2e-140
pdb|1OJT| Structure Of Dihydrolipoamide Dehydrogenase 493 2e-140
pdb|1EBD|A Chain A, Dihydrolipoamide Dehydrogenase Complexed Wi... 322 7e-089

Gene Protein Sequence:
MSKEIKTQVVVLGAGPAGYSAAFRCADLGLETVIVERYSTLGGVCLNVGC
IPSKALLHVAKVIEEAKHADKNGITFGEPIIDLDKVRKGKEAVVSKLTGG
LAGMAKARKVTVVEGLAAFTDSHTLVARDRDGNPTTIKFDNAIIAGGSRP
IELPFIPHEDPRIWNSTDALKLKEIPKKLLIMGGGIIGLEMGTVYQSLGS
EIEVVEMFDQVIPAADKDVVSIYSKQVEKKFKLMLETKVTAVKAEDDGIY
VSMEGKACNDTKRYDAVLVAIGRVPNGKLIDVGKAGVEVDERGFIHTDKQ
MRTNVPHIFAIGDVVGQPMLAHKGVHEGHVAAEVIAGKKRYFDPKVIPSI
AYTEPEVAWVGKTEKECKQEGLNYEVAKFPWAASGRAIASECSEGMTKLI
FDKDTHRLLGGAIVGSNGGELLGEIGLAIEMGCDAEDIALTIHAHPTLHE
SVGLAAEVFEGSITDLPNAKAKKR$

Gene Nucleotide Sequence:  Sequence Viewer
ATGAGTAAAGAAATTAAAACCCAAGTTGTTGTACTTGGTGCGGGCCCTGC
AGGTTATTCTGCAGCATTCCGTTGTGCAGATTTAGGTTTAGAAACGGTTA
TTGTTGAACGTTATTCAACATTAGGTGGTGTATGTTTAAATGTAGGGTGT
ATTCCTTCAAAAGCATTATTACACGTTGCTAAAGTGATTGAAGAAGCAAA
ACATGCGGATAAAAATGGTATTACATTCGGTGAACCAATCATTGATTTAG
ATAAAGTCCGTAAGGGTAAAGAAGCCGTAGTGTCAAAATTGACCGGTGGT
TTAGCGGGTATGGCTAAAGCGCGTAAAGTGACGGTTGTAGAAGGTTTAGC
GGCATTTACCGATTCGCATACCCTAGTTGCACGTGATCGAGATGGCAATC
CGACGACAATTAAATTTGATAATGCCATTATTGCAGGGGGTTCTCGCCCT
ATTGAATTACCATTTATTCCACACGAGGATCCTCGTATTTGGAACTCTAC
CGATGCACTTAAATTAAAAGAAATTCCGAAAAAACTTTTAATTATGGGCG
GTGGAATTATCGGCTTAGAAATGGGAACTGTATATCAATCACTAGGATCA
GAGATTGAAGTGGTTGAAATGTTTGATCAAGTTATCCCGGCGGCAGATAA
AGATGTTGTTTCAATTTATAGCAAACAAGTTGAGAAAAAATTCAAGTTAA
TGCTTGAAACCAAAGTAACGGCAGTAAAAGCGGAAGATGATGGTATTTAT
GTCTCAATGGAAGGCAAGGCTTGTAATGATACTAAGCGTTATGATGCTGT
TTTAGTTGCTATTGGCCGTGTACCAAATGGTAAATTGATCGATGTGGGTA
AAGCGGGCGTAGAAGTAGATGAACGCGGTTTTATTCATACTGATAAACAA
ATGCGTACTAATGTACCACATATTTTCGCTATCGGTGACGTTGTTGGCCA
ACCAATGCTAGCACATAAAGGTGTACACGAAGGTCATGTTGCTGCGGAAG
TTATTGCAGGAAAAAAACGTTATTTCGATCCAAAAGTAATTCCTTCAATT
GCTTATACCGAACCTGAAGTGGCTTGGGTGGGTAAAACAGAAAAAGAATG
TAAACAAGAAGGATTAAACTATGAAGTGGCTAAATTCCCTTGGGCTGCTT
CTGGACGTGCAATTGCTTCAGAATGTTCTGAAGGAATGACGAAATTAATC
TTTGATAAAGATACTCACCGCTTATTAGGTGGGGCAATCGTTGGTTCAAA
TGGCGGTGAATTACTAGGAGAAATTGGCTTAGCAATCGAAATGGGTTGCG
ATGCAGAAGATATTGCCTTAACTATTCATGCACACCCAACTTTACATGAA
TCCGTTGGTTTAGCCGCAGAAGTATTTGAAGGATCTATTACAGATTTACC
AAATGCGAAAGCAAAAAAACGCTAA


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