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

Haemophilus ducreyi Search Results

Record: 1 of 1  
MiniMap tRNA-Cys-1 tRNA-Gly-4 IGR1183 IGR1184 IGR1181 IGR1186 IGR1185 IGR1182 prsA, - HD1627 HD1621 pyrD, - HD1626 lpdA, - HD1623 HD1619 aceF,acoC, - HD1624 aceE, - HD1625 prsA, - HD1627 HD1621 pyrD, - HD1626 lpdA, - HD1623 HD1619 aceF,acoC, - HD1624 aceE, - HD1625 pyrD, - HD1626 lpdA, - HD1623 HD1619 aceF,acoC, - HD1624 aceE, - HD1625 HD1622 HD1622 HD1621
* Calculated from Protein Sequence

Gene ID: HD1624

DNA Molecule Name:
1  

Genbank ID:
0

Gene Name:
aceF  acoC  

Definition:
pyruvate dehydrogenase complex E2 component/dihydrolipoamide acetyltransferase

Gene Start:
1343687

Gene Stop:
1342116

Gene Length:
1572

Molecular Weight*:
55641

pI*:
5.80

Net Charge*:
-5.31

EC:
2.3.1.12  2.3.1.61  

Functional Class:
Energy metabolism; Pyruvate dehydrogenase  

Pathway: pathway table
Carbohydrate Metabolism; Citrate cycle (TCA cycle)
Carbohydrate Metabolism; Glycolysis / Gluconeogenesis
Carbohydrate Metabolism; Pyruvate metabolism

Secondary Evidence:
Rae,J.L., Cutfield,J.F. and Lamont,I.L.
Sequences and expression of pyruvate dehydrogenase genes from Pseudomonas aeruginosa.
J. Bacteriol. 179(11): 3561-3571, 1997.
Medline: 97315227.

Hein,S. and Steinbuchel,A.
Biochemical and molecular characterization of the Alcaligenes eutrophus pyruvate dehydrogenase complex and identification of a new type of dihydrolipoamide dehydrogenase.
J. Bacteriol. 176(14): 4394-4408, 1994.
Medline: 94292470.

Westphal,A.H. and de Kok,A. 1990. The 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. 2. Molecular cloning and sequence analysis of the gene encoding the succinyltransferase component. Eur. J. Biochem. 187(1): 235-239. Medline: 90126825.

Carlsson,P. and Hederstedt,L. 1989. Genetic characterization of Bacillus subtilis odhA and odhB, encoding 2-oxoglutarate dehydrogenase and dihydrolipoamide transsuccinylase, respectively. J. Bacteriol. 171(7): 3667-3672. Medline: 89291708.

Stephens,P.E., Darlison,M.G., Lewis,H.M. and Guest,J.R. 1983. The pyruvate dehydrogenase complex of Escherichia coli K12. Nucleotide sequence encoding the dihydrolipoamide acetyltransferase component. Eur. J. Biochem. 133(3): 481-489. Medline: 83234434.

Comment:
0

Blast Summary:  PSI-Blast Search
Several significant hits using gapped BLAST to dihydrolipoamide acetyltransferase sequences from H. influenzae (1171889), E. coli (129056), P. aeruginosa (2499414), Ralstonia (Alcaligenes) eutropha (2499412), among others.

HD1624 is similar to dihydrolipoamide succinyltransferases from C. pneumoniae (CPn0527 & CPn0377) and C. trachomatis (CT400 & CT055).
It is also similar to dihydrolipoamide acetyltransferases from M. pneumoniae (MP0447), M. genitalium (MG272), C. pneumoniae (CPn0306), and C. trachomatis (CT247). No similarity to proteins from U. urealyticum or T. pallidum.


COGS Summary:  COGS Search
BeTs to 8 clades of COG0508
COG name: Dihydrolipoamide acyltransferases
Functional Class:  C
The phylogenetic pattern of COG0508 is ----Y--cEBRH--gp--INX
Number of proteins in this genome belonging to this COG is 2

Blocks Summary:  Blocks Search
***** IPB001078 (2-Oxo acid dehydrogenase acyltransferase catalytic domain) with a combined E-value of 1.1e-92.
    IPB001078A    113-145
    IPB001078B    221-251
    IPB001078C    349-370
    IPB001078D    426-468
    IPB001078E    487-523
    IPB001078A    57-89
    IPB001078A    72-104
***** IPB003016 (2-oxo acid dehydrogenases acyltransferase component lipoyl binding site) with a combined E-value of 1.2e-17.
    IPB003016    116-150
    IPB003016    23-57
    IPB003016    60-94
***** IPB000089 (Biotin / Lipoyl attachment) with a combined E-value of 6.4e-16.
    IPB000089A    388-407
    IPB000089B    442-461
***** IPB002215 (HlyD family secretion protein) with a combined E-value of 2.1e-06.
    IPB002215A    40-76
    IPB002215B    138-172


ProDom Summary:  Protein Domain Search
Residues 109-168 are 90% similar to a (BIOTIN DIHYDROLIPOAMIDE LIPOYL CARBOXYLASE TRANSFERASE) protein domain (PD000268) which is seen in Q9CMD6_PASMU.

Residues 256-301 are 70% similar to a (DIHYDROLIPOAMIDE PYRUVATE LIPOYL PROTEOME) protein domain (PD073029) which is seen in ODP2_HAEIN.

Residues 252-301 are 60% similar to a (GLYCOLYSIS COMPONENT TRANSFERASE PYRUVATE) protein domain (PD405849) which is seen in ODP2_ECOLI.

Residues 303-523 are 91% similar to a (DIHYDROLIPOAMIDE TRANSFERASE LIPOYL DEHYDROGENASE E2) protein domain (PD001115) which is seen in Q9CMD6_PASMU.

Residues 217-251 are 91% similar to a (DIHYDROLIPOAMIDE TRANSFERASE LIPOYL E2 ACYLTRANSFERASE) protein domain (PD001730) which is seen in ODP2_HAEIN.



Paralogs:  Local Blast Search

HD1624 is paralogously related to HD1334 (3e-47), HD1513 (1e-04) and HD0783 (1e-04).


Pfam Summary:  Pfam Search
Residues 3 to 74 (E-value = 6.9e-26) place HD1624 in the Biotin_lipoyl family which is described as Biotin-requiring enzyme (PF00364)
Residues 96 to 167 (E-value = 8.6e-28) place HD1624 in the Biotin_lipoyl family which is described as Biotin-requiring enzyme (PF00364)
Residues 219 to 255 (E-value = 5.6e-17) place HD1624 in the E3_binding family which is described as e3 binding domain (PF02817)
Residues 290 to 523 (E-value = 1e-117) place HD1624 in the 2-oxoacid_dh family which is described as 2-oxoacid dehydrogenases acyltransferase (catalytic domain) (PF00198)

PDB Hit:
pdb|1DPC| Dihydrolipoyl Transacetylase (E.C.2.3.1.12) (Catal... 278 1e-075
pdb|1DPD| Dihydrolipoyl Transacetylase (E.C.2.3.1.12) (Catal... 275 9e-075
pdb|1EAF| Dihydrolipoyl Transacetylase (E.C.2.3.1.12) (Catal... 275 1e-074

Gene Protein Sequence:
MSKQINVPDIGGDEVTVTEVMVNVGDTITIDQSIINVEGDKASMEVPAPE
AGVVKQVLVKVGDKVTTGSAMLVLETADAVPQASAPVAASVASAIVEVNV
PDIGGDEVNVTEIMVKVGDAVEVDQSIINVEGDKASMEVPAPFAGVVKEI
LVRSGDKVSTGSLIMKFEVAGAAPAPASATVAPTAVVAPTTNHTQSAKEQ
GQSSLSQAQVEASSVFAHATPVIRRLAREFGVNLDKVKGSGRKGRIIKED
LQAYVKTAVQVFEQQGGTTVSASGAGLGLLPWPKVDFSKFGEVEEVELSR
INKISGANLHRNWVMIPHVTHFDRTDITALEEFRKEQNKLAEKQKLDVKI
TPVVFIMKAVAKALEAFPRFNSSLSEDAQRLTLKKYINIGVAVDTPNGLV
VPVFKNVNKKGIIELSRELMEVSKKARDGKLTASDMQGGCFTISSLGGIG
TTHFTPIVNAPEVAILGVSKSETLPVWNGKEFTPRLMLPLSLSFDHRVID
GADGARFLSYINGVLADIRRLVM$

Gene Nucleotide Sequence:  Sequence Viewer
ATGTCAAAACAAATTAATGTGCCAGATATTGGTGGTGATGAAGTTACCGT
AACAGAAGTAATGGTTAATGTTGGCGATACTATTACAATTGATCAATCAA
TTATTAATGTGGAAGGTGATAAGGCCTCAATGGAAGTGCCAGCACCTGAA
GCGGGCGTAGTAAAACAAGTATTAGTTAAAGTGGGTGATAAAGTCACGAC
CGGTTCAGCGATGCTCGTGTTAGAAACGGCAGATGCCGTACCGCAAGCTT
CAGCTCCGGTTGCTGCTTCAGTGGCATCAGCTATTGTTGAAGTAAATGTA
CCTGATATTGGTGGTGACGAAGTGAATGTTACCGAAATTATGGTAAAAGT
AGGTGATGCAGTTGAAGTTGATCAATCAATTATCAATGTAGAAGGGGATA
AAGCCTCAATGGAAGTGCCAGCACCATTTGCGGGTGTAGTAAAAGAAATT
TTAGTCAGATCAGGTGATAAAGTCTCAACCGGTTCATTAATTATGAAATT
TGAAGTAGCGGGTGCGGCTCCAGCTCCAGCTTCTGCAACTGTTGCACCAA
CCGCGGTAGTTGCGCCTACAACAAATCATACTCAGTCTGCTAAAGAACAA
GGGCAATCAAGTTTAAGCCAAGCACAAGTAGAAGCAAGTTCAGTATTTGC
GCATGCTACTCCAGTTATTCGCCGTTTAGCGCGTGAATTTGGCGTAAATT
TAGATAAAGTTAAAGGTTCAGGCCGTAAAGGGCGTATTATTAAAGAAGAT
CTTCAAGCATACGTTAAAACAGCTGTTCAAGTATTTGAACAACAAGGTGG
AACGACAGTAAGCGCAAGCGGAGCGGGTCTAGGTTTATTACCATGGCCAA
AAGTTGACTTTAGCAAATTCGGCGAAGTTGAAGAAGTTGAATTAAGTCGT
ATTAATAAAATTTCTGGTGCAAACTTACATCGCAACTGGGTTATGATTCC
ACATGTAACGCATTTTGATCGCACTGATATCACTGCACTTGAAGAGTTCC
GTAAAGAACAAAATAAACTAGCAGAAAAACAGAAATTAGACGTCAAAATC
ACACCGGTTGTATTCATTATGAAAGCCGTTGCAAAAGCATTAGAAGCATT
CCCTCGTTTCAATAGCTCACTTTCTGAAGATGCACAACGTTTAACACTTA
AAAAATATATTAATATTGGCGTAGCAGTAGATACACCAAATGGTCTAGTC
GTACCTGTGTTTAAAAATGTGAATAAAAAAGGTATTATTGAACTTTCTCG
TGAGTTAATGGAAGTATCTAAGAAAGCACGTGATGGCAAATTAACCGCTT
CGGATATGCAAGGTGGATGCTTTACTATCTCAAGTTTAGGCGGTATTGGT
ACAACGCACTTTACGCCAATTGTAAATGCGCCAGAAGTCGCTATTTTAGG
TGTTTCTAAATCTGAAACATTACCGGTATGGAATGGTAAAGAGTTTACTC
CTCGCTTAATGCTTCCATTATCATTATCATTTGACCACCGTGTAATCGAT
GGGGCTGATGGTGCACGCTTCTTAAGCTACATCAACGGCGTATTAGCAGA
CATTCGTCGTTTAGTAATGTAA


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