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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR0467 IGR0469 IGR0468 IGR0466 IGR0470 NG0563 aceF, - NG0564 lpdA,dldH, - NG0562 aceE, - NG0565 NG0561 drpA,proS, - NG0566 NG0563 aceF, - NG0564 lpdA,dldH, - NG0562 aceE, - NG0565 NG0561 drpA,proS, - NG0566 Type: tandem, Name:  - 29 NG0563 aceF, - NG0564 lpdA,dldH, - NG0562 aceE, - NG0565 NG0561 drpA,proS, - NG0566
* Calculated from Protein Sequence

Gene ID: NG0564

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
aceF  

Definition:
dihydrolipoamide S-acetyltransferase complex (E2 component of pyruvate dehydrogenase complex)

Gene Start:
546031

Gene Stop:
544445

Gene Length:
1587

Molecular Weight*:
54683

pI*:
5.10

Net Charge*:
-10.70

EC:
2.3.1.12  

Functional Class:
Energy metabolism; Pyruvate dehydrogenase  

Pathway: pathway table
Glycolysis / Gluconeogenesis
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:
From GenBANK (gi:1171889): The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA & CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) & lipoamide dehydrogenase (E3). Catalytic activity: acetyl-CoA + dihydrolipoamide = CoA + S-acetyldihydrolipoamide. The E2 component contains two covalently-bound lipoyl cofactors and forms a 24-polypeptide structural core with octahedral symmetry.

From Medline (9429247): The A. eutrophus pyruvate dehydrogenase complex, pdhA, pdhB, and pdhL encodes the pyruvate dehydrogenase (E1), the dihydrolipoamide acetyltransferase (E2), and the dihydrolipoamide dehydrogenase (E3) components, respectively. These genes occur colinearly in one gene cluster in the order pdhA, pdhB, ORF3, and pdhL. Microsequencing of the purified E3 component revealed an amino acid sequence which corresponded to the N-terminal amino acid sequence deduced from the nucleotide sequence of pdhL. The N-terminal region of PdhL comprising amino acids 1 to 112 was distinguished from all other known dihydrolipoamide dehydrogenases. It resembled the N terminus of dihydrolipoamide acyltransferases, and it contained one single lipoyl domain which was separated by an adjacent hinge region from the C-terminal region of the protein that exhibited high homology to classical dihydrolipoamide dehydrogenases.

See also: E1, NG0565, and E3, NG0562.

Oklahoma ID: NGO.564c

Blast Summary:  PSI-Blast Search
Numerous significant hits in gapped BLAST; e.g. residues 5-529 are 51% similar to gb|AAC22885.1| (U32803) dihydrolipoamide acetyltransferase (aceF) of Haemophilus influenzae Rd.

Residues 1-529 are 92% similar to NMA1555 and NMB1342, dihydrolipoamide acetyltransferase E2 component of pyruvate dehydrogenase complex, of N.meningitidis (11257474, 11257476).


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 3.9e-93.
    IPB001078A    22-54
    IPB001078B    231-261
    IPB001078C    357-378
    IPB001078D    432-474
    IPB001078E    493-529
    IPB001078A    160-192
    IPB001078A    59-91
***** IPB000089 (Biotin / Lipoyl attachment) with a combined E-value of 4.4e-17.
    IPB000089A    394-413
    IPB000089B    448-467
***** IPB003016 (2-oxo acid dehydrogenases acyltransferase component lipoyl binding site) with a combined E-value of 3.9e-16.
    IPB003016    126-160
    IPB003016    25-59
    IPB003016    163-197
    IPB003016    62-96


ProDom Summary:  Protein Domain Search
Residues 120-175 are 62% similar to a (BIOTIN DIHYDROLIPOAMIDE PYRUVATE DEHYDROGENASE) protein domain (PD000268) which is seen in Q51225_NEIME.

Residues 312-529 are 68% similar to a (DIHYDROLIPOAMIDE TRANSFERASE DEHYDROGENASE LIPOYL) protein domain (PD001115) which is seen in ODP2_ALCEU.

Residues 109-180 are 45% similar to a (PROTEIN REPEAT PRECURSOR DNA-BINDING NUCLEAR SIGNAL) protein domain (PD000540) which is seen in ODP2_ALCEU.



Paralogs:  Local Blast Search


NG0564 is paralogously related to NG0916 (dihydrolipoamide succinyltransferase E2 component) (3e-62), NG0562 (dihydrolipoamide dehydrogenase (pyruvate dehydrogenase, E3 component, lipoamide dehydrogenase) (glycine cleavage system L protein)) (7e-40), NG0045 (acetyl-Co carboxylase/biotin carboxylase carrier protein (BCCP)) (2e-04) and NG1056 (outer membrane antigenic lipoprotein b precursor) (0.001).


Pfam Summary:  Pfam Search
Residues 4 to 76 (E-value = 1e-21) place NG0564 in the Biotin_lipoyl family which is described as Biotin-requiring enzyme (PF00364)
Residues 105 to 177 (E-value = 8.1e-18) place NG0564 in the Biotin_lipoyl family which is described as Biotin-requiring enzyme (PF00364)
Residues 229 to 265 (E-value = 1.4e-14) place NG0564 in the E3_binding family which is described as e3 binding domain (PF02817)
Residues 300 to 529 (E-value = 4.5e-123) place NG0564 in the 2-oxoacid_dh family which is described as 2-oxoacid dehydrogenases acyltransferase (catalytic domain) (PF00198)

Structural Feature(s):
Feature Type  Start  Stop
non-globular  
1  
291
coil-coil  
411  
438

PDB Hit:
pdb|1DPC|1DPC DIHYDROLIPOYL TRANSACETYLASE (E.C.2.3.1.12) 245.0 1e-65
pdb|1DPD|1DPD DIHYDROLIPOYL TRANSACETYLASE (E.C.2.3.1.12) 243.0 5e-65
pdb|1EAA|1EAA DIHYDROLIPOYL TRANSACETYLASE (E.C.2.3.1.12) 242.0 2e-64
pdb|1DPB|1DPB DIHYD

Gene Protein Sequence:
MSIVEIKVPDIGGHENVDIIAVEVKAGDTIAVDDTLITLETDKATMDVPA
DAAGVVKEVKVKVGDKISEGGVILTVETGAAAAEAAPAAAAEAQPAPAAA
GGATVQVAVPDIGGHTDVDVIAVEIKVGDTVAEDDTLITLETDKATMDVP
CTAAGVVKAVFLKVGDKVSEGSAIIEVETAGSAAAAPAPAAQAAAPAAVP
TSAAPAAVPTSASPAAAKIDEAAFAKAHAGPSARKLARELGVDLGQVKGS
GLKGRIMGDDIKAFVKSVMQGGAAKPAAAGASLGGGLDLLPWPKVDFSKF
GNVEVKELSRIKKISGQNLSRNWVVIPHVTVHEEADMTELEEFRKQLNKE
WEREGVKLSPLAFIIKASVSALKAFPEFNASLDGDNLVLKNYFNIGFAAD
TPNGLVVPVIKDVDQKGLKQISQELTELSKKAREGKLKPQEMQGACFTIS
SLGGIGGTGFTPIVNAPEVAILGVCKSQIKPVWNGKEFAPRLMCPLSLSF
DHRVIDGAAGMRFTVFLANLLKDFRRITL

Gene Nucleotide Sequence:  Sequence Viewer
ATGAGTATCGTAGAAATCAAAGTCCCCGATATCGGCGGTCACGAAAACGT
CGACATCATCGCCGTAGAAGTTAAAGCGGGCGACACCATCGCCGTTGACG
ACACCCTGATTACACTGGAAACCGACAAAGCCACGATGGATGTGCCTGCC
GATGCGGCCGGTGTCGTGAAAGAAGTAAAAGTCAAAGTCGGCGACAAAAT
CTCCGAAGGCGGCGTAATTTTGACCGTTGAAACCGGTGCCGCCGCTGCCG
AAGCCGCCCCGGCTGCTGCCGCCGAAGCACAACCTGCACCCGCTGCCGCA
GGCGGTGCAACCGTTCAAGTAGCCGTTCCCGATATCGGCGGCCATACCGA
TGTAGATGTAATCGCCGTTGAAATCAAAGTTGGCGACACCGTTGCCGAAG
ACGACACGCTGATTACTTTGGAAACCGATAAAGCGACAATGGACGTACCT
TGTACCGCTGCCGGTGTCGTTAAAGCCGTATTCTTAAAAGTCGGCGACAA
AGTGTCCGAAGGCTCTGCCATTATCGAAGTGGAAACCGCCGGCTCTGCCG
CAGCAGCTCCTGCGCCTGCCGCTCAAGCTGCCGCACCCGCCGCCGTGCCT
ACATCTGCCGCACCCGCCGCCGTGCCTACATCTGCCTCGCCTGCCGCTGC
CAAAATCGATGAAGCCGCTTTCGCCAAAGCACACGCCGGTCCTTCCGCAC
GCAAACTGGCGCGCGAATTGGGCGTGGATTTGGGCCAAGTCAAAGGTAGC
GGCTTGAAAGGCCGTATCATGGGAGACGACATCAAAGCCTTTGTGAAATC
CGTAATGCAGGGCGGCGCGGCAAAACCTGCCGCAGCCGGCGCATCTTTGG
GCGGCGGTCTGGACTTGCTGCCGTGGCCTAAAGTGGACTTCTCCAAATTC
GGCAATGTCGAAGTTAAAGAATTGTCCCGCATTAAGAAAATCTCCGGTCA
AAACCTGTCCCGCAACTGGGTGGTGATTCCTCACGTTACCGTACACGAAG
AAGCGGATATGACCGAACTGGAAGAATTCCGCAAACAGCTGAACAAAGAA
TGGGAACGCGAAGGCGTGAAACTGTCCCCGTTGGCGTTCATCATCAAAGC
CTCCGTTTCCGCGCTGAAAGCCTTCCCCGAATTCAACGCTTCTTTGGACG
GCGACAACCTGGTGCTGAAAAACTACTTCAACATCGGTTTCGCAGCCGAT
ACGCCGAACGGCTTGGTTGTTCCCGTCATCAAAGACGTGGATCAAAAAGG
CTTGAAACAAATCAGCCAAGAATTGACCGAATTGTCCAAAAAAGCCCGCG
AAGGCAAGCTCAAACCGCAAGAAATGCAAGGCGCGTGCTTTACCATTTCC
AGCTTGGGCGGCATCGGCGGCACAGGTTTCACGCCGATTGTGAACGCTCC
CGAAGTCGCTATCTTGGGCGTGTGCAAATCCCAAATCAAACCGGTTTGGA
ACGGCAAAGAGTTTGCCCCGCGCCTGATGTGCCCGTTGAGCCTGTCCTTC
GACCACCGCGTCATCGACGGTGCCGCCGGTATGCGCTTCACCGTATTCCT
GGCGAACCTGTTGAAAGACTTCCGCCGCATTACCTTA


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