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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR0472 IGR0467 IGR0471 IGR0469 IGR0468 IGR0470 NG0563 NG0569 aceF, - NG0564 lpdA,dldH, - NG0562 aceE, - NG0565 NG0567 drpA,proS, - NG0566 NG0563 NG0569 aceF, - NG0564 lpdA,dldH, - NG0562 aceE, - NG0565 NG0567 drpA,proS, - NG0566 Type: tandem, Name:  - 29 NG0563 aceF, - NG0564 lpdA,dldH, - NG0562 aceE, - NG0565 NG0568 NG0569 NG0568 NG0567 drpA,proS, - NG0566
* Calculated from Protein Sequence

Gene ID: NG0565

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
aceE  

Definition:
pyruvate dehydrogenase, E1 component

Gene Start:
548844

Gene Stop:
546184

Gene Length:
2661

Molecular Weight*:
99590

pI*:
5.60

Net Charge*:
-18.69

EC:
1.2.4.1  

Functional Class:
Energy metabolism; Pyruvate dehydrogenase  

Pathway: pathway table
Butanoate metabolism
Glycolysis / Gluconeogenesis
Pyruvate metabolism
Valine, leucine and isoleucine biosynthesis

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 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: E2, NO0564, and E3, NG0565.

Oklahoma ID: NGO.565c

Blast Summary:  PSI-Blast Search
Numerous significant hits in gapped BLAST to pyruvate dehydrogenase E1 components; e.g. residues 6-880 are 62% similar to dbj|BAA05572.1| (D26562) pyruvate dehydrogenase (E1 component of pyruvate dehydrogenase complex) of Escherichia coli.

Residues 1-887 are 99% similar to NMB1341 and NMA1554, pyruvate dehydrogenase, E1 component of Neisseria meningitidis (11252260, NMA1554).

COGS Summary:  COGS Search
BeTs to 7 clades of COG0021
COG name: Transketolase
Functional Class:  G
The phylogenetic pattern of COG0021 is -m--YqVCEbrhujgp-lin-
Number of proteins in this genome belonging to this COG is 2

Blocks Summary:  Blocks Search
***** IPB000360 (Transketolase) with a combined E-value of 1.5e-14.
    IPB000360A    104-115
    IPB000360B    581-620
    IPB000360C    634-663


ProDom Summary:  Protein Domain Search
Residues 357-459 are 59% similar to a (PYRUVATE DEHYDROGENASE THIAMINE PYROPHOSPHATE E1 SUBUNIT) protein domain (PD000580) which is seen in ODP1_PSEAE.

Residues 7-79 are 50% similar to a (DEHYDROGENASE E1 PYRUVATE COMPONENT GLYCOLYSIS) protein domain (PD008560) which is seen in ODP1_HAEIN.

Residues 292-352 are 68% similar to a (DEHYDROGENASE E1 PYRUVATE COMPONENT GLYCOLYSIS) protein domain (PD009824) which is seen in ODP1_ALCEU.

Residues 460-877 are 65% similar to a (DEHYDROGENASE E1 PYRUVATE COMPONENT GLYCOLYSIS) protein domain (PD008826) which is seen in ODP1_ALCEU.



Paralogs:  Local Blast Search


NG0565 is paralogously related to NG1028 (transketolase) (4e-05).


Pfam Summary:  Pfam Search
Residues 76 to 355 (E-value = 9.8e-07) place NG0565 in the Transketolase_N family which is described as Transketolase, thiamine diphosphate binding domain (PF00456)

Structural Feature(s):
Feature Type  Start  Stop
non-globular  
700  
754

PDB Hit:
pdb|1L8A|1L8A-A E. COLI PYRUVATE DEHYDROGENASE 1106.0 0.000000

Gene Protein Sequence:
MSTQLHDVDPIETQEWLDALSSVLEYEGGERAQYLLENLLKYCRDKGVRM
PHGTTTPYLNTVSVENEKGIPGDQNIEHRIRAFVRWNAAAIVLRAGKKDL
ELGGHIASFQSAATMYEVGFNHFWKAKGEGEEGDLVFFQGHVAPGIYARA
FVEGRLTEDQLNNFRQEVDGHGLPSYPHPHLLPDFWQFPTVSMGLGPIMA
IYQARFLKYLESRGLAKTKGRKVWCFCGDGEMDEPESQGAIALAAREGLD
NLIFVINCNLQRLDGPVRGNGKIIQELEGNFAGAGWNVVKVIWGRRWDRL
LAKDKDGILRQRMEECLDGDYQTYKSKDGAYVREHFFNTPELKALVADMT
DEQLWALNRGGHDPQKVYNAYDRAANHADGKPTVILAKTIKGYGMGASGE
GQNVAHQAKKMDKASLKQFRDRFDIPVTDEQIESGDLPYLTFAPDTEEYK
YLHARRDALGGYLPQRKPTQEVLEVPELSAFDAQLKSSGEREFSTTMAFV
RILSTLLKDKKIGKRVVPIVPDESRTFGMEGMFRQYGIWNPKGQQYTPQD
KDQLMFYKESVDGQILQEGINEPGAMADWIAAATSYANSDFAMIPFYIYY
SMFGFQRIGDLAWAAGDMHARGFLLGGTAGRTTLNGEGLQHEDGHSHIQA
DLIPNCVSYDPTFQYEVAVIVQDGLRRMYANNEDVFYYITLMNENYTHPD
MPEGAEQDILKGMYLLKAGGKGDKKVQLMGSGTILQEVIAGAELLKADFG
VEADIWSCPSFNLLHRDAIETERFNRLHPLEAEKVPFVTSQLQGHDGPVI
AATDYIRSYADRIRAYIPNDYHVLGTDGFGRSDSRANLRRFFEVDRYNVA
VAALAALAEQGKVSKETVQQAIEKYGIKADSAPSWKR

Gene Nucleotide Sequence:  Sequence Viewer
ATGTCCACCCAATTACACGATGTTGACCCTATCGAAACCCAAGAGTGGCT
GGACGCGTTAAGCTCCGTCCTCGAATATGAAGGCGGCGAACGCGCGCAAT
ACCTCTTGGAAAACCTGCTCAAATACTGCCGCGACAAAGGCGTACGTATG
CCCCACGGCACGACCACCCCGTATTTGAATACCGTTTCGGTTGAAAACGA
AAAAGGCATTCCGGGCGACCAAAACATCGAACACCGCATTCGCGCATTCG
TGCGCTGGAACGCCGCCGCCATCGTATTGCGCGCCGGCAAGAAAGATTTG
GAACTGGGTGGGCACATCGCATCTTTCCAATCTGCCGCCACCATGTACGA
AGTCGGTTTCAACCACTTCTGGAAAGCCAAAGGTGAAGGTGAAGAAGGCG
ATTTGGTCTTCTTCCAAGGTCACGTTGCCCCGGGCATCTATGCACGCGCA
TTCGTCGAAGGCCGTCTGACCGAAGACCAGCTGAACAACTTCCGCCAAGA
AGTGGACGGACACGGTCTGCCTTCCTATCCACACCCCCACCTCTTGCCCG
ACTTCTGGCAGTTCCCGACCGTATCCATGGGCTTGGGCCCCATCATGGCG
ATTTATCAGGCGCGTTTCCTGAAATACTTGGAATCACGCGGCTTGGCAAA
AACCAAAGGCCGTAAAGTATGGTGTTTCTGCGGCGACGGCGAAATGGACG
AACCCGAATCCCAAGGTGCAATCGCGCTGGCTGCACGCGAAGGCTTGGAC
AACCTGATTTTCGTCATCAACTGCAACCTGCAACGCTTGGACGGTCCGGT
GCGCGGCAACGGCAAAATCATCCAAGAATTGGAAGGCAACTTTGCCGGTG
CCGGCTGGAATGTCGTCAAAGTCATTTGGGGCCGCCGTTGGGACCGCCTC
TTGGCGAAAGACAAAGACGGTATCCTGCGCCAACGTATGGAAGAATGTTT
GGACGGCGACTACCAAACTTACAAATCCAAAGACGGCGCGTATGTGCGCG
AACACTTCTTCAATACGCCCGAACTGAAAGCATTGGTTGCCGATATGACC
GATGAGCAACTCTGGGCATTGAACCGCGGCGGCCACGATCCTCAAAAAGT
GTACAACGCCTACGACCGCGCAGCGAACCATGCCGACGGCAAACCTACCG
TTATCTTGGCGAAAACCATTAAAGGTTACGGTATGGGCGCATCCGGCGAA
GGTCAGAACGTTGCCCACCAAGCCAAAAAAATGGACAAAGCGTCCCTGAA
ACAATTCCGCGACCGCTTTGACATTCCGGTTACCGACGAACAAATCGAAA
GCGGCGATCTGCCTTACCTGACTTTTGCCCCCGATACGGAAGAATACAAA
TACCTGCACGCACGCCGCGATGCTTTGGGCGGCTACCTGCCGCAACGCAA
ACCGACGCAGGAAGTATTGGAAGTGCCCGAGCTGTCGGCATTCGACGCAC
AACTCAAATCCAGCGGTGAACGCGAGTTCTCGACCACGATGGCATTCGTC
CGCATCCTGTCCACTTTGCTGAAAGACAAAAAAATCGGCAAACGCGTCGT
ACCTATCGTTCCCGACGAAAGCCGTACTTTCGGCATGGAAGGTATGTTCC
GCCAATACGGTATTTGGAATCCCAAAGGCCAACAATACACGCCTCAAGAC
AAAGACCAACTGATGTTCTATAAAGAATCCGTTGACGGTCAAATCTTGCA
AGAAGGTATTAACGAACCGGGCGCGATGGCCGACTGGATTGCGGCTGCGA
CCAGCTACGCCAACAGCGACTTCGCGATGATTCCGTTCTACATCTACTAC
TCCATGTTCGGTTTCCAACGTATCGGCGACTTGGCTTGGGCGGCGGGCGA
TATGCACGCGCGCGGCTTCCTGCTGGGCGGTACTGCCGGCCGTACGACGC
TGAACGGCGAAGGTCTGCAACACGAAGACGGCCACAGCCACATCCAGGCC
GACCTGATTCCGAACTGCGTATCTTATGACCCGACCTTCCAATACGAAGT
GGCCGTCATCGTACAAGACGGTCTGCGCCGTATGTATGCCAATAATGAAG
ACGTGTTCTACTACATCACCCTGATGAACGAGAACTACACCCATCCCGAT
ATGCCGGAAGGTGCGGAACAAGACATCCTCAAAGGTATGTACCTGCTGAA
AGCCGGCGGCAAAGGCGACAAGAAAGTCCAATTGATGGGTTCCGGTACGA
TTCTGCAAGAAGTGATTGCCGGTGCCGAGCTGCTGAAAGCCGACTTCGGC
GTGGAAGCGGACATCTGGTCTTGCCCGTCCTTCAACCTGCTGCACCGCGA
CGCCATCGAAACCGAACGCTTCAACCGCCTGCATCCGCTGGAAGCTGAAA
AAGTGCCTTTCGTTACTTCCCAACTGCAAGGTCATGACGGTCCGGTTATC
GCCGCTACCGACTATATCCGCAGCTATGCCGACCGTATCCGCGCGTACAT
CCCGAACGACTACCATGTCTTGGGCACTGACGGTTTCGGCCGTTCCGACA
GCCGCGCCAACCTGCGCCGCTTCTTTGAAGTGGACCGCTACAACGTTGCC
GTGGCAGCATTGGCCGCATTGGCGGAACAAGGCAAAGTCAGCAAAGAAAC
CGTTCAACAAGCCATTGAGAAATACGGCATCAAAGCCGATTCAGCCCCTA
GCTGGAAACGC


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