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Chlamydia trachomatis Search Results

Record: 1 of 1  
MiniMap IGR203 IGR205 IGR206 IGR208 IGR207 IGR204 CT244 dnaA, - CT250 glgP, - CT248 CT249 pdhA,odpA, - CT245 firA,lpxD, - CT243 pdhC,aceF, - CT247 CT244 dnaA, - CT250 glgP, - CT248 CT249 pdhA,odpA, - CT245 firA,lpxD, - CT243 pdhC,aceF, - CT247 CT244 dnaA, - CT250 glgP, - CT248 CT249 pdhA,odpA, - CT245 firA,lpxD, - CT243 pdhC,aceF, - CT247 odpB,pdhB, - CT246 odpB,pdhB, - CT246
* Calculated from Protein Sequence

Gene ID: CT247

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
pdhC  aceF  

Definition:
pyruvate dehydrogenase E2 component (dihydrolipoamide acetyltransferase)

Gene Start:
275569

Gene Stop:
276855

Gene Length:
1287

Molecular Weight*:
46278

pI*:
5.81

Net Charge*:
-4.76

EC:
2.3.1.12  

Functional Class:
energy metabolism; glycolysis and gluconeogenesis  

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

Comment:
The pyruvate dehydrogenase complex converts pyruvate to acetyl-CoA and CO2. The
E1 component of this complex appears to be represented by CT245, CT246, CT557,
CT054, CT055, and CT340. CT247 may be the E2 component; this component would convert acetyl-CoA + dihydrolipoamide
to CoA + 5-acetylydihydrolipoamide. See paralogs CT400 and CT055.

Blast Summary:  PSI-Blast Search
Numerous hits in gapped BLAST to dihydrolipoamide acetyltransferase sequences, e.g.,
residues 1-428 are approximately 29% similar to ODP2_BACST. Bacterial
and eukayotic sequences are similar in general. CT247 is similar to MG272, a predicted dihydrolipoamide
acetyltransferase in M.genitalium. No similarity to T.pallidum.

CT247 is orthologously related to CPn0306 and
they share 71% similarity.

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 3


Blocks Summary:  Blocks Search
Significant matches to two blocks: BL00189A,B,C,D,E, which encompass
2-oxy acid dehydrogenase sequences, and BL00188, which is concerned with
biotin-requiring enzymes. Residues 25-59 and 263-410 pertain to the first block, whereas
residues 16-87 pertain to the second block.

ProDom Summary:  Protein Domain Search
Residues 216-423 are 41% similar to the E2 component of the pyruvate dehydrogenase
complex, dihydrolipoamide pyruvate acetyltransferase, as represented in ODP2_HUMAN.
Other E2 domains observed in CT247 include residues 23-56, 150-202, and 156-179,
represented by sequences ODP2_HUMAN, ODO2_ECOLI, and ODO2_MYCTU.

Paralogs:  Local Blast Search
CT247 appears to be paralogously related to CT400, a lipoamide acyltransferase,
and to CT055, said to be a dihydrolipoamide succinyltransferase: residues 6-422
are 26% similar to the former and residues 207-427 are 34% similar to the latter.

Pfam Summary:  Pfam Search
Residues 3 to 76 (E-value = 2.6e-14) place CT247 in the Biotin_lipoyl family which is described as Biotin-requiring enzyme (PF00364)
Residues 148 to 184 (E-value = 2.5e-19) place CT247 in the E3_binding family which is described as e3 binding domain (PF02817)
Residues 201 to 428 (E-value = 1.1e-110) place CT247 in the 2-oxoacid_dh family which is described as 2-oxoacid dehydrogenases acyltransferase (catalytic domain) (PF00198)

Structural Feature(s):
Feature Type  Start  Stop
transmembrane  
289  
309

PDB Hit:
gi|1064952|pdb|1DPC| Dihydrolipoyl Transacetylase (E.C.2.3.1.12) (Catalytic Domain (Residues 382-637)) Mutant With Asn 614 Replaced By Asp (N614d)

Gene Protein Sequence:
MVSLLKMPKLSPTMEIGILVKWHKKAGDEIHFGDVLLEISTDKAVLEHTA
SEDGWLLEILVEEGTKTPIGTPIAVFSTEQNAQYDLKQLLPLEGTVVTDA
ATEASPKNSAQTDSQYTSGPSITMMGFRPEPPLAIPLTIKHSNDPVLASP
LAKKLAKEQNLDLSGVTGSGPGGRIVKKDLEKAPPLRIAGFGYPEAPNVN
PGSYIEEPLSPVREVISKRLQAAKTFIPHFYVRQRIYASPLLALLKELQE
QNIKLSINDCIVRACALALKEFPEINSGFNSVDNKIIRFSTIDISIAVAI
PDGVIAPIVRCADRKNIGMISAEIKGLATKAKQQSLAEEEYKGGSFCVSN
LGMTGISDFTAILNPPQAAILAVGSVEEQPVVLNGELAVGLTCMLTLSVD
HRVIDGYPAAMFMKRLQRLLEAPSVLLLN

Gene Nucleotide Sequence:  Sequence Viewer
GTGGTTTCTTTGTTAAAAATGCCTAAGCTCTCCCCTACAATGGAAATAGG
GATTCTTGTTAAATGGCACAAAAAAGCTGGGGATGAAATTCATTTCGGGG
ATGTATTACTAGAAATCTCTACTGATAAAGCTGTTTTAGAACATACAGCT
TCTGAAGATGGTTGGTTATTAGAAATTCTTGTTGAAGAAGGAACCAAAAC
TCCTATTGGCACTCCTATCGCTGTATTTTCAACAGAACAAAATGCTCAAT
ATGATTTAAAACAGCTCCTACCTTTGGAAGGAACTGTTGTTACAGATGCA
GCTACAGAAGCATCGCCAAAAAACTCTGCTCAAACAGATTCTCAATACAC
AAGTGGCCCTTCCATAACTATGATGGGATTCCGTCCGGAACCACCTTTAG
CTATTCCTCTAACTATTAAACATTCCAACGATCCAGTATTAGCTTCTCCT
TTAGCAAAAAAATTGGCCAAAGAGCAAAATCTAGACCTCTCTGGAGTAAC
TGGTAGTGGACCTGGAGGACGGATCGTAAAGAAAGATTTGGAAAAAGCTC
CTCCTTTAAGAATTGCTGGGTTTGGTTACCCTGAAGCTCCAAATGTTAAT
CCGGGATCTTATATAGAAGAACCTCTTTCCCCTGTTCGAGAAGTCATATC
TAAACGTCTGCAAGCTGCTAAAACCTTTATTCCTCACTTTTATGTAAGGC
AGCGCATTTACGCTTCCCCCCTTCTTGCATTATTAAAAGAACTTCAAGAA
CAAAATATTAAGCTCTCTATCAATGATTGTATTGTACGAGCCTGTGCTTT
AGCTCTGAAAGAATTCCCAGAAATTAATTCTGGATTCAATAGTGTCGACA
ATAAGATTATTCGGTTTTCTACGATTGATATCTCTATTGCTGTAGCTATT
CCTGATGGAGTTATCGCTCCTATTGTCCGCTGTGCTGATAGAAAAAATAT
TGGTATGATCTCTGCAGAAATCAAAGGACTTGCAACTAAAGCCAAACAGC
AGTCTCTTGCAGAAGAAGAATATAAAGGAGGTTCTTTCTGTGTATCTAAT
CTTGGTATGACAGGGATCTCTGATTTCACTGCTATTTTGAATCCTCCACA
AGCTGCTATTCTAGCTGTAGGAAGCGTAGAGGAACAACCTGTAGTCTTAA
ATGGAGAGCTAGCTGTAGGCTTGACCTGTATGTTGACATTGTCGGTAGAC
CACAGAGTGATTGATGGATATCCTGCAGCCATGTTCATGAAACGACTGCA
GAGACTCCTCGAAGCTCCTTCTGTTTTACTTCTCAAT


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