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Chlamydia trachomatis Search Results

Record: 1 of 1  
MiniMap rRNA-5SrRNA_2 rRNA-16SrRNA_2 rRNA-23SrRNA_2 IGR618 IGR620 IGR621 IGR622 IGR619 IGR617 CT753 amn, - CT751 icc, - CT754 CT755 efp, - CT752 tktB, - CT750 CT753 amn, - CT751 icc, - CT754 CT755 efp, - CT752 tktB, - CT750 CT753 amn, - CT751 icc, - CT754 CT755 efp, - CT752 tktB, - CT750
* Calculated from Protein Sequence

Gene ID: CT750

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
tktB  

Definition:
transketolase

Gene Start:
881422

Gene Stop:
883419

Gene Length:
1998

Molecular Weight*:
73116

pI*:
5.25

Net Charge*:
-18.26

EC:
2.2.1.1  

Functional Class:
energy metabolism; pentose phosphate cycle  

Pathway: pathway table
Carbohydrate Metabolism; Pentose phosphate cycle
Energy Metabolism; Carbon fixation

Comment:
In B.subtilis and E.coli, this enzyme converts sedoheptulose 7-phosphate and D-glyceraldehyde 3-phosphate to D-ribose 5-phosphate and D-xylulose 5-phosphate.

From Prosite PDOC00635:

Transketolase (EC 2.2.1.1) (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3-phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways.

TK requires thiamin pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 Kd subunits. TK sequences from a variety of eukaryotic and prokaryotic sources show that the enzyme has been evolutionarily conserved.

In the peroxisomes of methylotrophic yeast Hansenula polymorpha, there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) (EC 2.2.1.3) (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.

1-deoxyxylulose-5-phosphate synthase (DXP synthase) is an enzyme so far found in bacteria (gene dxs) and plants (gene CLA1) which catalyzes the thiamin pyrophosphoate-dependent acyloin condensation reaction between carbon atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (dxp), a precursor in the biosynthetic pathway to isoprenoids, thiamin (vitamin B1), and pyridoxol (vitamin B6). DXP synthase is evolutionary related to TK.


Blast Summary:  PSI-Blast Search
Hits in gapped BLAST to transketolase sequences, e.g. residues 13-664 are 45% similar to the A.aeolicus enzyme (AE000755).
CT750 is similar to TP0560, a predicted transketolase in T.pallidum.
It is also similar to MG066 of M.genitalium.

CT750 is orthologously related to CPn0893:
residues 4-665 are 73% similar to residues
3-664 of CPn0893.

COGS Summary:  COGS Search
BeTs to 12 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 1


Blocks Summary:  Blocks Search
Residues 20-604 span nine stretches with matches to blocks BL00801A-I, concerned with transketolase sequences, e.g. TKT_BACSU, TKT2_ECOLI, TKT2_YEAST.
Residues 65-84 are matched to block PR00788F, which encompasses nitrophorin signature sequences, e.g. A56385.

ProDom Summary:  Protein Domain Search
Residues 152-486 are 42% similar to a transketolase domain of TKT_HAEIN.
Residues 53-148, 487-586, 590-640 support this finding. Residues 6-101 are similar to an intergenic domain as seen in YQIE_BACSU.
Residues 225-286 and 524-579 are similar to component E1 pyruvate dehydrogenase domains as seen in
TKT_MYCLE, ODP1_ECOLI.

Paralogs:  Local Blast Search
CT750 is weakly paralogous to CT340, thought to be an oxoisovalerate dehydrogenase beta chain sequence: residues 140-589 are 22% similar to CT340.

Pfam Summary:  Pfam Search
Residues 11 to 340 (E-value = 4.9e-156) place CT750 in the Transketolase_N family which is described as Transketolase, thiamine diphosphate binding domain (PF00456)
Residues 357 to 527 (E-value = 9.3e-64) place CT750 in the Transket_pyr family which is described as Transketolase, pyridine binding domain (PF02779)

Structural Feature(s):
Feature Type  Start  Stop
non-globular  
304  
357

PDB Hit:
gi|809440|pdb|1TKA|A Chain A, Transketolase (E.C.2.2.1.1) Complexed With 3'-Deazo-Thiamin Diphosphate And Calcium

Gene Protein Sequence:
MAGNSDLDIDILEKIAGTIKQLSIESIQKASSGHPGMPLGCAELAAYLYG
YVLRYNSKDSRWVNRDRFVLSAGHGSALLYSCLHLAGFDVNLEDLQQFRQ
LQSRTPGHPEFRETDGVEATTGPLGQGVGNAVGMALSLKMLGARFNQPAN
SIFDAKVYCLAGDGCFMEGVSHEACSFAGSLGLDNLVLIYDHNEIILDGT
LHDVSIEDTKQRFLAYGWDVFETDGHDFESLHQVFTQIKKSQCKPTLIIA
HTIIGHGSPKEGTNKAHGSPLGEDGVAQTKSFWHLPEEKFFVPSAVKMFF
AAKQQEGKKLQEEWQERFRVWSKQAPEQHQEYLRLIQEISIQELEEILNL
IDMPESIAGRAASNKVIQVLAEDIPSLVGGSADLSSSDGTWIAKEGTISA
SDFLGRNIRYGVREFGMGTIMNGLAYSQVFRPFGGTFLVFSDYLRSAIRL
AALSKLPVIYQFTHDSIFVGEDGPTHQPIEQIMSLRAIPGLRVIRPADAN
EVKGAWLAALESAGPTALILSRQNLPTLKETKRSFREGVRKGAYILVKEE
GDRPDYTLCASGSEVHLAIEVAQSLMALDNRVRVISFPCWELFERQDVEY
RESVIGGDLGLRVSIEAGTALGWYKYIGSNGLAIAMDGFGMSGAPNEVAE
TCGFTVDNIVQRILSV

Gene Nucleotide Sequence:  Sequence Viewer
ATGGCTGGCAATAGTGATTTAGATATAGACATCTTAGAAAAGATTGCAGG
AACTATTAAACAGTTGAGCATAGAAAGTATTCAGAAAGCATCTTCAGGTC
ATCCAGGAATGCCTTTAGGATGCGCAGAGCTCGCTGCTTATTTATATGGT
TACGTATTGCGATATAATTCTAAAGATTCTCGATGGGTGAATAGGGATCG
CTTTGTTCTCTCTGCTGGACATGGTTCTGCTCTTCTTTACTCTTGTTTGC
ATTTAGCAGGATTCGATGTAAACCTAGAGGATCTGCAACAATTTCGTCAG
CTCCAATCCCGAACTCCCGGGCATCCAGAATTTAGAGAAACTGATGGTGT
AGAAGCCACTACAGGACCTCTAGGACAAGGAGTAGGAAATGCTGTTGGAA
TGGCTCTTTCATTAAAAATGTTAGGAGCCAGATTTAATCAGCCTGCGAAT
TCTATCTTTGATGCAAAAGTGTATTGCTTAGCAGGAGATGGGTGCTTCAT
GGAAGGCGTGAGTCATGAAGCTTGTAGTTTCGCGGGTTCTTTAGGCTTGG
ATAATCTCGTTTTGATTTATGATCATAATGAGATTATTTTAGACGGGACT
CTTCACGATGTAAGTATTGAGGATACAAAACAGAGATTCTTAGCATATGG
CTGGGATGTGTTTGAAACTGACGGACATGATTTTGAGAGCTTGCATCAGG
TTTTCACACAGATCAAGAAAAGCCAATGCAAACCTACGTTGATTATTGCA
CATACTATTATTGGACACGGCTCCCCTAAAGAAGGAACCAATAAAGCACA
TGGGTCTCCTTTAGGAGAGGATGGTGTTGCTCAAACTAAAAGTTTCTGGC
ATCTCCCAGAAGAAAAGTTTTTCGTTCCTTCGGCAGTGAAGATGTTCTTT
GCTGCAAAACAACAGGAAGGTAAGAAATTACAGGAAGAATGGCAAGAACG
CTTCCGAGTCTGGTCTAAACAAGCTCCCGAGCAACATCAAGAATATCTTC
GATTGATTCAAGAGATCTCGATTCAAGAACTCGAAGAAATTTTGAATCTT
ATTGATATGCCAGAGTCCATAGCCGGGCGTGCAGCTTCGAATAAAGTCAT
TCAGGTATTAGCAGAGGATATTCCATCCCTCGTAGGGGGATCGGCGGATC
TCTCTAGTTCAGATGGTACCTGGATAGCTAAAGAAGGAACTATTAGTGCT
AGCGATTTTCTTGGGCGGAATATTCGCTATGGAGTGCGCGAATTCGGAAT
GGGCACGATTATGAACGGATTAGCGTATAGTCAAGTATTCCGTCCTTTTG
GGGGAACTTTTTTAGTCTTTTCCGATTATTTGCGTTCCGCGATTCGATTA
GCAGCATTATCTAAATTGCCGGTAATTTATCAGTTCACTCATGATTCGAT
TTTTGTTGGAGAGGATGGACCTACACATCAGCCTATAGAGCAAATCATGT
CGCTGCGGGCTATTCCAGGGCTAAGAGTGATTCGTCCTGCGGATGCGAAT
GAAGTGAAAGGAGCATGGTTAGCTGCTTTAGAAAGCGCTGGTCCAACAGC
GTTAATTTTATCTCGACAAAATCTACCTACTCTTAAAGAGACGAAACGTT
CTTTCAGAGAAGGAGTAAGAAAGGGTGCTTATATTCTGGTTAAAGAGGAA
GGAGATCGCCCAGACTATACGCTGTGTGCTTCTGGATCCGAGGTGCATTT
GGCTATAGAGGTTGCACAAAGTCTTATGGCTTTAGATAATCGTGTGCGAG
TGATTTCATTCCCTTGTTGGGAGCTATTCGAGAGACAAGACGTTGAGTAT
CGCGAATCCGTAATAGGAGGAGATTTAGGGTTGCGTGTTTCTATAGAAGC
AGGTACCGCCTTGGGTTGGTACAAATACATCGGTAGCAATGGCTTAGCCA
TTGCCATGGATGGGTTTGGAATGTCCGGAGCTCCCAATGAGGTGGCAGAG
ACTTGCGGTTTCACTGTAGATAATATTGTGCAGAGAATCCTTTCTGTT


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