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Chlamydia trachomatis Search Results

Record: 1 of 1  
MiniMap IGR256 IGR259 IGR257 IGR255 IGR258 IGR254 CT312 atpE, - CT310 tal, - CT313 atpA, - CT308 rpoB, - CT315 rpoC, - CT314 CT311 CT312 atpE, - CT310 tal, - CT313 atpA, - CT308 rpoB, - CT315 rpoC, - CT314 CT311 CT312 atpE, - CT310 tal, - CT313 atpA, - CT308 rpoB, - CT315 rpoC, - CT314 CT309 CT309 CT311
* Calculated from Protein Sequence

Gene ID: CT313

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
tal  

Definition:
transaldolase

Gene Start:
350375

Gene Stop:
349395

Gene Length:
981

Molecular Weight*:
36128

pI*:
4.76

Net Charge*:
-8.88

EC:
2.2.1.2  

Functional Class:
energy metabolism; pentose phosphate cycle  

Pathway: pathway table
Carbohydrate Metabolism; Pentose phosphate cycle

Comment:
Transaldolase converts sedohetulose 7-phosphate + D-glyceraldehyde 3-phosphate
to D-erythrose 4-phosphate + D-fructose 6-phosphate as part of the
pentose-phosphate pathway. A 3D structure is available for the E.coli transaldolase homodimer.

From Prosite PDOC00741:

Transaldolase (EC 2.2.1.2) catalyzes the reversible transfer of a three-carbon ketol unit from sedoheptulose 7-phosphate to glyceraldehyde 3-phosphate to form erythrose 4-phosphate and fructose 6-phosphate. This enzyme, together with transketolase, provides a link between the glycolytic and pentose-phosphate pathways. Transaldolase is an enzyme of about 34 Kd whose sequence has been well conserved throughout evolution. A lysine has been implicated in the catalytic mechanism of the enzyme; it acts as a nucleophilic group that attacks the carbonyl group of fructose-6-phosphate.

Transaldolase is evolutionary related to a bacterial protein of about 20 Kd (known as talC in Escherichia coli), whose exact function is not yet known.

Blast Summary:  PSI-Blast Search
Numerous hits in gapped BLAST to transaldolase sequences, e.g., residues
3-319 are 48% similar to TALA_ECOLI. Hits to eukaryotic enzymes. No similarities
to T.pallidum ot M.genitalium. Also similar to PG209 of P.gingivalis.

CT313 is orthologously related to CPn0083 and
they share 81% similarity.

COGS Summary:  COGS Search
BeTs to 10 clades of COG0176
COG name: Transaldolase
Functional Class:  G
The phylogenetic pattern of COG0176 is -m--YqvcEbrhuj----in-
Number of proteins in this genome belonging to this COG is 1


Blocks Summary:  Blocks Search
Residues 31-42, 49-70, 90-104, 127-142, 140-161, 150-160, 203-238, and
290-311 are significantly matched to blocks BL01054A,B,C,D,E,F, which
encompass transaldolase sequences, namely TAL1_HUMAN, TAL_SYNY3, TALA_ECOLI,
TAL1_KLULA, TAL_MYCLE.

ProDom Summary:  Protein Domain Search
Residues 175-307 are 56% similar to a transaldolase domain as observed in
TAL1_KLULA. Residues 12-87 and 102-165 support this assignment, as
exemplified by matches to TALB_ECOLI and TAL_SYNY3.

Paralogs:  Local Blast Search
No evidence of paralogs in C.trachomatis.

Pfam Summary:  Pfam Search
Residues 13 to 315 (E-value = 6e-116) place CT313 in the Transaldolase family which is described as Transaldolase (PF00923)

Structural Feature(s):
Feature Type  Start  Stop
transmembrane  
151  
185

PDB Hit:
gi|1941982|pdb|1ONR|A Chain A, Structure Of Transaldolase B Transferase, Pentose Shunt, Multigene Family Mol_id: 1; Molecule: Transaldolase B; Chain: A, B; Ec: 2.2.1.2; Engineered: Yes

Gene Protein Sequence:
MSSQFDQLKLWSVLVGDTGDPALIKTLGVQDATTNPSLILKVAQEPKYQS
MLTEAISWGIRQNGDDVQTLTFVLDKIQVNLGLEILKHVPGRVSLEIDAR
LSFNTEAMVQRAIFLSQLFEKMGGDKKRLLVKIPGTWEGICAAEVLESQG
IACNVTLIFNLVQAIAAAKAKVTLVSPFVGRIYDWWIAAYGAEGYSIEAD
PGVASVANIYSYYKKFDIPTQIMAASFRTKEQVLALAGCDFLTISPKLLE
ELKKDQQPVERKLSVEEAKKLDIQPVELSESVFRFLMNEDAMATEKLAEG
IRIFSGDTQILESAVTEFIRQIAAQEA

Gene Nucleotide Sequence:  Sequence Viewer
ATGTCTAGCCAGTTCGATCAGCTTAAGCTTTGGAGTGTTCTTGTTGGAGA
TACTGGAGATCCCGCTTTAATCAAGACGTTAGGGGTTCAGGATGCTACAA
CAAATCCTTCTTTGATCTTGAAGGTTGCTCAGGAGCCTAAGTACCAGTCG
ATGCTGACGGAAGCAATTTCTTGGGGCATCCGGCAGAATGGTGATGATGT
TCAAACTCTGACTTTTGTTTTAGATAAGATCCAAGTTAATTTAGGCTTGG
AGATTCTAAAGCATGTTCCTGGTCGGGTATCATTAGAAATTGATGCCCGG
CTTTCTTTTAATACAGAAGCAATGGTTCAGCGAGCGATTTTTTTATCTCA
ACTATTTGAGAAAATGGGAGGAGATAAGAAACGTTTATTAGTTAAAATTC
CTGGGACTTGGGAAGGTATCTGTGCTGCAGAGGTTTTAGAAAGCCAAGGG
ATTGCTTGTAACGTAACTTTAATTTTTAACCTTGTGCAAGCGATCGCAGC
AGCAAAAGCTAAAGTAACATTGGTCTCGCCTTTCGTTGGTCGGATTTATG
ATTGGTGGATCGCTGCTTATGGCGCAGAAGGGTATTCTATCGAAGCCGAT
CCTGGAGTTGCTTCCGTAGCAAATATCTATTCTTACTATAAGAAATTTGA
TATTCCGACTCAGATTATGGCGGCTTCTTTTAGAACGAAAGAGCAAGTGC
TTGCTTTAGCCGGATGTGATTTTTTAACAATTTCTCCTAAATTATTAGAA
GAACTCAAGAAAGATCAACAGCCTGTTGAAAGAAAGCTGAGCGTAGAAGA
AGCGAAAAAATTGGATATTCAACCTGTGGAGTTGTCAGAGAGCGTATTTC
GGTTCTTAATGAATGAAGATGCCATGGCAACAGAGAAGCTAGCTGAAGGT
ATTCGCATTTTTTCTGGTGACACTCAAATTTTAGAGTCTGCAGTTACCGA
ATTTATTAGACAGATCGCAGCCCAGGAAGCA


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