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Chlamydia trachomatis Search Results

Record: 1 of 1  
MiniMap tRNA-Met-3 IGR272 IGR269 IGR274 IGR270.1 IGR271 IGR273 IGR270.2 CT326.2 trpC, - CT327 CT326 CT330 CT325 tpiS,tpiA, - CT328 CT324 pk,pykF, - CT332 xseA, - CT329 dxs,tkt, - CT331 CT326.2 trpC, - CT327 CT326 CT330 CT325 tpiS,tpiA, - CT328 CT324 pk,pykF, - CT332 xseA, - CT329 dxs,tkt, - CT331 trpC, - CT327 CT326 CT326.1 CT326.2 CT326.1 CT330 tpiS,tpiA, - CT328 CT324 pk,pykF, - CT332 xseA, - CT329 dxs,tkt, - CT331 CT325
* Calculated from Protein Sequence

Gene ID: CT328

DNA Molecule Name:
1  

Genbank ID:
3328746

Gene Name:
tpiS  tpiA  

Definition:
triosephosphate isomerase

Gene Start:
369332

Gene Stop:
370153

Gene Length:
822

Molecular Weight*:
29750

pI*:
5.57

Net Charge*:
-7.78

EC:
5.3.1.1  

Functional Class:
energy metabolism; glycolysis and gluconeogenesis  

Pathway: pathway table
Carbohydrate Metabolism; Fructose and mannose metabolism
Carbohydrate Metabolism; Glycolysis / Gluconeogenesis
Energy Metabolism; Carbon fixation
Metabolism of Complex Lipids; Glycerolipid metabolism

Comment:
Triosephosphate isomerase converts glyceraldehyde-3-phosphate to dihydroxyacetone phosphate. A 3D structure is available for TPIS_BACST.

From Prosite PDOC00155:

Triosephosphate isomerase (EC 5.3.1.1) (TIM) is the glycolytic enzyme that catalyzes the reversible interconversion of glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. TIM plays an important role in several metabolic pathways and is essential for efficient energy production. It is a dimer of identical subunits, each of which is made up of about 250 amino-acid residues. A glutamic acid residue is involved in the catalytic mechanism. The sequence around the active site residue is perfectly conserved in all known TIM's and can be used as a signature pattern for this type of enzyme.

Blast Summary:  PSI-Blast Search
Numerous hits in gapped BLAST to triose isomerase sequences, e.g. residues
25-270 are 43% similar to TPIS_BACSU. CT328 is similar to
TP0537 of T.pallidum, a predicted triosephosphate isomerase. It is also
similar to MG431 of M.genitalium and similar to PG561 of P.gingivalis.

CT328 is orthologously related to CPn1063, a predicted Triosephosphate Isomerase: residues
25-273 are 48% similar to CPn1063.

COGS Summary:  COGS Search
BeTs to 16 clades of COG0149
COG name: Triosephosphate isomerase
Functional Class:  G
The phylogenetic pattern of COG0149 is amtkyqvcebrhujgpolin-
Number of proteins in this genome belonging to this COG is 1


Blocks Summary:  Blocks Search
Residues 24-36, 86-136, 180-212, 228-262 are matched to blocks BL00171A-D, which comprise
triosephosphate isomerase sequences, e.g. TPIS_DROME, TPIS_TRYBB.

ProDom Summary:  Protein Domain Search
Residues 25-268 are 43% similar to a triosephosphate isomerase domain of
TPIS_BACSU. Residues 49-132 and 165-271 are similar to triosephosphat isomerase domains
of TPIS_METJA.

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

Pfam Summary:  Pfam Search
Residues 24 to 272 (E-value = 4.3e-101) place CT328 in the TIM family which is described as Triosephosphate isomerase (PF00121)

PDB Hit:
gi|1431731|pdb|1BTM|A Chain A, Triosephosphate Isomerase (Tim) Complexed With 2-Phosphoglycolic Acid Mol_id: 1; Molecule: Triosephosphate Isomerase; Chain: A, B; Synonym: Tim; Ec: 5.3.1.1; Engineered: Yes; Biological_unit: Dimer

Gene Protein Sequence:
MFTDKETHRKPFPTWAHLLHSEPSKQFVFGNWKMNKTLTEAQTFLKSFIS
SDILSNPQIITGIIPPFTLLSACQQAVSDSPIFLGAQTTHEADSGAFTGE
ISAPMLKDIGVDFVLIGHSERRHIFHEQNPVLAEKAAAAIHSGMIPVLCI
GETLEEQESGATQDILLNQLTTGLSKLPEQASFILAYEPVWAIGTGKVAH
PDLVQETHAFCRKTIASLFSKDIAERTPILYGGSVKADNARSLSLCPDVN
GLLVGGASLSSENFLSIIQQIDIP

Gene Nucleotide Sequence:  Sequence Viewer
ATGTTTACAGACAAAGAAACTCACAGAAAACCATTTCCAACTTGGGCCCA
CCTTCTCCACTCTGAGCCATCAAAGCAATTTGTTTTCGGTAATTGGAAAA
TGAACAAAACACTTACTGAAGCTCAGACCTTTTTAAAAAGTTTCATCTCT
AGTGACATTCTGTCTAATCCCCAAATCATTACAGGAATCATTCCTCCTTT
CACACTGCTGTCAGCTTGTCAACAAGCTGTAAGCGATTCCCCCATCTTTC
TTGGAGCCCAAACCACTCATGAAGCTGACTCAGGAGCTTTTACTGGTGAG
ATTTCAGCCCCAATGCTCAAAGATATCGGAGTCGATTTTGTTCTCATCGG
ACATTCCGAAAGACGTCATATCTTTCATGAACAAAATCCTGTACTTGCTG
AAAAAGCTGCTGCAGCTATCCATAGTGGAATGATTCCAGTTCTGTGTATT
GGAGAAACTCTAGAAGAACAAGAATCTGGAGCAACTCAAGATATTCTTTT
AAATCAACTGACTACAGGATTATCTAAACTCCCTGAGCAAGCCTCTTTCA
TTCTAGCTTATGAACCAGTCTGGGCTATAGGCACCGGAAAAGTAGCTCAT
CCTGATCTAGTTCAGGAAACCCATGCTTTCTGTAGAAAAACGATTGCTTC
TCTCTTTTCCAAAGATATTGCGGAACGCACCCCCATTCTTTACGGAGGAT
CTGTGAAAGCCGATAATGCTCGCTCACTTTCCCTCTGCCCTGATGTTAAT
GGTCTTTTAGTTGGAGGAGCCTCTTTATCTTCAGAGAATTTCTTATCCAT
TATACAACAAATCGATATCCCA


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