Basic Search | Intermediate Search | Advanced SQL Search | Gene Image Map |  Home

Chlamydia trachomatis Search Results

Record: 1 of 1  
MiniMap tRNA-Pro-2 IGR519 IGR518 IGR517 IGR515 IGR514 IGR520 IGR521 IGR522 IGR516 glmU, - CT629 rpsD,rs4, - CT626 tctD, - CT630 ispA, - CT628 CT632 mviN, - CT624 CT631 end4, - CT625 CT627 hemB, - CT633 glmU, - CT629 rpsD,rs4, - CT626 tctD, - CT630 ispA, - CT628 CT632 mviN, - CT624 CT631 end4, - CT625 CT627 hemB, - CT633 glmU, - CT629 rpsD,rs4, - CT626 tctD, - CT630 ispA, - CT628 CT632 mviN, - CT624 CT631 end4, - CT625 CT627 hemB, - CT633
* Calculated from Protein Sequence

Gene ID: CT628

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
ispA  

Definition:
geranylgeranyl pyrophosphate synthase

Gene Start:
716361

Gene Stop:
715489

Gene Length:
873

Molecular Weight*:
32536

pI*:
4.73

Net Charge*:
-16.37

EC:
2.5.1.0  

Functional Class:
cofactor biosynthesis; ubiquinone and quinones  

Pathway: pathway table

Comment:
Prokaryotic GGPP synthetase is involved in the biosynthesis of carotenoids (gene crtE).

From Prosite PDOC00407:

A variety of isoprenoid compounds are synthesized by various organisms. For example in eukaryotes the isoprenoid biosynthetic pathway is responsible for the synthesis of a variety of end products including cholesterol, dolichol, ubiquinone or coenzyme Q. In bacteria this pathway leads to the synthesis of isopentenyl tRNA, isoprenoid quinones, and sugar carrier lipids. Among the enzymes that participate in that pathway, are a number of polyprenyl synthetase enzymes which catalyze a 1'4-condensation between 5 carbon isoprene units.

- Eukaryotic geranylgeranyl pyrophosphate synthetase (GGPP synthetase) (EC 2.5.1.1 / EC 2.5.1.10 / EC 2.5.1.29) which catalyzes the sequential addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate. In plants GGPP synthase is a chloroplast enzyme involved in the biosynthesis of terpenoids; in fungi, such as Neurospora crassa (gene al-3), this enzyme is involved in the biosynthesis of carotenoids.


Blast Summary:  PSI-Blast Search
Hits in gapped BLAST to geranylgeranyl pyrophosphate synthase sequences,
e.g. residues 29-235 are 31% similar to ISPA_BACSU. CT628 is similar to TP0683,
a predicted octaprenyl-diphosphate synthase in T.pallidum. No similarity to M.genitalium.

CT628 is orthologous to CPn0748: residues 7-286 are 51% similar to CPn0748.

COGS Summary:  COGS Search
BeTs to 16 clades of COG0142
COG name: Geranylgeranyl pyrophosphate synthase
Functional Class:  H
The phylogenetic pattern of COG0142 is AmtkYQVCEBRHUJ--olinx
Number of proteins in this genome belonging to this COG is 1


Blocks Summary:  Blocks Search
Residues 40-50, 71-114, 157-169, 212-238 are matched to blocks
BL00723A,B,C,D, concerned with polyprenyl synthetases,e.g. ISPA_BACSU.

ProDom Summary:  Protein Domain Search
Residues 68-162 are 35% similar to a geranyltransferase domain
represented by ISPA_BACSU.
Residues 197-237 are 46% similar to a similar domain from ISPA_BACST.

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

Pfam Summary:  Pfam Search
Residues 29 to 285 (E-value = 2.9e-29) place CT628 in the polyprenyl_synt family which is described as Polyprenyl synthetase (PF00348)

Structural Feature(s):
Feature Type  Start  Stop
coil-coil  
118  
152

PDB Hit:
none

Gene Protein Sequence:
MDYFSVYRSKVEKKLRDSLGDFGNTQGGLRDPIEYALLGGGKRVRPLLVG
LFAEGVHKERDVLDTAIAIEYIHTSTLIADDLPCMDDDDMRRGKPSVHKA
FDEASALLASYALIPAAYARIRKNAKALKAVVSCEQDVEEAYEDILELIE
LRFGVGGILGGQYEDIFFHDFSKENVLGIIKKKTGALFEIACVSGWLFGG
GERESSTLVAEFAEHFGLLFQIRDDLADLSQDDQEEKHMNYALLFGEVAA
KELLDHSFESCIKNLHLLQERGLECLEPLEMLCKNVFCGWK

Gene Nucleotide Sequence:  Sequence Viewer
ATGGATTATTTCAGCGTTTATCGATCGAAAGTAGAAAAAAAGCTTCGCGA
TTCTTTGGGAGATTTCGGTAACACTCAGGGTGGATTAAGAGACCCAATAG
AGTATGCCCTTTTAGGAGGGGGGAAACGCGTTCGTCCCTTGCTTGTTGGT
TTGTTTGCGGAAGGTGTCCATAAAGAGCGAGATGTCTTGGATACCGCCAT
TGCTATTGAGTATATCCATACATCTACGTTAATAGCCGATGACTTGCCGT
GTATGGACGATGATGATATGCGTAGAGGCAAGCCTTCGGTTCACAAAGCT
TTTGATGAAGCTTCGGCTCTCCTGGCTTCGTATGCTCTTATTCCAGCTGC
TTATGCACGAATTCGTAAGAATGCAAAAGCGCTAAAAGCTGTAGTTTCTT
GTGAACAAGATGTAGAAGAGGCTTACGAAGATATTTTGGAGCTGATTGAG
TTGCGTTTTGGCGTAGGAGGAATTTTAGGAGGCCAATATGAAGATATATT
TTTTCATGATTTCTCCAAAGAGAACGTATTAGGGATTATTAAAAAGAAAA
CGGGAGCTCTTTTTGAAATTGCTTGCGTATCAGGATGGTTGTTTGGAGGA
GGAGAACGGGAAAGCTCCACTTTAGTAGCTGAATTTGCTGAACATTTTGG
GTTACTTTTCCAAATACGTGATGATCTTGCCGATCTTAGTCAAGATGATC
AGGAAGAGAAACATATGAACTATGCGTTATTATTCGGAGAAGTGGCAGCA
AAAGAGTTGCTAGACCATTCTTTTGAATCCTGTATTAAAAATCTCCACCT
ATTGCAGGAGAGGGGATTGGAGTGTTTGGAGCCGCTAGAGATGTTGTGCA
AAAATGTGTTTTGTGGATGGAAA


Los Alamos National Laboratory     
Operated by the University of California for the National Nuclear Security Administration,
of the US Department of Energy.     Copyright © 2001 UC | Disclaimer/Privacy