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Chlamydia trachomatis Search Results

Record: 1 of 1  
MiniMap tRNA-Ser-1 IGR303 IGR302 IGR298 IGR299 IGR301 IGR305 IGR304 IGR300 IGR297 CT357R bioY, - CT359 CT360 dapB, - CT364 dapA, - CT361 lysC, - CT362 CT365 CT356 CT357 CT358 aroA, - CT366 CT357R bioY, - CT359 CT360 dapB, - CT364 dapA, - CT361 lysC, - CT362 CT365 CT356 CT357 CT358 aroA, - CT366 CT357R bioY, - CT359 CT360 dapB, - CT364 dapA, - CT361 lysC, - CT362 CT365 CT356 asd, - CT363 asd, - CT363 CT358 aroA, - CT366 CT357
* Calculated from Protein Sequence

Gene ID: CT362

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
lysC  

Definition:
aspartokinase-I

Gene Start:
414229

Gene Stop:
412937

Gene Length:
1293

Molecular Weight*:
47636

pI*:
4.86

Net Charge*:
-14.18

EC:
2.7.2.4  

Functional Class:
amino acid biosynthesis; aspartate family  

Pathway: pathway table
Amino Acid Metabolism; Lysine biosynthesis

Comment:
This enzyme catalyzes two nonconsecutive steps in amino acid biosynthetic pathways, 1) taking homoserine to aspartate semialdehyde (EC 1.1.1.3) and 2) taking aspartate to aspartyl phosphate (EC 2.7.2.4). The enzyme is a homotetramer. An aspartokinase -II/homoserine dehydrogenase -II and an aspartokinase-III are also sometimes present, but apparently not in C.trachomatis. See CT361, CT363, CT364 and CT430.

From Prosite PDOC00289:

Aspartokinase (EC 2.7.2.4) (AK) catalyzes the phosphorylation of aspartate. The product of this reaction can then be used in the biosynthesis of lysine or in the pathway leading to homoserine, which participates in the biosynthesis of threonine, isoleucine and methionine.

In Escherichia coli, there are three different isozymes which differ in their sensitivity to repression and inhibition by Lys, Met and Thr. AK1 (gene thrA) and AK2 (gene metL) are bifunctional enzymes which both consist of an N-terminal AK domain and a C-terminal homoserine dehydrogenase domain. AK1 is involved in threonine biosynthesis and AK2, in that of methionine. The third isozyme, AK3 (gene lysC), is monofunctional and involved in lysine synthesis. In yeast, there is a single isozyme of AK (gene HOM3).

Blast Summary:  PSI-Blast Search
Numerous hits in gapped BLAST to aspartokinase-I/homoserine dehydrogenase-I sequences, e.g., residues 10-430 are 23% similar to the enzyme in E.coli (U14003). No similarities to T.pallidum and M.genitalium.

CT362 is orthologously related to CPn1049: residues 9-427 are 41% similar to CPn1049.

COGS Summary:  COGS Search
BeTs to 14 clades of COG0527
COG name: Aspartokinases
Functional Class:  E
The phylogenetic pattern of COG0527 is amtKyqVcEBrHuj----inx
Number of proteins in this genome belonging to this COG is 1


Blocks Summary:  Blocks Search
Residues 10-20 and 199-253 are matched to blocks BL00324A,B, which consist of aspartokinase protein sequences, e.g., AK2_BACSU, AKAB_CORFL. Residues 74-107 and 192-225 are more weakly matched to block BL00902C, concerned with glutamate-5-kinase proteins.

ProDom Summary:  Protein Domain Search
Residues 195-237 are 48% similar to an aspartokinase domain as observed in AKH1_MAIZE. Residues 9-158, 12-51, and 245-304 support this assignment; see AK3_ECOLI, AK_METJA, AKH_DAUCA.

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

Pfam Summary:  Pfam Search
Residues 7 to 272 (E-value = 6.7e-55) place CT362 in the AA_kinase family which is described as Amino acid kinase family (PF00696)

PDB Hit:
none

Gene Protein Sequence:
MLRQETAPLVCKFGGTSVGTAQSIRRVCEIIQEERPSFVVVSAVAGVTDW
LEEFCRLPKGKRAALTEKIRERHESIAKELGIEVSLAIFWEILEHFEDVE
ELFSEDQARILAIGEDLSSTLICSYCCTYVLPLKRLEARQVILTDSQFLR
AVPDLALMQTAWGELALQEDTIYLMQGFLGATSSGKTTVLGRGGSDFSAS
LIGELCKARELRIYTDVCGVHTADPKILKDTQLIDSLTFEEMQELASSGA
KVLHQDMLKPCVRAKVPIFVTSTFNVTKEGTWICASLNESTEGPVIKALS
LKSNQALWFVEYNSPLVRLEDVLGCVRSLGFVPGVVMAQSLGVYFTIDWE
EYPQTITKALEAFGTVSCEGPLSLVALVGAKLASWSMSRVFEALHRTPVL
CWSQTDTVINLIINKDFGVAVTELLHDCLFK

Gene Nucleotide Sequence:  Sequence Viewer
ATGCTTAGACAAGAAACAGCTCCTCTTGTGTGTAAATTCGGTGGAACAAG
TGTGGGCACAGCCCAAAGTATTCGACGAGTTTGCGAGATTATACAAGAAG
AAAGACCTTCTTTTGTTGTTGTTAGCGCAGTAGCTGGTGTTACGGATTGG
TTAGAAGAGTTTTGTCGGCTTCCTAAAGGGAAGAGAGCGGCATTGACTGA
AAAGATTCGAGAAAGACATGAATCAATAGCAAAGGAATTAGGTATAGAGG
TTTCTCTAGCTATCTTTTGGGAGATCTTGGAACATTTTGAAGATGTAGAA
GAGCTTTTTTCTGAAGATCAAGCCAGGATTTTGGCTATAGGTGAGGATTT
ATCTTCGACTTTGATTTGTAGCTACTGCTGTACCTATGTGTTACCGCTTA
AGCGGTTAGAAGCTCGTCAAGTAATTCTCACCGACTCGCAATTTTTGCGG
GCGGTTCCAGATTTAGCTTTGATGCAAACTGCTTGGGGTGAGTTGGCATT
ACAAGAAGATACTATTTACCTTATGCAAGGCTTCCTTGGAGCAACGTCTT
CAGGGAAAACTACAGTTCTTGGTCGAGGGGGGAGTGACTTTTCTGCCTCT
CTGATAGGAGAACTGTGTAAAGCAAGAGAGTTGCGTATTTATACAGATGT
TTGTGGCGTGCATACTGCCGACCCAAAAATTTTGAAAGATACACAACTCA
TAGATTCTTTAACCTTTGAAGAGATGCAGGAGTTAGCAAGTTCTGGTGCT
AAGGTATTGCACCAAGATATGTTAAAGCCTTGTGTTCGAGCGAAGGTGCC
TATTTTTGTGACTTCAACATTTAATGTAACCAAAGAAGGGACTTGGATTT
GCGCTTCATTAAATGAGAGTACAGAGGGTCCTGTGATCAAAGCACTCTCA
TTGAAGTCGAATCAAGCTCTTTGGTTTGTAGAATACAATTCTCCTCTAGT
GAGACTAGAGGATGTTTTGGGTTGTGTACGAAGCTTGGGATTTGTTCCAG
GAGTTGTCATGGCTCAAAGTTTAGGAGTGTATTTCACTATAGATTGGGAA
GAGTATCCTCAGACTATAACAAAGGCTCTTGAAGCTTTTGGTACAGTAAG
TTGTGAGGGGCCTTTATCTTTAGTTGCATTAGTGGGAGCGAAGCTAGCTT
CATGGAGTATGTCTAGAGTCTTTGAGGCTCTACACAGAACTCCAGTTTTA
TGTTGGAGTCAAACGGATACGGTTATTAATTTAATTATTAATAAGGATTT
TGGGGTCGCTGTAACCGAGTTGTTGCACGATTGCCTATTTAAA


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