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

Chlamydia trachomatis Search Results

Record: 1 of 1  
MiniMap tRNA-Ala-1 tRNA-Ile-1 IGR154 IGR148 IGR155 IGR153 IGR149 IGR150 IGR152 IGR151 CT179 tdk, - CT188 tauB,nrtC, - CT180 CT181 dnaX,dnaZ, - CT187 devB,zwf,nagB, - CT186 CT178 zwf, - CT185 pyrG, - CT183 CT179 tdk, - CT188 tauB,nrtC, - CT180 CT181 dnaX,dnaZ, - CT187 devB,zwf,nagB, - CT186 CT178 zwf, - CT185 pyrG, - CT183 CT179 tdk, - CT188 tauB,nrtC, - CT180 CT181 dnaX,dnaZ, - CT187 devB,zwf,nagB, - CT186 CT178 zwf, - CT185 pyrG, - CT183 yqgF, - CT184 kdsB, - CT182 yqgF, - CT184 kdsB, - CT182
* Calculated from Protein Sequence

Gene ID: CT183

DNA Molecule Name:
1  

Genbank ID:
3328588

Gene Name:
pyrG  

Definition:
CTP synthetase (UTP ammonia ligase)

Gene Start:
204429

Gene Stop:
206045

Gene Length:
1617

Molecular Weight*:
60193

pI*:
6.24

Net Charge*:
-9.65

EC:
6.3.4.2  

Functional Class:
purines, pyrimidines, nucleosides and nucleotides; pyrimidines  

Pathway: pathway table
Nucleotide Metabolism; Pyrimidine metabolism

Primary Evidence:
Wylie JL, Wang LL, Tipples G and McClarty G. 1996. A Single Point Mutation in CTP Synthetase of Chlamydia trachomatis Confers Resistance to Cyclopentenyl Cytosine. J. Biol. Chem. 271(26): 15393-15400. Medline: 9119498.

Secondary Evidence:
Tipples G, McClarty G. 1995. Cloning and expression of the Chlamydia trachomatis gene for CTP synthetase. J Biol Chem 270(14):7908-14. Medline: 7713886.

Comment:
The C. trachomatis enzyme is reported to be sensitive to feedback inhibition by CTP. See also CT182.

Blast Summary:  PSI-Blast Search
96% identical to ORF2 product of U15192. 50% similar to CTP synthetases
from archaeal bacteria and from Synechocystis. CT183 is similar to TP0305
of T.pallidum, a predicted CTP synthase: residues 6-533 are 44% similar
to this protein. No similarity to M.genitalium.

CT183 is orthologously related to CPn0236: residues 1-535 are 67% similar to CPn0236.

COGS Summary:  COGS Search
BeTs to 16 clades of COG0504
COG name: CTP synthase (UTP-ammonia lyase)
Functional Class:  F
The phylogenetic pattern of COG0504 is amtkYqvcebrhuj--olinx
Number of proteins in this genome belonging to this COG is 1


Blocks Summary:  Blocks Search
Residues 375-384 and 499-509 match to blocks BL00442B and BL00442A for glutamine
amidotransferase, e.g. PYRG_CHLTR. Residues 342-358, 377-387,, 491-524
are matched to blocks BL01236A,B,E, concerned with uncharacterized proteins,
e.g. YFGO_YEAST, YMY5_YEAST., YG61_METJA. Residues 135-147, 146-189 are
matched to blocks BL00144A,B, concerned with asparaginase
sequences, e.g. ASG1_YEAST.

ProDom Summary:  Protein Domain Search
Three domains are recognized: residues 4-308 and 387-506 characteristic
of CTP synthetases (PYRG and PYRH proteins) and residues 336-377 found
in glutamine anthranilate synthase component II (PYRG, TRPG, GUAA
proteins).

Paralogs:  Local Blast Search
No significant paralogs in C.trachomatis.

Pfam Summary:  Pfam Search
Residues 3 to 280 (E-value = 9.8e-195) place CT183 in the CTP_synth_N family which is described as CTP synthase N-terminus (PF06418)
Residues 303 to 525 (E-value = 1.9e-74) place CT183 in the GATase family which is described as Glutamine amidotransferase class-I (PF00117)

PDB Hit:
None.

Gene Protein Sequence:
MSFKSIFLTGGVVSSLGKGLTAASLALLLERQDLKVAMLKLDPYLNVDPG
TMNPYEHGEVYVTDDGVETDLDLGHYHRFSSVQLSKYSTATSGQIYTKVL
TKERNGEFLGSTVQVIPHVTNEIINVIQSCADHHKPDILIVEIGGTIGDI
ESLPFLEAVRQFRCEHPQDCLSIHMTYVPYLRAAKEIKTKPTQHSVQNLR
SIGISPDVILCRSEAPLSTEVKRKISLFCNVPEHAVFNAIDLERSIYEMP
LLLAKENISDFLLNKLGFSPKPLDLSDWQDLVEALCDKERQHVRIGLVGK
YLEHKDAYKSVFESLFHASVPANCSLELVPIAPESEDLLEQLSQCDGCLI
PGGFGTRSWEGKISAARYCRERNIPCFGICLGMQALVVEYARNVLDKPLA
NSMEINPETPDPVVCMMEGQDSVVKGGTMRLGAYPCRIAPGSLASAAYKT
DLVQERHRHRYEVNPSYIERLEEHGLKIAGVCPLGELCEIVEIPNHRWML
GVQFHPEFLSKLAKPHPLFIEFIRAAKAYSLEKANHEHR

Gene Nucleotide Sequence:  Sequence Viewer
ATGTCTTTCAAAAGCATCTTTTTGACTGGAGGCGTAGTTTCTTCTTTAGG
TAAAGGACTTACCGCAGCCTCTCTAGCTCTTCTACTAGAGAGACAAGACT
TGAAAGTTGCCATGCTCAAGTTGGACCCCTATTTAAACGTAGATCCAGGG
ACCATGAATCCTTATGAGCATGGAGAAGTATACGTGACCGACGATGGCGT
AGAAACTGATCTCGATCTTGGCCATTATCATCGCTTTTCTTCTGTACAAC
TGTCTAAATACTCCACCGCCACTTCTGGACAAATTTATACTAAGGTGCTC
ACTAAGGAACGTAATGGAGAATTTCTTGGCAGTACAGTTCAGGTTATCCC
TCACGTAACTAATGAGATTATTAATGTCATTCAATCGTGCGCAGATCACC
ATAAGCCTGATATCCTTATTGTGGAAATCGGAGGGACAATTGGAGATATA
GAATCGCTACCTTTTCTAGAAGCTGTACGACAATTCCGCTGCGAACATCC
TCAGGATTGCCTTAGCATTCACATGACATATGTCCCTTATCTAAGAGCTG
CAAAAGAAATTAAAACCAAACCTACTCAACATTCCGTACAGAACTTGCGC
AGCATTGGAATTTCTCCTGATGTAATTTTGTGCCGTTCTGAAGCTCCACT
TAGCACGGAAGTAAAAAGAAAAATCAGCCTGTTTTGTAATGTGCCAGAAC
ATGCAGTTTTTAACGCGATAGACTTAGAGCGCTCCATTTACGAAATGCCC
TTGTTATTGGCTAAAGAAAATATCTCAGACTTCTTGTTAAATAAACTTGG
TTTTTCACCTAAACCTTTGGATCTTTCAGATTGGCAAGATCTTGTGGAGG
CTTTATGTGATAAGGAGCGCCAACATGTTCGCATAGGGCTTGTTGGAAAA
TACCTAGAACATAAAGACGCATATAAATCTGTATTCGAATCTCTTTTCCA
TGCGTCTGTGCCAGCAAACTGCTCTTTGGAACTTGTTCCTATTGCTCCTG
AATCAGAAGATCTTTTAGAACAACTGTCTCAGTGCGATGGATGTTTAATT
CCTGGAGGTTTTGGCACAAGAAGTTGGGAAGGGAAAATCTCAGCAGCTCG
TTATTGCCGAGAACGGAATATCCCCTGTTTCGGAATCTGTTTAGGAATGC
AGGCTTTAGTAGTCGAATATGCAAGAAATGTTTTGGACAAACCTCTTGCC
AATTCTATGGAAATAAATCCAGAGACTCCAGATCCAGTCGTCTGCATGAT
GGAAGGACAAGATTCTGTCGTTAAAGGGGGCACTATGAGATTAGGAGCTT
ATCCTTGCCGAATTGCTCCCGGATCTTTAGCCTCTGCTGCTTATAAGACG
GATCTTGTACAAGAACGTCACCGCCATCGATATGAAGTAAATCCTTCTTA
TATAGAACGTTTAGAAGAACATGGATTAAAAATAGCTGGGGTCTGTCCTT
TAGGAGAGCTTTGCGAAATTGTTGAAATCCCCAATCATAGATGGATGCTT
GGCGTACAGTTTCATCCCGAATTTTTATCAAAATTAGCTAAGCCTCATCC
ACTATTTATAGAATTCATTCGCGCTGCTAAAGCCTATTCTTTGGAGAAAG
CGAATCATGAACATCGC


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