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

Chlamydia trachomatis Search Results

Record: 1 of 1  
MiniMap IGR432 IGR435 IGR438 IGR434 IGR431 IGR433 IGR440 IGR439 IGR441 IGR437 IGR436 rs19, - CT524 rl22, - CT523 rl23, - CT526 fabZ, - CT532 vldD,yciA, - CT535 rl3, - CT528 rl4, - CT527 rl2, - CT525 lpxC, - CT533 CT529 fmt, - CT530 cutE,lnt, - CT534 rs19, - CT524 rl22, - CT523 rl23, - CT526 fabZ, - CT532 vldD,yciA, - CT535 rl3, - CT528 rl4, - CT527 rl2, - CT525 lpxC, - CT533 CT529 fmt, - CT530 cutE,lnt, - CT534 rl22, - CT523 rl23, - CT526 fabZ, - CT532 vldD,yciA, - CT535 rl3, - CT528 rl4, - CT527 rl2, - CT525 lpxC, - CT533 CT529 fmt, - CT530 cutE,lnt, - CT534 lpxA, - CT531 lpxA, - CT531 rs19, - CT524
* Calculated from Protein Sequence

Gene ID: CT530

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
fmt  

Definition:
methionyl-tRNA formyltransferase

Gene Start:
598790

Gene Stop:
597843

Gene Length:
948

Molecular Weight*:
33915

pI*:
9.19

Net Charge*:
5.31

EC:
2.1.2.9  

Functional Class:
translation; tRNA modification  

Pathway: pathway table
Amino Acid Metabolism; Methionine metabolism
Metabolism of Macromolecules; Aminoacyl-tRNA biosynthesis

Comment:
This enzyme catalyzes the addition of the formyl moiety to met-tRNA: 10-formyltetrahydrofolate + L-met-tRNA -> N-formylmethionyly-tRNA + tetrahydrofolate. In E.coli, the enzyme is a monomer (a 3D structure is available).

From Prosite PDOC00319:

Escherichia coli methionyl-tRNA formyltransferase (EC 2.1.2.9) (gene fmt) is the enzyme responsible for modifying the free amino group of the aminoacyl moiety of methionyl-tRMA(fMet). The central part of fmt seems to be evolutionary related to GART's active site region.

Blast Summary:  PSI-Blast Search
Several hits in gapped BLAST to methionyl-tRNA formyltransferase sequences, e.g.
residues 2-308 are 36% similar to FMT_ECOLI. CT530 is similar to TP0756
in T.pallidum and to MG365 in M.genitalium.

CT530 is orthologously related to CPn0649: residues 1-307 of CT530
are 60% similar to residues 1-307 of CPn0649, a predicted
methionyl-tRNA formyltransferase from C. pneumoniae.


COGS Summary:  COGS Search
BeTs to 13 clades of COG0223
COG name: Methionyl-tRNA formyltransferase
Functional Class:  J
The phylogenetic pattern of COG0223 is ----yQvcEbRhujgpolinx
Number of proteins in this genome belonging to this COG is 1


Blocks Summary:  Blocks Search
Residues 106-118 and 128-162 are matched to blocks BL00373B,C, which encompass
phosphoribosylglycinamide formyltransferase sequences, e.g. FMT_THETH, FMT_HAEIN.

ProDom Summary:  Protein Domain Search
Residues 74-157 are 50% similar to a formyltransferase domain as observed
in FMT_HAEIN. Residues 208-237 are 50% similar to an FMT domain as seen in
FTDM_RAT.

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

Pfam Summary:  Pfam Search
Residues 3 to 182 (E-value = 1.4e-31) place CT530 in the Formyl_trans_N family which is described as Formyl transferase (PF00551)
Residues 207 to 309 (E-value = 6.4e-46) place CT530 in the Formyl_trans_C family which is described as Formyl transferase, C-terminal domain (PF02911)

PDB Hit:
gi|2914332|pdb|1FMT|A Chain A, Methionyl-Trnafmet Formyltransferase From Escherichia Coli Formyltransferase, Initiator Trna, Translation Initiation Mol_id: 1; Molecule: Methionyl-Trna Fmet Formyltransferase; Chain: A, B; Synonym: 10-Formyltetrahydrofolate

Gene Protein Sequence:
MSLRVVYLGTPQFAATVLKTLLDAHTHIVGVVTRADKPQKRSSKLISSPV
KQLALSKNIPLLQPIKTTDPAFLAQLREWQADVFIVVAYGVILKQELLDI
PTYGCYNLHAGLLPAYRGAAPIQRCIMDGGVLSGNTVIRMDAGMDTGDIA
NVNYVAIGEDMTAGGLAEALAASGGELLLKTLQEIEAGTVRHVPQNEAMA
TLAPKLTKEEGGIHWDAPASQVYAHIRGVSPAPGAWTRYLSQGKEARRLG
VLSARMESFSGNYGDPGEVLGVSGEDLLIACRQGALRLRMVQPEGKALMK
AKDFFNGQSRLVSKLF

Gene Nucleotide Sequence:  Sequence Viewer
TTGAGTCTTAGAGTCGTTTATCTGGGGACTCCCCAATTTGCGGCTACTGT
TTTAAAAACACTTTTGGATGCACATACTCATATTGTCGGTGTTGTTACGC
GAGCTGATAAACCGCAAAAACGCTCGTCTAAGCTGATTAGTTCTCCAGTA
AAACAGTTAGCCTTGTCTAAAAATATTCCTTTACTTCAACCCATTAAGAC
TACGGATCCCGCTTTTCTTGCTCAATTACGAGAATGGCAGGCTGATGTTT
TTATTGTCGTCGCATACGGGGTGATTTTAAAGCAGGAGCTTTTAGATATC
CCTACATACGGTTGTTATAATCTTCATGCTGGGTTACTACCCGCATATCG
CGGAGCAGCTCCTATTCAGCGTTGTATTATGGATGGCGGAGTTCTGTCTG
GAAACACGGTGATCCGTATGGACGCTGGGATGGATACTGGGGATATAGCT
AATGTGAATTATGTAGCCATTGGCGAAGATATGACTGCAGGGGGGTTAGC
GGAAGCTTTAGCCGCCTCTGGTGGAGAGCTTTTGTTAAAGACTTTACAAG
AGATTGAGGCCGGAACAGTGCGCCATGTTCCTCAAAATGAAGCGATGGCT
ACGCTGGCTCCTAAATTAACTAAGGAAGAGGGAGGGATTCATTGGGATGC
TCCAGCTTCTCAAGTGTACGCGCATATCCGGGGAGTCTCGCCTGCTCCGG
GCGCTTGGACTCGCTATCTATCCCAAGGGAAAGAGGCTCGCCGTCTCGGA
GTGCTCTCTGCTAGAATGGAATCTTTCTCTGGCAATTATGGAGATCCAGG
TGAAGTCCTTGGAGTTTCTGGAGAGGATTTGCTGATCGCTTGCCGTCAAG
GAGCTTTGCGATTGCGTATGGTTCAGCCAGAAGGAAAAGCTTTGATGAAA
GCAAAAGATTTTTTTAACGGCCAATCAAGGTTGGTTTCAAAGCTTTTC


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