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Ureaplasma urealyticum Search Results

Record: 1 of 1  
MiniMap IGR384 IGR389 IGR388 IGR382 IGR383 IGR381 IGR385 IGR386 IGR387 UU464 outB,nadE, - UU460 UU462 fmt, - UU463 syfA,pheS, - UU458 obg, - UU461 syfB,pheT, - UU457 pdf,def, - UU465 parE,gyrB, - UU466 parC,gyrA, - UU467 UU464 outB,nadE, - UU460 UU462 fmt, - UU463 syfA,pheS, - UU458 obg, - UU461 syfB,pheT, - UU457 pdf,def, - UU465 parE,gyrB, - UU466 parC,gyrA, - UU467 Type: tandem, Name:  - 277 Type: tandem, Name:  - 274 Type: tandem, Name:  - 275 Type: tandem, Name:  - 276 Type: tandem, Name:  - 415 UU464 outB,nadE, - UU460 UU462 fmt, - UU463 syfA,pheS, - UU458 obg, - UU461 syfB,pheT, - UU457 UU459 UU459 pdf,def, - UU465 parE,gyrB, - UU466 parC,gyrA, - UU467
* Calculated from Protein Sequence

Gene ID: UU463

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
fmt  

Definition:
methionyl-tRNA formyltransferase

Gene Start:
527861

Gene Stop:
526944

Gene Length:
918

Molecular Weight*:
34780

pI*:
9.10

Net Charge*:
6.50

EC:
2.1.2.9  

Functional Class:
translation; tRNA modification  

Pathway: pathway table
Aminoacyl-tRNA biosynthesis
Methionine metabolism
One carbon pool by folate

Comment:
This protein modifies the free amino acid group of the aminacyl moiety of methionyl-tRNA (FMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by:
1) promoting its recognition by IF2 and
2) impairing its binding to EFTU-GTP.

Reaction:
10-FORMYLTETRAHYDROFOLATE + L-METHIONYL-TRNA + H(2)O = TETRAHYDROFOLATE + N-FORMYLMETHIONYL-TRNA.

There is a 3D structure of the E. coli protein.

See Prosite PDOC00319.

Blast Summary:  PSI-Blast Search
Numerous significant hits in gapped BLAST to methionyl-tRNA formyltransferases; e.g. residues 4-285 are 31% similar to FMT_BACSU; residues 3-304 are 31% similar to FMY_MYCGE; and residues 5-300 are 30% similar to FMT_HAEIN.
BLAST also reveals significant similarity to MG365, TP0756, and CT530, all of which are methionyl-tRNA formyltransferases.

COGS Summary:  COGS Search
The phylogenetic pattern of COG0223 is Ehgpc-yu.
Cog name: Methionyl-tRNA formyltransferase.
Functional class: J.
BeTs to -hg-c-yu.
Number of proteins in this genome belonging to this COG is 1



Blocks Summary:  Blocks Search
Residues 105-117 and 133-149 are in the 99.98th percentile of similarity to blocks BL00373C,D (Phosphoribosylglycinamide formyltransferase proteins.)
Residues 236-263, 149-184, 225-245, and 263-301 are in the 99.51th percentile of similarity to blocks DM01354A,F,S,X (kw TRANSCRIPTASE REVERSE II ORF2.)

ProDom Summary:  Protein Domain Search
Residues 28-179 are 43% similar to a defined domain of FMT_BACSU.
Residues 194-300 are 33% similar to a defined domain of FMT_HAEIN.
Residues 3-56 are 42% similar to a defined domain of FMT_MYCGE.

Paralogs:  Local Blast Search
No paralogs in U.u.

Pfam Summary:  Pfam Search
Residues 3 to 185 (E-value = 1.2e-27) place UU463 in the Formyl_trans_N family which is described as Formyl transferase (PF00551)
Residues 206 to 301 (E-value = 3.8e-12) place UU463 in the Formyl_trans_C family which is described as Formyl transferase, C-terminal domain (PF02911)

Structural Feature(s):
Feature Type  Start  Stop
transmembrane  
81  
107

PDB Hit:
gi|2914332|pdb|1FMT|A Chain A, Methionyl-Trnafmet Formyltransferase From Escherichia Coli

Gene Protein Sequence:
MKYKVMFFGTPEIAKIVLETLFNMHEVDLIAVVSQPDAHFDRKKNVIYSP
VKQFCLDHNIKLFQPEKIKEIEEEIRILGPDIIITCAFGQFINQGIIDIP
KYKIVNIHASLLPKLRGGAPIHYAILNGELKTGITLMHTIKKMDAGNILF
QRSLEINDCTTTKSLTLELANLSALMIKEHFLELVKPNLVGIQQDENSVS
FAYNIQKDQNIINFDQPAFFINRFVNAMYDKPIAIMQYNGVSIKVYQVKI
TNQKSCQKPGTIMIFKNQLFVSTQDFDIELLLIQLPNKKPLSPKVLLNGK
NPFIN$

Gene Nucleotide Sequence:  Sequence Viewer
ATGAAATATAAAGTAATGTTTTTTGGTACACCAGAAATCGCTAAAATTGT
TTTGGAAACATTGTTTAACATGCATGAAGTTGATTTAATCGCTGTTGTTA
GTCAACCAGATGCACATTTTGATCGAAAAAAGAATGTTATCTACTCTCCT
GTTAAACAGTTTTGTTTAGATCATAATATTAAGTTATTTCAACCAGAAAA
AATCAAAGAAATTGAAGAAGAAATCCGTATTTTAGGACCAGATATTATCA
TTACTTGTGCTTTTGGTCAATTTATTAATCAAGGGATAATTGATATTCCT
AAATACAAAATCGTTAATATTCATGCTTCACTTTTACCAAAATTACGTGG
CGGAGCACCAATTCATTATGCCATTTTAAATGGTGAATTAAAAACAGGAA
TCACTTTAATGCATACGATTAAAAAAATGGATGCAGGTAATATTTTATTT
CAAAGAAGTTTAGAAATAAACGATTGCACAACAACCAAATCACTAACTTT
AGAGTTAGCTAATCTTAGTGCATTGATGATTAAAGAACATTTTTTAGAAT
TAGTAAAACCAAATTTAGTTGGAATTCAACAAGATGAAAATTCTGTTAGT
TTTGCTTATAATATTCAAAAGGACCAAAATATTATTAATTTTGACCAACC
AGCTTTTTTTATTAATCGTTTTGTTAATGCTATGTATGATAAACCAATCG
CTATTATGCAATATAATGGCGTTTCAATTAAAGTATATCAAGTTAAAATC
ACTAATCAAAAGTCATGTCAAAAACCTGGAACAATCATGATTTTTAAAAA
TCAACTTTTTGTAAGTACGCAAGATTTTGATATTGAACTATTATTGATTC
AGCTTCCAAATAAAAAACCTTTATCTCCAAAAGTTTTATTGAATGGGAAA
AACCCTTTTATTAATTAA


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