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Mycoplasma genitalium Search Results

Record: 1 of 1  
MiniMap IGR277 IGR275 IGR273 IGR272 IGR276 IGR271 rpsT, - MG363.1 plsX, - MG368 MG360 MG369 rpL32, - MG363 rplL7/12,rplL, - MG362 rpL10, - MG361 ruvB, - MG359 fmt, - MG365 MG366 rpsT, - MG363.1 plsX, - MG368 MG360 MG369 rpL32, - MG363 rplL7/12,rplL, - MG362 rpL10, - MG361 ruvB, - MG359 fmt, - MG365 MG366 rpsT, - MG363.1 plsX, - MG368 MG360 MG369 rnc, - MG367 rnc, - MG367 rpL32, - MG363 rpL10, - MG361 ruvB, - MG359 fmt, - MG365 MG366 MG364 ruvA, - MG358 MG364 ruvA, - MG358 rplL7/12,rplL, - MG362
* Calculated from Protein Sequence

Gene ID: MG365

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
fmt  

Definition:
methionyl-tRNA formyltransferase

Gene Start:
461682

Gene Stop:
462614

Gene Length:
933

Molecular Weight*:
35522

pI*:
10.01

Net Charge*:
14.64

EC:
2.1.2.9  

Functional Class:
Translation; tRNA modification  

Pathway: pathway table
Amino Acid Metabolism; Methionine metabolism
Metabolism of Cofactors, Vitamins, and Other Substances; One carbon pool by folate
Metabolism of Macromolecules; Aminoacyl-tRNA biosynthesis

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
Hits in gapped BLAST to methionyl-tRNA formyltransferase and
its related sequences, e.g. residues 1-310 are 66% similar to
FMT_MYCPN. MG365 is similar to T.pallidum TP0756, a predicted
methionyl-tRNA formyltransferase sequence. It is also similar to
C.trachomatis methionyl-tRNA formyltransferase sequence CT530.

COGS Summary:  COGS Search
The phylogenetic pattern of COG0223 is ehgpc-y.
COG name: Methionyl-tRNA formyltransferase.
Functional Class: J
BeTs to g,c,y.

Blocks Summary:  Blocks Search
Residues 104-116, 126-160 are matched to blocks BL00373B,C,
concerned with Phosphoribosylglycinamide formyltransferase
proteins, e.g. FMT_THETH.

ProDom Summary:  Protein Domain Search
Residues 1-21, 37-59, 69-168, 197-237, 249-311 constitute defined
domains of FMT_MYCGE.

Paralogs:  Local Blast Search
No evidence of paralogs in M.genitalium.

Pfam Summary:  Pfam Search
Residues 2 to 180 (E-value = 1.3e-77) place MG365 in the Formyl_trans_N family which is described as Formyl transferase (PF00551)
Residues 204 to 302 (E-value = 2.8e-33) place MG365 in the Formyl_trans_C family which is described as Formyl transferase, C-terminal domain (PF02911)

Structural Feature(s):
Feature Type  Start  Stop
non-globular  
237  
311

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:
MFKIVFFGTSTLSKKCLEQLFYDNDFEICAVVTQPDKINHRNNKIVPSDV
KSFCLEKNITFFQPKQSISIKADLEKLKADIGICVSFGQYLHQDIIDLFP
NKVINLHPSKLPLLRGGAPLHWTIINGFKKSALSVIQLVKKMDAGPIWKQ
QDFLVNNDWNTGDLSIYVEEHSPSFLIECTKEILNKKGKWFEQIGEPTFG
LNIRKEQEHLDLNQIYKSFLNWVKGLAPKPGGWLSFEGKNIKIFKAKYVS
KSNYKHQLGEIVNISRKGINIALKSNEIISIEKIQIPGKRVMEVSEIING
KHPFVVGKCFK

Gene Nucleotide Sequence:  Sequence Viewer
ATGTTTAAAATTGTTTTCTTTGGTACTTCAACGCTTTCAAAAAAATGTTT
AGAACAACTTTTTTACGATAATGATTTTGAAATTTGTGCTGTTGTAACTC
AGCCAGACAAAATTAATCATCGTAACAATAAAATAGTACCTTCTGATGTT
AAGTCTTTTTGTTTGGAAAAAAACATAACTTTTTTTCAACCAAAACAAAG
CATAAGCATAAAAGCTGATCTAGAAAAATTAAAAGCTGATATTGGTATTT
GCGTTTCATTTGGTCAGTATCTTCATCAAGATATTATTGATCTTTTTCCA
AATAAAGTAATTAACTTACATCCTTCTAAGTTACCACTACTTCGTGGTGG
TGCACCATTACATTGAACCATTATTAATGGTTTTAAAAAATCTGCATTGA
GTGTAATTCAATTGGTTAAAAAAATGGATGCAGGTCCGATTTGAAAACAA
CAAGATTTTTTAGTTAATAATGACTGAAATACTGGTGATTTATCCATATA
TGTAGAAGAACATTCACCCTCTTTTTTAATTGAATGTACTAAAGAAATTC
TCAATAAAAAAGGGAAATGATTTGAACAAATAGGTGAACCTACTTTTGGA
TTAAACATAAGAAAAGAACAAGAACATCTTGATCTTAATCAGATTTACAA
GAGTTTTTTAAACTGAGTAAAAGGTTTAGCTCCCAAACCTGGTGGTTGGT
TAAGCTTTGAAGGAAAAAACATCAAAATTTTCAAAGCTAAATATGTTAGT
AAAAGTAATTACAAACATCAATTAGGAGAGATAGTTAATATATCTCGAAA
AGGAATTAATATTGCTTTAAAAAGCAATGAAATTATTTCAATTGAAAAAA
TTCAAATACCTGGAAAAAGGGTGATGGAAGTAAGTGAAATAATAAACGGA
AAACATCCTTTTGTTGTTGGTAAATGTTTCAAA


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