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Escherichia coli K-12 substr. MG1655 Enzyme: tRNA Um32 methyltransferase / tRNA Cm32 methyltransferase



Gene: trmJ Accession Numbers: G7327 (EcoCyc), b2532, ECK2529

Synonyms: yfhQ, TrMet(Xm32)

Regulation Summary Diagram: ?

Subunit composition of tRNA Um32 methyltransferase / tRNA Cm32 methyltransferase = [TrmJ]2
         tRNA Cm32/Um32 methyltransferase = TrmJ

Summary:
TrmJ is the tRNA:Cm32/Um32 methyltransferase which introduces methyl groups at the 2'-O position of C32 and U32 of several tRNAs in vitro. The tRNAs 2'-O-methylated at the C/U32 position in vivo are tRNAGln1 and tRNAGln2 (at the U32 position), and tRNAfMet1, tRNAfMet2, tRNASer1 and tRNATrp1 (at the C32 position) [Purta06].

TrmJ belongs to the SPOUT superfamily of methyltransferases [Anantharaman02]. Sequence analysis suggests that the active sites of TrmH and TrmJ are conserved, and the enzymes may thus use a similar reaction mechanism [Purta06].

Review: [El12]

Locations: cytosol

Map Position: [2,660,605 <- 2,661,345] (57.34 centisomes)
Length: 741 bp / 246 aa

Molecular Weight of Polypeptide: 27.048 kD (from nucleotide sequence)

Molecular Weight of Multimer: 58.0 kD (experimental) [Purta06]

Unification Links: ASAP:ABE-0008332 , EchoBASE:EB3225 , EcoGene:EG13452 , EcoliWiki:b2532 , ModBase:P0AE01 , OU-Microarray:b2532 , PortEco:trmJ , PR:PRO_000024116 , Pride:P0AE01 , Protein Model Portal:P0AE01 , RefSeq:NP_417027 , RegulonDB:G7327 , SMR:P0AE01 , String:511145.b2532 , UniProt:P0AE01

Relationship Links: InterPro:IN-FAMILY:IPR001537 , InterPro:IN-FAMILY:IPR004384 , Pfam:IN-FAMILY:PF00588

In Paralogous Gene Group: 429 (2 members)

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0002128 - tRNA nucleoside ribose methylation Inferred from experiment [Purta06]
GO:0006396 - RNA processing Inferred by computational analysis [GOA01]
GO:0008033 - tRNA processing Inferred by computational analysis [UniProtGOA11]
GO:0032259 - methylation Inferred by computational analysis [UniProtGOA11]
Molecular Function: GO:0042803 - protein homodimerization activity Inferred from experiment [Purta06]
GO:0052665 - tRNA (uracil-2'-O-)-methyltransferase activity Inferred from experiment [Purta06]
GO:0052666 - tRNA (cytosine-2'-O-)-methyltransferase activity Inferred from experiment [Purta06]
GO:0003723 - RNA binding Inferred by computational analysis [GOA01]
GO:0008168 - methyltransferase activity Inferred by computational analysis [UniProtGOA11]
GO:0008173 - RNA methyltransferase activity Inferred by computational analysis [GOA01]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, LopezCampistrou05]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11a, UniProtGOA11]

MultiFun Terms: information transfer RNA related RNA modification

Essentiality data for trmJ knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Credits:
Created 07-Sep-2006 by Keseler I , SRI International
Last-Curated ? 31-Jul-2013 by Keseler I , SRI International


Enzymatic reaction of: tRNA Um32 methyltransferase

Synonyms: TrMet(Um32)

EC Number: 2.1.1.200

a uridine32 in tRNA + S-adenosyl-L-methionine <=> a 2'-O-methyluridine32 in tRNA + S-adenosyl-L-homocysteine + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the direction shown.


Enzymatic reaction of: tRNA Cm32 methyltransferase

Synonyms: TrMet(Cm32)

EC Number: 2.1.1.200

a cytidine 32 in tRNA + S-adenosyl-L-methionine <=> a 2'-O-methylcytidine32 in tRNA + S-adenosyl-L-homocysteine + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is physiologically favored in the direction shown.


Sequence Features

Feature Class Location Citations Comment
Amino-Acid-Sites-That-Bind 114
[UniProt10]
UniProt: S-adenosyl-L-methionine; via carbonyl oxygen; Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 134
[UniProt10]
UniProt: S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen; Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 143
[UniProt10]
UniProt: S-adenosyl-L-methionine; via amide nitrogen; Non-Experimental Qualifier: by similarity;


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


References

Anantharaman02: Anantharaman V, Koonin EV, Aravind L (2002). "SPOUT: a class of methyltransferases that includes spoU and trmD RNA methylase superfamilies, and novel superfamilies of predicted prokaryotic RNA methylases." J Mol Microbiol Biotechnol 4(1);71-5. PMID: 11763972

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

El12: El Yacoubi B, Bailly M, de Crecy-Lagard V (2012). "Biosynthesis and function of posttranscriptional modifications of transfer RNAs." Annu Rev Genet 46;69-95. PMID: 22905870

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532

Purta06: Purta E, van Vliet F, Tkaczuk KL, Dunin-Horkawicz S, Mori H, Droogmans L, Bujnicki JM (2006). "The yfhQ gene of Escherichia coli encodes a tRNA:Cm32/Um32 methyltransferase." BMC Mol Biol 7(1);23. PMID: 16848900

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Mon Nov 24, 2014, BIOCYC13B.