⊟Summary[edit | edit source]
- pan ID?: SAUPAN006489000
- symbol?: trmE
- synonym:
- description?: tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE
- tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE
- tRNA modification GTPase TrmE
- tRNA modification GTPase
- GTPase and tRNA-U34 5-formylation enzyme TrmE
- tRNA (5-carboxymethylaminomethyl-2-thiouridylate) synthase
- tRNA modification GTPase mnmE
descriptions from strain specific annotations:
- strand?: -
- coordinates?: 6523994..6525373
- synteny block?: BlockID0051960
- occurrence?: in 100% of 34 strains
mnmE (trmE) : tRNA uridine(34)-C(5)-carboxymethylaminomethyltransferase subunit E [1]
Transfer RNAs containing uridine at wobble anticodon position 34 often require modifications to provide maximal fidelity during protein synthesis starting from a shared 5-carboxymethylaminomethyl-2-thiouridine(34) (“cmnm5s2U”, “$”) generated by MnmAEG. In the second step, MnmE binds its glycine, GTP and methylene-tetrahydrofolate cofactors and MnmG binds NADH and FAD cofactors. The monomers bind 2-thiouridine(34) tRNA as a dimer of dimers and the methylene group from methylene-THF is transferred to the NADH-reduced FAD. This positions the reactive FAD-bound methylene group for transfer to the C(5) position of the bound tRNA. Finally, GTP hydrolysis by the MnmE subunit alters the heterotetramer conformation bringing the amino nitrogen of glycine close enough to react with the 5-methylene-2-thiouridine(34) resulting in 5-carboxymethylaminomethyl-2-thiouridine(34) tRNA. Alternatively, MnmE can bind an ammonium cofactor instead of glycine resulting in modest production of 5-aminomethyl-2-thiouridine(34) tRNA.
tRNA : s2U (34) → cmnm5s2U (34)
⊟Orthologs[edit | edit source]
⊟Genome Viewer[edit | edit source]
COL | |
N315 | |
NCTC8325 | |
Newman | |
USA300_FPR3757 |
⊟Alignments[edit | edit source]
- alignment of orthologues: CLUSTAL format alignment by MAFFT L-INS-i (v7.307)
COL MDLDTITSISTPMGEGAIGIVRLSGPQAVEIADKLYKGKHLLNDVPSHTINYGHIIDPES
N315 MDLDTITSISTPMGEGAIGIVRLSGPQAVEIADKLYKGKHLLNDVPSHTINYGHIIDPES
NCTC8325 MDLDTITSISTPMGEGAIGIVRLSGPQAVEIADKLYKGKHLLNDVPSHTINYGHIIDPES
Newman MDLDTITSISTPMGEGAIGIVRLSGPQAVEIADKLYKGKHLLNDVPSHTINYGHIIDPES
USA300_FPR3757 MDLDTITSISTPMGEGAIGIVRLSGPQAVEIADKLYKGKHLLNDVPSHTINYGHIIDPES
************************************************************
COL KEVIEEVMVSVLRAPKTFTREDIIEINCHGGILTINRVLELTMTYGARMAEPGEFTKRAF
N315 KEVVEEVMVSVLRAPKTFTREDIIEINCHGGILTINRVLELTMTYGARMAEPGEFTKRAF
NCTC8325 KEVVEEVMVSVLRAPKTFTREDIIEINCHGGILTINRVLELTMTYGARMAEPGEFTKRAF
Newman KEVIEEVMVSVLRAPKTFTREDIIEINCHGGILTINRVLELTMTYGARMAEPGEFTKRAF
USA300_FPR3757 KEVIEEVMVSVLRAPKTFTREDIIEINCHGGILTINRVLELTMTYGARMAEPGEFTKRAF
***:********************************************************
COL LNGRIDLSQAEAVMDFIRSKTDRASKVAMNQIEGRLSDLIKKQRQSILEILAQVEVNIDY
N315 LNGRIDLSQAEAVMDFIRSKTDRASKVAMNQIEGRLSDLIKKQRQSILEILAQVEVNIDY
NCTC8325 LNGRIDLSQAEAVMDFIRSKTDRASKVAMNQIEGRLSDLIKKQRQSILEILAQVEVNIDY
Newman LNGRIDLSQAEAVMDFIRSKTDRASKVAMNQIEGRLSDLIKKQRQSILEILAQVEVNIDY
USA300_FPR3757 LNGRIDLSQAEAVMDFIRSKTDRASKVAMNQIEGRLSDLIKKQRQSILEILAQVEVNIDY
************************************************************
COL PEYDDVEDATTEFLLEQSKEIKQEINRLLDTGAQGKIMREGLSTVIVGKPNVGKSSMLNN
N315 PEYDDVEDATTEFLLEQSKEIKQEINRLLDTGAQGKIMREGLSTVIVGKPNVGKSSMLNN
NCTC8325 PEYDDVEDATTEFLLEQSKEIKQEINRLLDTGAQGKIMREGLSTVIVGKPNVGKSSMLNN
Newman PEYDDVEDATTEFLLEQSKEIKQEINRLLDTGAQGKIMREGLSTVIVGKPNVGKSSMLNN
USA300_FPR3757 PEYDDVEDATTEFLLEQSKEIKQEINRLLDTGAQGKIMREGLSTVIVGKPNVGKSSMLNN
************************************************************
COL LIQDNKAIVTEVAGTTRDVLEEYVNVRGVPLRLVDTAGIRETEDIVEKIGVERSRKALSQ
N315 LIQDNKAIVTEVAGTTRDVLEEYVNVRGVPLRLVDTAGIRETEDIVEKIGVERSRKALSQ
NCTC8325 LIQDNKAIVTEVAGTTRDVLEEYVNVRGVPLRLVDTAGIRETEDIVEKIGVERSRKALSQ
Newman LIQDNKAIVTEVAGTTRDVLEEYVNVRGVPLRLVDTAGIRETEDIVEKIGVERSRKALSQ
USA300_FPR3757 LIQDNKAIVTEVAGTTRDVLEEYVNVRGVPLRLVDTAGIRETEDIVEKIGVERSRKALSQ
************************************************************
COL ADLILFVLNNNEALTQEDYTLYEVVKNEDVIVIVNKMDLEQNIDINEVKDMIGDTPLIQT
N315 ADLILFVLNNNEALTQEDYTLYEVVKNEDVIVIVNKMDLEQNIDINEVKDMIGDTPLIQT
NCTC8325 ADLILFVLNNNEALTQEDYTLYEVVKNEDVIVIVNKMDLEQNIDINEVKDMIGDTPLIQT
Newman ADLILFVLNNNEALTQEDYTLYEVVKNEDVIVIVNKMDLEQNIDINEVKDMIGDTPLIQT
USA300_FPR3757 ADLILFVLNNNEALTQEDYTLYEVVKNEDVIVIVNKMDLEQNIDINEVKDMIGDTPLIQT
************************************************************
COL SMLKQEGIDELEIQIRDLFFGGEVQNQDMTYVSNSRHISLLKQARQTIQDAIDAAESGVP
N315 SMLKQEGIDELEIQIRDLFFGGEVQNQDMTYVSNSRHISLLKQARQTIQDAIDAAESGVP
NCTC8325 SMLKQEGIDELEIQIRDLFFGGEVQNQDMTYVSNSRHISLLKQARQTIQDAIDAAESGVP
Newman SMLKQEGIDELEIQIRDLFFGGEVQNQDMTYVSNSRHISLLKQARQTIQDAIDAAESGVP
USA300_FPR3757 SMLKQEGIDELEIQIRDLFFGGEVQNQDMTYVSNSRHISLLKQARQTIQDAIDAAESGVP
************************************************************
COL MDMVQIDLTRTWEILGEIIGETASDELIDQLFSQFCLGK
N315 MDMVQIDLTRTWEILGEIIGETASDELIDQLFSQFCLGK
NCTC8325 MDMVQIDLTRTWEILGEIIGETASDELIDQLFSQFCLGK
Newman MDMVQIDLTRTWEILGEIIGETASDELIDQLFSQFCLGK
USA300_FPR3757 MDMVQIDLTRTWEILGEIIGETASDELIDQLFSQFCLGK
***************************************
- ↑ Amit Priyadarshi, Ki Hyun Nam, Eunice Eunkyeong Kim, Kwang Yeon Hwang
Crystallization and preliminary X-ray crystallographic analysis of the probable tRNA-modification GTPase (TrmE) from Staphylococcus aureus.
Acta Crystallogr Sect F Struct Biol Cryst Commun: 2008, 64(Pt 12);1166-8
[PubMed:19052377] [WorldCat.org] [DOI] (I p)Geoffrey S Briggs, Wiep Klaas Smits, Panos Soultanas
Chromosomal replication initiation machinery of low-G+C-content Firmicutes.
J Bacteriol: 2012, 194(19);5162-70
[PubMed:22797751] [WorldCat.org] [DOI] (I p)Praneeth Bommisetti, Anthony Young, Vahe Bandarian
Elucidation of the substrate of tRNA-modifying enzymes MnmEG leads to in vitro reconstitution of an evolutionarily conserved uridine hypermodification.
J Biol Chem: 2022, 298(11);102548
[PubMed:36181794] [WorldCat.org] [DOI] (I p)Praneeth Bommisetti, Vahe Bandarian
Insights into the Mechanism of Installation of 5-Carboxymethylaminomethyl Uridine Hypermodification by tRNA-Modifying Enzymes MnmE and MnmG.
J Am Chem Soc: 2023, 145(49);26947-26961
[PubMed:38050996] [WorldCat.org] [DOI] (I p)