Rhea - reaction knowledgebase

Enzymes

UniProtKB ^help_outline	37,848 proteins
Enzyme class ^help_outline	EC 2.7.1.180 FAD:protein FMN transferase

Reaction participants Show >> << Hide

Name ^help_outline FAD Identifier CHEBI:57692 Charge -3 Formula C27H30N9O15P2 InChIKey^help_outline IMGVNJNCCGXBHD-UYBVJOGSSA-K SMILES^help_outline Cc1cc2nc3c(nc(=O)[n-]c3=O)n(C[C@H](O)[C@H](O)[C@H](O)COP([O-])(=O)OP([O-])(=O)OC[C@H]3O[C@H]([C@H](O)[C@@H]3O)n3cnc4c(N)ncnc34)c2cc1C 2D coordinates Mol file for the small molecule Search links Involved in 170 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name^help_outline L-threonyl-[protein] Identifier RHEA-COMP:11060 Reactive part ^help_outline
- Name ^help_outline L-threonine residue Identifier CHEBI:30013 Charge 0 Formula C4H7NO2 SMILES^help_outline O=C(*)[C@@H](N*)[C@H](O)C 2D coordinates Mol file for the small molecule Search links Involved in 39 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Search links Involved in 18 reaction(s) Find proteins in UniProtKB for this molecule
Name ^help_outline AMP Identifier CHEBI:456215 Charge -2 Formula C10H12N5O7P InChIKey^help_outline UDMBCSSLTHHNCD-KQYNXXCUSA-L SMILES^help_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 508 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name^help_outline FMN-L-threonyl-[protein] Identifier RHEA-COMP:11061 Reactive part ^help_outline
- Name ^help_outline FMN-L-threonine residue Identifier CHEBI:74257 Charge -2 Formula C21H24N5O10P SMILES^help_outline P(=O)(OC[C@H]([C@@H](O)[C@H](CN1C=2C(=NC3=C1C=C(C)C(=C3)C)C([N-]C(N2)=O)=O)O)O)(O[C@H](C)[C@@H](C(*)=O)N*)[O-] 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Search links Involved in 1 reaction(s) Find proteins in UniProtKB for this molecule
Name ^help_outline H⁺ Identifier CHEBI:15378 Charge 1 Formula H InChIKey^help_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILES^help_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule

Cross-references

	RHEA:36847	RHEA:36848	RHEA:36849	RHEA:36850
Reaction direction	undefined	left-to-right	right-to-left	bidirectional
UniProtKB ^help_outline	37,848 proteins
EC numbers ^help_outline	2.7.1.180
KEGG ^help_outline				R10613
MetaCyc ^help_outline				RXN-14461

Publications

Alternative pyrimidine biosynthesis protein ApbE is a flavin transferase catalyzing covalent attachment of FMN to a threonine residue in bacterial flavoproteins.

Bertsova Y.V., Fadeeva M.S., Kostyrko V.A., Serebryakova M.V., Baykov A.A., Bogachev A.V.

Na(+)-translocating NADH:quinone oxidoreductase (Na(+)-NQR) contains two flavin residues as redox-active prosthetic groups attached by a phosphoester bond to threonine residues in subunits NqrB and NqrC. We demonstrate here that flavinylation of truncated Vibrio harveyi NqrC at Thr-229 in Escheric ... >> More

Na(+)-translocating NADH:quinone oxidoreductase (Na(+)-NQR) contains two flavin residues as redox-active prosthetic groups attached by a phosphoester bond to threonine residues in subunits NqrB and NqrC. We demonstrate here that flavinylation of truncated Vibrio harveyi NqrC at Thr-229 in Escherichia coli cells requires the presence of a co-expressed Vibrio apbE gene. The apbE genes cluster with genes for Na(+)-NQR and other FMN-binding flavoproteins in bacterial genomes and encode proteins with previously unknown function. Experiments with isolated NqrC and ApbE proteins confirmed that ApbE is the only protein factor required for NqrC flavinylation and also indicated that the reaction is Mg(2+)-dependent and proceeds with FAD but not FMN. Inactivation of the apbE gene in Klebsiella pneumoniae, wherein the nqr operon and apbE are well separated in the chromosome, resulted in a complete loss of the quinone reductase activity of Na(+)-NQR, consistent with its dependence on covalently bound flavin. Our data thus identify ApbE as a novel modifying enzyme, flavin transferase. << Less

J. Biol. Chem. 288:14276-14286(2013) [PubMed] [EuropePMC]

RHEA:36847 FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H(+)

Enzymes

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Cross-references

Publications

Alternative pyrimidine biosynthesis protein ApbE is a flavin transferase catalyzing covalent attachment of FMN to a threonine residue in bacterial flavoproteins.