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Identification
NameBifunctional protein RIB2
Synonyms
  • tRNA pseudouridine synthase 8, cytoplasmic
  • tRNA pseudouridylate synthase 8
  • tRNA-uridine isomerase 8
  • Diaminohydroxyphosphoribosylaminopyrimidine deaminase
  • DRAP deaminase
  • Riboflavin-specific deaminase
Gene NameRIB2
Enzyme Class
Biological Properties
General FunctionInvolved in zinc ion binding
Specific FunctionInvolved in riboflavin biosynthesis. Converts 2,5- diamino-6-(ribosylamino)-4(3H)-pyrimidinone 5'-phosphate into 5- amino-6-(ribosylamino)-2,4(1H,3H)-pyrimidinedione 5'-phosphate
Cellular LocationCytoplasm
SMPDB Pathways
Riboflavin metabolismPW002443 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Riboflavin metabolismec00740 Map00740
SMPDB Reactions
2,5-Diamino-6-(1-D-ribitylamino)pyrimidin-4(3H)-one 5'-phosphate 5-Amino-2,6-dioxy-4-(5'-phospho-D-ribitylamino)pyrimidine
KEGG Reactions
2,5-Diamino-6-(5-phosphono)ribitylamino-4(3H)-pyrimidinone + water + hydron5-Amino-6-(5'-phosphoribitylamino)uracil + Ammonium
Metabolites
YMDB IDNameView
YMDB00091AmmoniaShow
YMDB001472,5-Diamino-4-hydroxy-6-(5-phosphoribosylamino)pyrimidineShow
YMDB001635-Amino-6-(5'-phosphoribosylamino)uracilShow
YMDB00423AmmoniumShow
YMDB004242,5-Diamino-6-(5-phosphono)ribitylamino-4(3H)-pyrimidinoneShow
YMDB004255-Amino-6-(5-phospho-D-ribitylamino)uracilShow
YMDB00862hydronShow
YMDB00890waterShow
YMDB163102,5-Diamino-6-(1-D-ribitylamino)pyrimidin-4(3H)-one 5'-phosphate Show
YMDB163115-Amino-2,6-dioxy-4-(5'-phospho-D-ribitylamino)pyrimidine Show
GO Classification
Component
Not Available
Function
RNA binding
ion binding
cation binding
metal ion binding
transition metal ion binding
catalytic activity
zinc ion binding
hydrolase activity
isomerase activity
intramolecular transferase activity
binding
nucleic acid binding
pseudouridine synthase activity
Process
RNA metabolic process
RNA modification
pseudouridine synthesis
metabolic process
macromolecule metabolic process
cellular macromolecule metabolic process
Gene Properties
Chromosome Locationchromosome 15
LocusYOL066C
Gene Sequence>1776 bp ATGGAGGACTCTAATAATGAAGCCAGCGATGACTTCAACAACTTATTAAACAAAGAAATT GAGTCTGCAAAGGAAGTGAAGTTAAGAAAATTCGCGAACAGGAATAATAATAGGAACGAA AACAGTTCCAAAGTCAAAGATGCGAGTGGATTCAGACTGAGAGTTATTCAAACCGATGGG CACAAAACTAAAAAGACAGACCCTGATTATGAAGTGACAATTGATGGACCCTTAAGGAAG ATTGAGCCTTATTTTTTCACTTATAAAACTTTCTGTAAGGAGAGGTGGAGAGATCGTAAG TTGGTGGATGTATTCGTGAGCGAATTCAGGGATCGAGAGCCCAGCTATTATTCCAAAACC ATTGCAGAGGGAAAAGTATACTTAAACGATGAACCTGCAAACCTTGATACCATCATTCGT GACGGTGATCTGATCACACATAAAGTACATCGACATGAACCGCCAGTCACATCTAAACCA ATAGATATTGTGTTTGAAGACGAAGATATCCTTGTCATTGATAAACCCAGCAGTATTCCA GTGCACCCAACGGGCAGATACAGATTCAATACCATTACAAAAATGCTAGAAAGACAGCTA GGTTATTCAGTACATCCATGTAATAGACTAGACAAGCCAACTAGTGGACTAATGTTTTTA GCCAAGACTCCATTAGGTGCAGATAGAATGGGAGACCAAATGAAAGCGAGGGAAGTCACC AAAGAATACGTAGCCCGCGTGAAGGGCGAGTTCCCTATAGGTATAGTAGAGGTAGATAAG CCTGTCAGATCTGTTAACCCTAAAGTTGCACTAAACGCTGTTTGCGAGATGAGCGATGAA AACGCTAAACATGCCAAGACCGTTTTCCAAAGGGTTAGCTATGATGGACAGACGAGTATT GTAAAGTGTAAACCATTGACAGGTAGAACTCACCAAATAAGAGTCCATTTGCAGTACTTG GGATTTCCCATAGCAAATGACCCTATATACTCGAACCCAGATATCTGGGGTCCAGATTTG GGCCGCGGTGGACTTCAAAACTATGATGACATCGTTCTGAAACTAGACGCTATTGGCAAG ACTAATCCTGCAGAGAGCTGGATTCATCCTCATAGCGAGGGTGAATACTTGCTTGGCCGT CAGTGCGAAGAATGCGAGGCTGAAATGTACACAGATCCCGGTACTAATGATCTCGACCTC TGGCTGCATGCCTTCCGGTACGAGTCATTGGAAAGAAATTCGGATACGCAAAAACCTCTC TGGAGTTATAGAACAAAATACCCTGAATGGGCCTTAGAGCCACATCGCCGATATATGGAA ATGGCCGTTAAGGAAGCTGGTAAGTGTGGCCCGACAAAGACTGCTTTTAGTGTTGGTGCC GTTCTTGTTCATGGAACTCAAGTACTTGCCACAGGATATTCAAGAGAGCTACCAGGAAAC ACTCATGCAGAACAGTGTGCTTTGATAAAGTACTCGCAGTTACACCCGAACTGTCCCACT ATAGTCCCTATGGGAACAGTGCTCTATACAACCATGGAACCCTGTTCCTTCAGGCTAAGT GGCAATGAGCCTTGCTGCGATAGAATCCTGGCCACCCAAGGTGCCATTGGTACTGTCTTC GTGGGGGTTATGGAGCCCGATACATTTGTTAAAAACAATACAAGTTTGAACAAGCTGGAA TCGCACGGTGTGAACTACATACAAATACCAGGCTACGAGGAGGAGTGCACCATCATTGCC TTCAAAGGCCACGATAATAGTGACGACAAAGCTTAG
Protein Properties
Pfam Domain Function
Protein Residues591
Protein Molecular Weight67035.29688
Protein Theoretical pI6.51
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Bifunctional protein RIB2 MEDSNNEASDDFNNLLNKEIESAKEVKLRKFANRNNNRNENSSKVKDASGFRLRVIQTDG HKTKKTDPDYEVTIDGPLRKIEPYFFTYKTFCKERWRDRKLVDVFVSEFRDREPSYYSKT IAEGKVYLNDEPANLDTIIRDGDLITHKVHRHEPPVTSKPIDIVFEDEDILVIDKPSSIP VHPTGRYRFNTITKMLERQLGYSVHPCNRLDKPTSGLMFLAKTPLGADRMGDQMKAREVT KEYVARVKGEFPIGIVEVDKPVRSVNPKVALNAVCEMSDENAKHAKTVFQRVSYDGQTSI VKCKPLTGRTHQIRVHLQYLGFPIANDPIYSNPDIWGPDLGRGGLQNYDDIVLKLDAIGK TNPAESWIHPHSEGEYLLGRQCEECEAEMYTDPGTNDLDLWLHAFRYESLERNSDTQKPL WSYRTKYPEWALEPHRRYMEMAVKEAGKCGPTKTAFSVGAVLVHGTQVLATGYSRELPGN THAEQCALIKYSQLHPNCPTIVPMGTVLYTTMEPCSFRLSGNEPCCDRILATQGAIGTVF VGVMEPDTFVKNNTSLNKLESHGVNYIQIPGYEEECTIIAFKGHDNSDDKA
References
External Links
ResourceLink
Saccharomyces Genome Database RIB2
Uniprot IDQ12362
Uniprot NameRIB2_YEAST
GenBank Gene IDZ21618
Genebank Protein ID642221
General Reference
  • Tzermia, M., Katsoulou, C., Alexandraki, D. (1997). "Sequence analysis of a 33.2 kb segment from the left arm of yeast chromosome XV reveals eight known genes and ten new open reading frames including homologues of ABC transporters, inositol phosphatases and human expressed sequence tags." Yeast 13:583-589.9178509
  • Dujon, B., Albermann, K., Aldea, M., Alexandraki, D., Ansorge, W., Arino, J., Benes, V., Bohn, C., Bolotin-Fukuhara, M., Bordonne, R., Boyer, J., Camasses, A., Casamayor, A., Casas, C., Cheret, G., Cziepluch, C., Daignan-Fornier, B., Dang, D. V., de Haan, M., Delius, H., Durand, P., Fairhead, C., Feldmann, H., Gaillon, L., Kleine, K., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Nature 387:98-102.9169874
  • Bacher, A., Baur, R., Oltmanns, O., Lingens, F. (1969). "Biosynthesis of riboflavin. Mutants accumulating 6-hydroxy-2,4,5-triaminopyrimidine." FEBS Lett 5:316-318.11947306
  • Oltmanns, O., Bacher, A. (1972). "Biosynthesis of riboflavine in Saccharomyces cerevisiae: the role of genes rib 1 and rib 7 ." J Bacteriol 110:818-822.4555411
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Behm-Ansmant, I., Grosjean, H., Massenet, S., Motorin, Y., Branlant, C. (2004). "Pseudouridylation at position 32 of mitochondrial and cytoplasmic tRNAs requires two distinct enzymes in Saccharomyces cerevisiae." J Biol Chem 279:52998-53006.15466869