Probable kynurenine--oxoglutarate transaminase BNA3 (P47039)

Identification
NameProbable kynurenine--oxoglutarate transaminase BNA3
Synonyms
  • Biosynthesis of nicotinic acid protein 3
  • Kynurenine aminotransferase
Gene NameBNA3
Enzyme Class
Biological Properties
General FunctionInvolved in 1-aminocyclopropane-1-carboxylate synthase activity
Specific FunctionCatalyzes the irreversible transamination of the L- tryptophan metabolite L-kynurenine to form kynurenic acid (KA)
Cellular LocationCytoplasm. Mitochondrion
SMPDB Pathways
L-alanine metabolismPW002373 ThumbThumb?image type=greyscaleThumb?image type=simple
Tryptophan metabolismPW002442 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Tryptophan metabolismec00380 Map00380
SMPDB Reactions
Pyruvic acid + L-Glutamic acid → Oxoglutaric acid + L-Alanine
KEGG Reactions
water + N-Formyl-L-kynurenine → Formic acid + L-Kynurenine + hydron
Metabolites
YMDB IDNameView
YMDB000104-(2-Aminophenyl)-2,4-dioxobutanoic acidShow
YMDB00153Oxoglutaric acidShow
YMDB00154L-AlanineShow
YMDB00175Pyruvic acidShow
YMDB00271L-Glutamic acidShow
YMDB00375L-KynurenineShow
YMDB00385Formic acidShow
YMDB00725N-Formyl-L-kynurenineShow
YMDB00862hydronShow
YMDB00890waterShow
GO Classification
Component
Not Available
Function
cofactor binding
pyridoxal phosphate binding
carbon-sulfur lyase activity
1-aminocyclopropane-1-carboxylate synthase activity
catalytic activity
transferase activity
lyase activity
binding
transferase activity, transferring nitrogenous groups
Process
metabolic process
biosynthetic process
Gene Properties
Chromosome Locationchromosome 10
LocusYJL060W
Gene Sequence>1335 bp ATGAAACAACGATTCATTCGTCAATTTACGAACCTAATGTCTACTTCGAGACCGAAAGTT GTTGCCAACAAATATTTCACTTCTAACACTGCCAAAGATGTTTGGTCGCTAACCAATGAA GCCGCTGCAAAAGCTGCCAATAACTCCAAAAACCAAGGCCGTGAACTTATTAATTTAGGC CAAGGCTTTTTTTCATATTCCCCTCCTCAATTCGCCATTAAGGAGGCTCAGAAAGCCCTA GACATTCCAATGGTCAATCAATATTCTCCAACTAGAGGTCGACCTTCATTAATTAATTCC TTGATTAAGTTGTATTCTCCTATTTATAACACAGAATTGAAAGCGGAAAATGTTACCGTA ACAACAGGTGCCAATGAAGGTATACTTTCTTGCTTGATGGGGCTTTTGAACGCTGGCGAC GAGGTTATTGTTTTTGAACCTTTCTTTGACCAATATATTCCAAATATCGAACTTTGCGGT GGTAAAGTTGTTTACGTCCCCATAAATCCTCCAAAGGAATTGGATCAAAGGAATACTAGA GGTGAAGAATGGACCATTGACTTTGAGCAGTTCGAAAAAGCGATTACATCCAAGACAAAA GCTGTCATTATCAATACCCCTCACAACCCAATTGGTAAAGTTTTCACGCGCGAGGAATTA ACCACTTTAGGTAACATTTGCGTCAAGCACAACGTTGTGATTATATCTGATGAAGTCTAT GAACACCTTTACTTCACTGATTCTTTCACTAGAATTGCCACACTCTCTCCAGAAATTGGG CAACTAACCTTAACGGTCGGTTCTGCCGGTAAATCGTTTGCTGCTACTGGTTGGAGAATT GGTTGGGTCTTATCCTTGAACGCAGAGTTGTTAAGTTATGCAGCTAAGGCACATACAAGA ATTTGTTTTGCATCTCCATCCCCTCTACAGGAAGCTTGTGCAAACTCTATTAACGACGCT TTAAAAATTGGGTATTTTGAAAAAATGAGACAGGAATATATCAACAAATTCAAAATTTTC ACATCGATCTTTGATGAATTGGGACTACCATATACAGCTCCAGAGGGTACATATTTTGTC CTCGTTGATTTCTCTAAAGTGAAAATTCCCGAGGACTATCCCTACCCAGAGGAGATCCTG AATAAGGGAAAAGATTTTCGCATTTCTCACTGGTTGATCAATGAATTAGGTGTGGTTGCC ATTCCACCAACTGAATTCTATATCAAAGAGCACGAAAAGGCTGCTGAGAATTTGTTAAGG TTTGCAGTTTGTAAAGATGATGCTTATCTAGAAAATGCCGTAGAGAGATTAAAACTACTC AAGGACTACTTATAA
Protein Properties
Pfam Domain Function
Protein Residues444
Protein Molecular Weight50081.89844
Protein Theoretical pI6.53
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Probable kynurenine--oxoglutarate transaminase BNA3 MKQRFIRQFTNLMSTSRPKVVANKYFTSNTAKDVWSLTNEAAAKAANNSKNQGRELINLG QGFFSYSPPQFAIKEAQKALDIPMVNQYSPTRGRPSLINSLIKLYSPIYNTELKAENVTV TTGANEGILSCLMGLLNAGDEVIVFEPFFDQYIPNIELCGGKVVYVPINPPKELDQRNTR GEEWTIDFEQFEKAITSKTKAVIINTPHNPIGKVFTREELTTLGNICVKHNVVIISDEVY EHLYFTDSFTRIATLSPEIGQLTLTVGSAGKSFAATGWRIGWVLSLNAELLSYAAKAHTR ICFASPSPLQEACANSINDALKIGYFEKMRQEYINKFKIFTSIFDELGLPYTAPEGTYFV LVDFSKVKIPEDYPYPEEILNKGKDFRISHWLINELGVVAIPPTEFYIKEHEKAAENLLR FAVCKDDAYLENAVERLKLLKDYL
References
External Links
ResourceLink
Saccharomyces Genome Database BNA3
Uniprot IDP47039
Uniprot NameBNA3_YEAST
GenBank Gene IDZ49335
Genebank Protein ID1008205
General Reference
  • Galibert, F., Alexandraki, D., Baur, A., Boles, E., Chalwatzis, N., Chuat, J. C., Coster, F., Cziepluch, C., De Haan, M., Domdey, H., Durand, P., Entian, K. D., Gatius, M., Goffeau, A., Grivell, L. A., Hennemann, A., Herbert, C. J., Heumann, K., Hilger, F., Hollenberg, C. P., Huang, M. E., Jacq, C., Jauniaux, J. C., Katsoulou, C., Karpfinger-Hartl, L., et, a. l. .. (1996). "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X." EMBO J 15:2031-2049.8641269
  • Huh, W. K., Falvo, J. V., Gerke, L. C., Carroll, A. S., Howson, R. W., Weissman, J. S., O'Shea, E. K. (2003). "Global analysis of protein localization in budding yeast." Nature 425:686-691.14562095
  • 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
  • Albuquerque, C. P., Smolka, M. B., Payne, S. H., Bafna, V., Eng, J., Zhou, H. (2008). "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Mol Cell Proteomics 7:1389-1396.18407956
  • Wogulis, M., Chew, E. R., Donohoue, P. D., Wilson, D. K. (2008). "Identification of formyl kynurenine formamidase and kynurenine aminotransferase from Saccharomyces cerevisiae using crystallographic, bioinformatic and biochemical evidence." Biochemistry 47:1608-1621.18205391