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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
carbon-sulfur lyase activity
1-aminocyclopropane-1-carboxylate synthase activity
catalytic activity
transferase activity
lyase activity
binding
transferase activity, transferring nitrogenous groups
cofactor binding
pyridoxal phosphate binding
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