3-hydroxyanthranilate 3,4-dioxygenase (P47096)

Identification
Name3-hydroxyanthranilate 3,4-dioxygenase
Synonyms
  • 3-hydroxyanthranilate oxygenase
  • 3-HAO
  • 3-hydroxyanthranilic acid dioxygenase
  • HAD
  • Biosynthesis of nicotinic acid protein 1
Gene NameBNA1
Enzyme Class
Biological Properties
General FunctionInvolved in 3-hydroxyanthranilate 3,4-dioxygenase activity
Specific FunctionCatalyzes the oxidative ring opening of 3- hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate
Cellular LocationCytoplasm. Nucleus
SMPDB Pathways
NAD metabolismPW002421 ThumbThumb?image type=greyscaleThumb?image type=simple
Tryptophan metabolismPW002442 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Tryptophan metabolismec00380 Map00380
SMPDB Reactions
3-Hydroxyanthranilic acid + oxygen → hydron + 2-Amino-3-carboxymuconic acid semialdehyde
KEGG Reactions
3-Hydroxyanthranilic acid + oxygen → 2-amino-3-(3-oxoprop-1-enyl)but-2-enedioate + hydron
Metabolites
YMDB IDNameView
YMDB002543-Hydroxyanthranilic acidShow
YMDB002652-Amino-3-carboxymuconic acid semialdehydeShow
YMDB004623-HydroxyanthranilateShow
YMDB004792-amino-3-(3-oxoprop-1-enyl)but-2-enedioateShow
YMDB00862hydronShow
YMDB00900oxygenShow
GO Classification
Component
Not Available
Function
iron ion binding
oxidoreductase activity
oxidoreductase activity, acting on single donors with incorporation of molecular oxygen
oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
3-hydroxyanthranilate 3,4-dioxygenase activity
catalytic activity
binding
ion binding
cation binding
metal ion binding
transition metal ion binding
Process
oxidation reduction
metabolic process
Gene Properties
Chromosome Locationchromosome 10
LocusYJR025C
Gene Sequence>534 bp ATGTTTAATACTACACCAATTAATATCGACAAATGGTTGAAGGAGAACGAAGGCCTTTTG AAACCACCGGTGAATAATTATTGCTTACATAAAGGGGGATTCACTGTGATGATTGTCGGT GGGCCTAATGAAAGAACCGGTTATCACATCAATCCAACTCCCGAATGGTTCTATCAAAAA AAAGGATCTATGCTTTTAAAGGTTGTGGATGAGACAGACGCTGAACCAAAGTTCATTGAT ATCATCATCAATGAAGGCGATTCATATTTATTGCCAGGAAATGTTCCTCACAGTCCTGTT CGGTTTGCTGATACTGTGGGTATTGTTGTGGAACAAGATAGGCCTGGGGGAGAAAACGAT AAGATAAGGTGGTACTGTTCTCATTGTCGCCAAGTGGTCCACGAGAGTGAACTGCAAATG TTAGACTTAGGTACCCAAGTGAAAGAAGCCATTTTAGATTTTGAAAATGATGTCGAAAAG AGGACATGTTTCCATTGCAAGACGTTAAACTACGCACGCCCTCAATCTAATTAA
Protein Properties
Pfam Domain Function
Protein Residues177
Protein Molecular Weight20234.90039
Protein Theoretical pI5.59
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>3-hydroxyanthranilate 3,4-dioxygenase MFNTTPINIDKWLKENEGLLKPPVNNYCLHKGGFTVMIVGGPNERTGYHINPTPEWFYQK KGSMLLKVVDETDAEPKFIDIIINEGDSYLLPGNVPHSPVRFADTVGIVVEQDRPGGEND KIRWYCSHCRQVVHESELQMLDLGTQVKEAILDFENDVEKRTCFHCKTLNYARPQSN
References
External Links
ResourceLink
Saccharomyces Genome Database BNA1
Uniprot IDP47096
Uniprot Name3HAO_YEAST
GenBank Gene IDAY558309
Genebank Protein ID45270508
General Reference
  • Zagulski, M., Babinska, B., Gromadka, R., Migdalski, A., Rytka, J., Sulicka, J., Herbert, C. J. (1995). "The sequence of 24.3 kb from chromosome X reveals five complete open reading frames, all of which correspond to new genes, and a tandem insertion of a Ty1 transposon." Yeast 11:1179-1186.8619316
  • 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
  • Hu, Y., Rolfs, A., Bhullar, B., Murthy, T. V., Zhu, C., Berger, M. F., Camargo, A. A., Kelley, F., McCarron, S., Jepson, D., Richardson, A., Raphael, J., Moreira, D., Taycher, E., Zuo, D., Mohr, S., Kane, M. F., Williamson, J., Simpson, A., Bulyk, M. L., Harlow, E., Marsischky, G., Kolodner, R. D., LaBaer, J. (2007). "Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Genome Res 17:536-543.17322287
  • Kucharczyk, R., Zagulski, M., Rytka, J., Herbert, C. J. (1998). "The yeast gene YJR025c encodes a 3-hydroxyanthranilic acid dioxygenase and is involved in nicotinic acid biosynthesis." FEBS Lett 424:127-130.9539135
  • 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
  • Gruhler, A., Olsen, J. V., Mohammed, S., Mortensen, P., Faergeman, N. J., Mann, M., Jensen, O. N. (2005). "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Mol Cell Proteomics 4:310-327.15665377
  • Li, X., Gerber, S. A., Rudner, A. D., Beausoleil, S. A., Haas, W., Villen, J., Elias, J. E., Gygi, S. P. (2007). "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." J Proteome Res 6:1190-1197.17330950
  • 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
  • Li, X., Guo, M., Fan, J., Tang, W., Wang, D., Ge, H., Rong, H., Teng, M., Niu, L., Liu, Q., Hao, Q. (2006). "Crystal structure of 3-hydroxyanthranilic acid 3,4-dioxygenase from Saccharomyces cerevisiae: a special subgroup of the type III extradiol dioxygenases." Protein Sci 15:761-773.16522801