L-aspartate oxidase (P10902)

Identification
Name:L-aspartate oxidase
Synonyms:
  • LASPO
  • Quinolinate synthase B
Gene Name:nadB
Enzyme Class:
Biological Properties
General Function:Involved in electron carrier activity
Specific Function:Catalyzes the oxidation of L-aspartate to iminoaspartate
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
  • Alanine, aspartate and glutamate metabolism ec00250
  • Metabolic pathways eco01100
  • Nicotinate and nicotinamide metabolism ec00760
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Aspartic acid + 1.0Oxygen ↔ 1.0Hydrogen ion + 1.0Hydrogen peroxide + 1.0Iminoaspartic acid
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Aspartic acid + 1.0Water + 1.0Oxygen ↔ 1.0Oxalacetic acid + 1.0Ammonia + 1.0Hydrogen peroxide
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0L-Aspartic acid + 1.0Oxygen ↔ 1.0Iminoaspartic acid + 1.0Hydrogen peroxide
ReactionCard
SMPDB Reactions:
1.0L-Aspartic acid+1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Aspartic acid + 1.0Water + 1.0Oxygen + 1.0L-Aspartic acid → 1.0Oxalacetic acid + 1.0Ammonia + 1.0Hydrogen peroxide
ReactionCard
1.0L-Aspartic acid+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Aspartic acid + 1.0Oxygen + 1.0L-Aspartic acid → 1.0Hydrogen peroxide + 1.0Hydrogen ion + 1.0Iminoaspartic acid
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Aspartic acid + 1.0Fumaric acid → 1.0Hydrogen ion + 1.0Iminoaspartic acid + 1.0Succinic acid
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Aspartic acid + 1.0Oxygen ↔ 1.0Hydrogen ion + 1.0Hydrogen peroxide + 1.0Iminoaspartic acid
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0L-Aspartic acid + 1.0Oxygen ↔ 1.0Iminoaspartic acid + 1.0Hydrogen peroxide
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Oxygen + 1.0L-Aspartic acid → 1.0Hydrogen ion + 1.0Hydrogen peroxide + 1.0Iminoaspartic acid
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Aspartic acid + 1.0Ubiquinone-8 → 1.0Hydrogen ion + 1.0Iminoaspartic acid + 1.0Ubiquinol-8
ReactionCard
1.0Thumb+1.0Menaquinone 8 → 1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Aspartic acid + 1.0Menaquinone 8 → 1.0Hydrogen ion + 1.0Iminoaspartic acid + 1.0Menaquinol 8
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0L-Aspartic acid + 1.0Oxygen → 1.0Iminoaspartic acid + 1.0Hydrogen peroxide
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00051AmmoniaMetaboCard
ECMDB00176Fumaric acidMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21232Hydrogen peroxideMetaboCard
ECMDB01131Iminoaspartic acidMetaboCard
ECMDB00191L-Aspartic acidMetaboCard
ECMDB21245Menaquinol 8MetaboCard
ECMDB00223Oxalacetic acidMetaboCard
ECMDB04124OxygenMetaboCard
ECMDB00254Succinic acidMetaboCard
ECMDB01060Ubiquinol-8MetaboCard
ECMDB21296Ubiquinone-8MetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
aspartate oxidase activity
catalytic activity
electron carrier activity
L-aspartate oxidase activity
oxidoreductase activity
oxidoreductase activity, acting on the CH-NH2 group of donors
oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
Process
cellular metabolic process
coenzyme biosynthetic process
coenzyme metabolic process
cofactor metabolic process
metabolic process
NAD biosynthetic process
nicotinamide nucleotide biosynthetic process
oxidation reduction
pyridine nucleotide biosynthetic process
Gene Properties
Blattner:b2574
Gene OrientationClockwise
Centisome Percentage:58.38
Left Sequence End2708442
Right Sequence End2710064
Gene Sequence:
>1623 bp
ATGAATACTCTCCCTGAACATTCATGTGACGTGTTGATTATCGGTAGCGGCGCAGCCGGA
CTTTCACTGGCGCTACGCCTGGCTGACCAGCATCAGGTCATCGTTCTAAGTAAAGGCCCG
GTAACGGAAGGTTCAACATTTTATGCCCAGGGCGGTATTGCCGCCGTGTTTGATGAAACT
GACAGCATTGACTCGCATGTGGAAGACACATTGATTGCCGGGGCTGGTATTTGCGATCGC
CATGCAGTTGAATTTGTCGCCAGCAATGCACGATCCTGTGTGCAATGGCTAATCGACCAG
GGGGTGTTGTTTGATACCCACATTCAACCGAATGGCGAAGAAAGTTACCATCTGACCCGT
GAAGGTGGACATAGTCACCGTCGTATTCTTCATGCCGCCGACGCCACCGGTAGAGAAGTA
GAAACCACGCTGGTGAGCAAGGCGCTGAACCATCCGAATATTCGCGTGCTGGAGCGCAGC
AACGCGGTTGATCTGATTGTTTCTGACAAAATTGGCCTGCCGGGCACGCGACGGGTTGTT
GGCGCGTGGGTATGGAACCGTAATAAAGAAACGGTGGAAACCTGCCACGCAAAAGCGGTG
GTGCTGGCAACCGGCGGTGCGTCGAAGGTTTATCAGTACACCACCAATCCGGATATTTCT
TCTGGCGATGGCATTGCTATGGCGTGGCGCGCAGGCTGCCGGGTTGCCAATCTCGAATTT
AATCAGTTCCACCCTACCGCGCTATATCACCCACAGGCACGCAATTTCCTGTTAACAGAA
GCACTGCGCGGCGAAGGCGCTTATCTCAAGCGCCCGGATGGTACGCGTTTTATGCCCGAT
TTTGATGAGCGCGGCGAACTGGCCCCGCGCGATATTGTCGCCCGCGCCATTGACCATGAA
ATGAAACGCCTCGGCGCAGATTGTATGTTCCTTGATATCAGCCATAAGCCCGCCGATTTT
ATTCGCCAGCATTTCCCGATGATTTATGAAAAGCTGCTCGGGCTGGGGATTGATCTCACA
CAAGAACCGGTACCGATTGTGCCTGCTGCACATTATACCTGCGGTGGTGTAATGGTTGAT
GATCATGGGCGTACGGACGTCGAGGGCTTGTATGCCATTGGCGAGGTGAGTTATACCGGC
TTACACGGCGCTAACCGCATGGCCTCGAATTCATTGCTGGAGTGTCTGGTCTATGGCTGG
TCGGCGGCGGAAGATATCACCAGACGTATGCCTTATGCCCACGACATCAGTACGTTACCG
CCGTGGGATGAAAGCCGCGTTGAGAACCCTGACGAACGGGTAGTAATTCAGCATAACTGG
CACGAGCTACGTCTGTTTATGTGGGATTACGTTGGCATTGTGCGCACAACGAAGCGCCTG
GAACGCGCCCTGCGGCGGATAACCATGCTCCAACAAGAAATAGACGAATATTACGCCCAT
TTCCGCGTCTCAAATAATTTGCTGGAGCTGCGTAATCTGGTACAGGTTGCCGAGTTGATT
GTTCGCTGTGCAATGATGCGTAAAGAGAGTCGGGGGTTGCATTTCACGCTGGATTATCCG
GAACTGCTCACCCATTCCGGTCCGTCGATCCTTTCCCCCGGCAATCATTACATAAACAGA
TAA
Protein Properties
Pfam Domain Function:
Protein Residues:540
Protein Molecular Weight:60337
Protein Theoretical pI:6
PDB File:1CHU
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>L-aspartate oxidase
MNTLPEHSCDVLIIGSGAAGLSLALRLADQHQVIVLSKGPVTEGSTFYAQGGIAAVFDET
DSIDSHVEDTLIAGAGICDRHAVEFVASNARSCVQWLIDQGVLFDTHIQPNGEESYHLTR
EGGHSHRRILHAADATGREVETTLVSKALNHPNIRVLERSNAVDLIVSDKIGLPGTRRVV
GAWVWNRNKETVETCHAKAVVLATGGASKVYQYTTNPDISSGDGIAMAWRAGCRVANLEF
NQFHPTALYHPQARNFLLTEALRGEGAYLKRPDGTRFMPDFDERGELAPRDIVARAIDHE
MKRLGADCMFLDISHKPADFIRQHFPMIYEKLLGLGIDLTQEPVPIVPAAHYTCGGVMVD
DHGRTDVEGLYAIGEVSYTGLHGANRMASNSLLECLVYGWSAAEDITRRMPYAHDISTLP
PWDESRVENPDERVVIQHNWHELRLFMWDYVGIVRTTKRLERALRRITMLQQEIDEYYAH
FRVSNNLLELRNLVQVAELIVRCAMMRKESRGLHFTLDYPELLTHSGPSILSPGNHYINR
References
External Links:
ResourceLink
Uniprot ID:P10902
Uniprot Name:NADB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85675465
PDB ID:1CHU
Ecogene ID:EG10631
Ecocyc:EG10631
ColiBase:b2574
Kegg Gene:b2574
EchoBASE ID:EB0625
CCDB:NADB_ECOLI
BacMap:16130499
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Flachmann, R., Kunz, N., Seifert, J., Gutlich, M., Wientjes, F. J., Laufer, A., Gassen, H. G. (1988). "Molecular biology of pyridine nucleotide biosynthesis in Escherichia coli. Cloning and characterization of quinolinate synthesis genes nadA and nadB." Eur J Biochem 175:221-228. Pubmed: 2841129
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Mattevi, A., Tedeschi, G., Bacchella, L., Coda, A., Negri, A., Ronchi, S. (1999). "Structure of L-aspartate oxidase: implications for the succinate dehydrogenase/fumarate reductase oxidoreductase family." Structure 7:745-756. Pubmed: 10425677
  • Seifert, J., Kunz, N., Flachmann, R., Laufer, A., Jany, K. D., Gassen, H. G. (1990). "Expression of the E. coli nadB gene and characterization of the gene product L-aspartate oxidase." Biol Chem Hoppe Seyler 371:239-248. Pubmed: 2187483