L-aspartate oxidase

Details

Name
L-aspartate oxidase
Synonyms
  • 1.4.3.16
  • LASPO
  • nicB
  • Quinolinate synthase B
Gene Name
nadB
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0012086|L-aspartate oxidase
MNTLPEHSCDVLIIGSGAAGLSLALRLADQHQVIVLSKGPVTEGSTFYAQGGIAAVFDET
DSIDSHVEDTLIAGAGICDRHAVEFVASNARSCVQWLIDQGVLFDTHIQPNGEESYHLTR
EGGHSHRRILHAADATGREVETTLVSKALNHPNIRVLERSNAVDLIVSDKIGLPGTRRVV
GAWVWNRNKETVETCHAKAVVLATGGASKVYQYTTNPDISSGDGIAMAWRAGCRVANLEF
NQFHPTALYHPQARNFLLTEALRGEGAYLKRPDGTRFMPDFDERGELAPRDIVARAIDHE
MKRLGADCMFLDISHKPADFIRQHFPMIYEKLLGLGIDLTQEPVPIVPAAHYTCGGVMVD
DHGRTDVEGLYAIGEVSYTGLHGANRMASNSLLECLVYGWSAAEDITRRMPYAHDISTLP
PWDESRVENPDERVVIQHNWHELRLFMWDYVGIVRTTKRLERALRRITMLQQEIDEYYAH
FRVSNNLLELRNLVQVAELIVRCAMMRKESRGLHFTLDYPELLTHSGPSILSPGNHYINR
Number of residues
540
Molecular Weight
60336.885
Theoretical pI
6.32
GO Classification
Functions
flavin adenine dinucleotide binding / L-aspartate / L-aspartate oxidase activity
Processes
'de novo' NAD biosynthetic process from aspartate
Components
cytosol
General Function
L-aspartate:fumarate oxidoreductase activity
Specific Function
Catalyzes the oxidation of L-aspartate to iminoaspartate.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0012087|L-aspartate oxidase (nadB)
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
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP10902
UniProtKB Entry NameNADB_ECOLI
GenBank Gene IDX12714
General References
  1. Flachmann R, Kunz N, Seifert J, Gutlich M, Wientjes FJ, Laufer A, Gassen HG: Molecular biology of pyridine nucleotide biosynthesis in Escherichia coli. Cloning and characterization of quinolinate synthesis genes nadA and nadB. Eur J Biochem. 1988 Aug 1;175(2):221-8. [Article]
  2. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  3. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  4. Seifert J, Kunz N, Flachmann R, Laufer A, Jany KD, Gassen HG: Expression of the E. coli nadB gene and characterization of the gene product L-aspartate oxidase. Biol Chem Hoppe Seyler. 1990 Mar;371(3):239-48. [Article]
  5. Mattevi A, Tedeschi G, Bacchella L, Coda A, Negri A, Ronchi S: Structure of L-aspartate oxidase: implications for the succinate dehydrogenase/fumarate reductase oxidoreductase family. Structure. 1999 Jul 15;7(7):745-56. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03147Flavin adenine dinucleotideapprovedunknownDetails