3-hydroxyanthranilate 3,4-dioxygenase
Details
- Name
- 3-hydroxyanthranilate 3,4-dioxygenase
- Synonyms
- 1.13.11.6
- 3-HAO
- 3-hydroxyanthranilate oxygenase
- 3-hydroxyanthranilic acid dioxygenase
- HAD
- Gene Name
- nbaC
- Organism
- Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34)
- Amino acid sequence
>lcl|BSEQ0017064|3-hydroxyanthranilate 3,4-dioxygenase MLTYGAPFNFPRWIDEHAHLLKPPVGNRQVWQDSDFIVTVVGGPNHRTDYHDDPLEEFFY QLRGNAYLNLWVDGRRERADLKEGDIFLLPPHVRHSPQRPEAGSACLVIERQRPAGMLDG FEWYCDACGHLVHRVEVQLKSIVTDLPPLFESFYASEDKRRCPHCGQVHPGRAA
- Number of residues
- 174
- Molecular Weight
- 20027.475
- Theoretical pI
- 6.5
- GO Classification
- Functions3-hydroxyanthranilate 3,4-dioxygenase activity / iron ion bindingProcessesNAD biosynthetic process
- General Function
- Iron ion binding
- Specific Function
- Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.
- Pfam Domain Function
- 3-HAO (PF06052)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0017065|3-hydroxyanthranilate 3,4-dioxygenase (nbaC) ATGCTGACCTACGGAGCGCCCTTCAATTTCCCGCGCTGGATCGACGAGCATGCACACCTG TTGAAGCCGCCCGTCGGCAACCGGCAGGTGTGGCAGGACAGCGATTTCATCGTGACGGTG GTGGGCGGGCCCAACCACCGCACGGATTATCACGACGATCCGCTCGAGGAATTTTTCTAC CAGCTGCGCGGCAATGCCTACCTGAATCTCTGGGTCGACGGCAGGCGCGAGCGGGCGGAC CTGAAAGAGGGTGACATCTTCCTGCTGCCCCCGCACGTTCGCCATTCCCCGCAGCGTCCC GAGGCCGGCAGCGCCTGCCTGGTGATCGAGCGGCAGCGGCCCGCCGGTATGCTGGACGGA TTCGAGTGGTATTGCGATGCATGCGGTCACCTGGTGCATCGCGTCGAGGTGCAGCTCAAG AGCATCGTCACCGACCTCCCGCCTCTTTTCGAGAGCTTCTACGCCTCGGAAGACAAGCGC CGCTGCCCGCACTGCGGACAGGTCCATCCCGGACGCGCGGCCTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q1LCS4 UniProtKB Entry Name 3HAO_CUPMC GenBank Gene ID CP000353 - General References
- Colabroy KL, Zhai H, Li T, Ge Y, Zhang Y, Liu A, Ealick SE, McLafferty FW, Begley TP: The mechanism of inactivation of 3-hydroxyanthranilate-3,4-dioxygenase by 4-chloro-3-hydroxyanthranilate. Biochemistry. 2005 May 31;44(21):7623-31. [Article]
- Zhang Y, Colabroy KL, Begley TP, Ealick SE: Structural studies on 3-hydroxyanthranilate-3,4-dioxygenase: the catalytic mechanism of a complex oxidation involved in NAD biosynthesis. Biochemistry. 2005 May 31;44(21):7632-43. [Article]