Protein Info for RR42_RS15390 in Cupriavidus basilensis FW507-4G11
Updated annotation (from data): Tryptophan 2,3-dioxygenase (EC 1.13.11.11)
Rationale: Specifically important for utilizing L-Tryptophan. Automated validation from mutant phenotype: the predicted function (RXN-8665) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually.
Original annotation: tryptophan 2,3-dioxygenase
These analyses and tools can help you predict a protein's function, but be skeptical. For enzymes, over 10% of annotations from KEGG or SEED are probably incorrect. For other types of proteins, the error rates may be much higher. MetaCyc and Swiss-Prot have low error rates, but the best hits in these databases are often quite distant, so this protein's function may not be the same. TIGRFam has low error rates. Finally, many experimentally-characterized proteins are not in any of these databases. To find relevant papers, use PaperBLAST.
Protein Families and Features
Best Hits
Swiss-Prot: 86% identical to T23O_CUPNH: Tryptophan 2,3-dioxygenase (kynA) from Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
KEGG orthology group: K00453, tryptophan 2,3-dioxygenase [EC: 1.13.11.11] (inferred from 86% identity to reh:H16_A2816)MetaCyc: 38% identical to tryptophan 2,3-dioxygenase (Streptosporangium sibiricum)
Tryptophan 2,3-dioxygenase. [EC: 1.13.11.11, 1.13.11.52]
Predicted SEED Role
"Tryptophan 2,3-dioxygenase (EC 1.13.11.11)" in subsystem Aromatic amino acid degradation or NAD and NADP cofactor biosynthesis global (EC 1.13.11.11)
MetaCyc Pathways
- L-tryptophan degradation IX (11/12 steps found)
- L-tryptophan degradation XII (Geobacillus) (11/12 steps found)
- NAD de novo biosynthesis II (from tryptophan) (8/9 steps found)
- superpathway of NAD biosynthesis in eukaryotes (11/14 steps found)
- L-tryptophan degradation I (via anthranilate) (3/3 steps found)
- L-tryptophan degradation to 2-amino-3-carboxymuconate semialdehyde (4/5 steps found)
- superpathway of aromatic compound degradation via 3-oxoadipate (25/35 steps found)
- 3-hydroxy-4-methyl-anthranilate biosynthesis II (3/5 steps found)
- L-tryptophan degradation III (eukaryotic) (10/15 steps found)
- 3-hydroxy-4-methyl-anthranilate biosynthesis I (2/6 steps found)
- L-tryptophan degradation XI (mammalian, via kynurenine) (11/23 steps found)
- superpathway of aromatic compound degradation via 2-hydroxypentadienoate (21/42 steps found)
KEGG Metabolic Maps
Isozymes
No predicted isozymesUse Curated BLAST to search for 1.13.11.11 or 1.13.11.52
Sequence Analysis Tools
PaperBLAST (search for papers about homologs of this protein)
Search CDD (the Conserved Domains Database, which includes COG and superfam)
Predict protein localization: PSORTb (Gram-negative bacteria)
Predict transmembrane helices and signal peptides: Phobius
Check the current SEED with FIGfam search
Find homologs in fast.genomics or the ENIGMA genome browser
See A0A0C4Y532 at UniProt or InterPro
Protein Sequence (291 amino acids)
>RR42_RS15390 Tryptophan 2,3-dioxygenase (EC 1.13.11.11) (Cupriavidus basilensis FW507-4G11) MSNHKGCPMSGAGATETSDASWHDAQMDFAKDMSYGDYLALDQILNAQHPLSPEHNEMLF IVQHQTSELWMKLALHELRAARECVRQDQLPPAFKMLTRVSRIMEQLVQAWNVLATMTPP EYSAMRPYLGMSSGFQSFQYREIEFILGNKNAAMLRPHAHQPQHLALLEEALRTPSLYDE AIRLMARRGFAIDAACIERDWTRPAGENASVEAAWLEVYRKPEAHWELYELGEKFVDLED AFRQWRFRHVTTVERVIGFKRGTGGTEGVSYLRKMLDVVLFPELWKLRTDL