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Q81PQ0 (T23O_BACAN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tryptophan 2,3-dioxygenase

Short name=TDO
EC=1.13.11.11
Alternative name(s):
Tryptamin 2,3-dioxygenase
Tryptophan oxygenase
Short name=TO
Short name=TRPO
Tryptophan pyrrolase
Tryptophanase
Gene names
Name:kynA
Ordered Locus Names:BA_2751, GBAA_2751, BAS2565
OrganismBacillus anthracis
Taxonomic identifier1392 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length279 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring By similarity.

Catalytic activity

L-tryptophan + O2 = N-formyl-L-kynurenine.

Cofactor

Binds 2 heme groups per tetramer By similarity.

Pathway

Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 1/2.

Subunit structure

Homotetramer By similarity.

Sequence similarities

Belongs to the tryptophan 2,3-dioxygenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 279279Tryptophan 2,3-dioxygenase
PRO_0000360084

Regions

Region23 – 275Substrate binding By similarity
Region48 – 525Substrate binding By similarity

Sites

Metal binding2371Iron (heme axial ligand) By similarity
Binding site1101Substrate By similarity
Binding site1141Substrate By similarity
Binding site1211Heme By similarity
Binding site2511Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q81PQ0 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 3B99D150F6ED0624

FASTA27932,758
        10         20         30         40         50         60 
MKENEKVIME KGIHTDFKEN MTYGEYLQLD SLLSSQKRLS DHHDEMLFIV IHQASELWMK 

        70         80         90        100        110        120 
LILHELNAAI ESIKQDKLQP AFKMLARVSK IQSQIIQSWD ILATLTPSEY IEFRDSLGQA 

       130        140        150        160        170        180 
SGFQSYQYRM IEYALGYKTP HALKIYEKDP ELHARLHTAL HAPSLYNVAI QALVKEGFPI 

       190        200        210        220        230        240 
HKDVLNRDIT QPYEEDATVE AAWLEVYADV KKYWNLYQLA EKLIDIEDWL QQWRFRHMKT 

       250        260        270 
VERIIGHKMG TGGSSGVSYL KRVLDQRFFP ELWNVRTKL 

« Hide

References

[1]"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. expand/collapse author list , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
Nature 423:81-86(2003) [PubMed: 12721629] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames / isolate Porton.
[2]"Complete genome sequence of Bacillus anthracis Sterne."
Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sterne.
[3]"Bacillus anthracis comparative genomics."
Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames ancestor.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016879 Genomic DNA. Translation: AAP26587.1.
AE017334 Genomic DNA. Translation: AAT31867.1.
AE017225 Genomic DNA. Translation: AAT54875.1.
RefSeqNP_845101.1. NC_003997.3.
YP_019392.1. NC_007530.2.
YP_028824.1. NC_005945.1.

3D structure databases

HSSPHSSP built from PDB template 1YW0 based on UniProtKB Q8PDA8.
ProteinModelPortalQ81PQ0.
SMRQ81PQ0. Positions 20-279.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000008130; EBBACP00000007886; EBBACG00000008122.
EBBACT00000016170; EBBACP00000015791; EBBACG00000016162.
EBBACT00000021185; EBBACP00000020670; EBBACG00000021176.
GeneID1088379.
2819588.
2849155.
GenomeReviewsGene locus BA_2751 in contig AE016879_GR.
Gene locus BAS2565 in contig AE017225_GR.
Gene locus GBAA_2751 in contig AE017334_GR.
KEGGban:BA_2751.
bar:GBAA_2751.
bat:BAS2565.
TIGRBA_2751.
GBAA_2751.

Phylogenomic databases

GeneTreeEBGT00050000004238.
HOGENOMHBG647485.
OMAKLLVDQV.
ProtClustDBCLSK904616.

Enzyme and pathway databases

BioCycBANT260799:BAS2565-MONOMER.
BANT261594:GBAA2751-MONOMER.

Family and domain databases

InterProIPR017485. Trp_2-3-dOase_bac.
IPR004981. Trp_2_3_dOase.
[Graphical view]
KOK00453.
PANTHERPTHR10138. Trp_2_3_dOase. 1 hit.
PfamPF03301. Trp_dioxygenase. 1 hit.
[Graphical view]
TIGRFAMsTIGR03036. Trp_2_3_diox. 1 hit.
ProtoNetSearch...

Entry information

Entry nameT23O_BACAN
AccessionPrimary (citable) accession number: Q81PQ0
Secondary accession number(s): Q6HXW4, Q6KRY6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: June 1, 2003
Last modified: November 16, 2011
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families