Reviewed, UniProtKB/Swiss-Prot Q1LK00 (T23O_RALME)

Names and origin

Protein names

Recommended name:
    Tryptophan 2,3-dioxygenase
      Short name=TDO
    EC=1.13.11.11
Alternative name(s):
    Tryptophan pyrrolase
      Short name=Tryptophanase
    Tryptophan oxygenase
      Short name=TRPO
      Short name=TO
    Tryptamin 2,3-dioxygenase

Gene names

Name:	kynA
Ordered Locus Names:	Rmet_2651

Organism

Ralstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839) [Complete proteome] [HAMAP]

Taxonomic identifier

266264 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

Protein attributes

Sequence length	299 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring. Ref.2 Ref.3
Catalytic activity	L-tryptophan + O2 = N-formyl-L-kynurenine. Ref.2 Ref.3
Cofactor	Binds 2 heme groups per tetramer.
Pathway	Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 1/2.
Subunit structure	Homotetramer. Ref.3
Sequence similarities	Belongs to the tryptophan 2,3-dioxygenase family.
Biophysicochemical properties	Kinetic parameters: KM=350 µM for tryptophan

Ontologies

Keywords
Biological process	Tryptophan catabolism
Ligand	Heme Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	NAD biosynthetic process Ref.3 Non-traceable author statement. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW protein homooligomerization Ref.3 Inferred from direct assay. Source: UniProtKB quinolinate biosynthetic process Ref.3 Non-traceable author statement. Source: UniProtKB tryptophan catabolic process to kynurenine Ref.3 Inferred from direct assay. Source: UniProtKB
Molecular function	heme binding Ref.3 Inferred from direct assay. Source: UniProtKB tryptophan 2,3-dioxygenase activity Ref.3 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 299

299

Tryptophan 2,3-dioxygenase

PRO_0000360128

Regions

Region

43 – 47

5

Substrate binding By similarity

Region

68 – 72

5

Substrate binding Probable

Sites

Metal binding

257

1

Iron (heme axial ligand)

Binding site

130

1

Substrate Probable

Binding site

134

1

Substrate Probable

Binding site

141

1

Heme

Binding site

271

1

Substrate Probable

Experimental info

Mutagenesis

68

1

F → A: Abolishes catalytic activity. Ref.3

Mutagenesis

130

1

Y → F: 15-fold increase in catalytic activity. Ref.3

Mutagenesis

134

1

R → A: Abolishes catalytic activity. Ref.3

Mutagenesis

271

1

T → A: Abolishes catalytic activity. Ref.3

Secondary structure

1

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299

Helix Strand Turn

Details...

Helix

52 – 54

3

Helix

65 – 90

26

Helix

98 – 117

20

Helix

119 – 122

4

Helix

127 – 133

7

Helix

134 – 136

3

Helix

146 – 154

9

Helix

160 – 166

7

Helix

170 – 181

12

Helix

185 – 195

11

Helix

202 – 205

4

Helix

217 – 228

12

Helix

230 – 233

4

Helix

234 – 238

5

Helix

242 – 264

23

Helix

278 – 283

6

Helix

290 – 298

9

Sequences

	Sequence		Length	Mass (Da)
	Q1LK00-1 [UniParc]. Last modified May 30, 2006. Version 1. Checksum: 735273ABF87FA296	FASTA	299	34,304
	10 20 30 40 50 60 MSEFKGCPMG HGAAPQNGDG GDSGDTGNGW HGAQMDFARD MSYGDYLGLD QILSAQHPLS 70 80 90 100 110 120 PDHNEMLFIV QHQTTELWMK LMLHELRAAR DGVKSDQLQP AFKMLARVSR IMDQLVQAWN 130 140 150 160 170 180 VLATMTPPEY SAMRPYLGAS SGFQSYQYRE IEFILGNKNA AMLRPHAHRP EHLELVETAL 190 200 210 220 230 240 HTPSMYDEAI RLMARRGFQI DPEVVERDWT QPTQYNASVE AAWLEVYRNP SAHWELYELG 250 260 270 280 290 EKFVDLEDAF RQWRFRHVTT VERVIGFKRG TGGTEGVSYL RRMLDVVLFP ELWKLRTDL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequence of the chromosome of Ralstonia metallidurans CH34." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Martinez M., Goltsman E., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. , Kim E., Mergeay M., Benotmane M.A., Vallaeys T., Michaux A., Monchy S., Dunn J., McCorkle S., Taghavi S., van der Lelie D., Richardson P. Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"NAD biosynthesis: identification of the tryptophan to quinolinate pathway in bacteria." Kurnasov O., Goral V., Colabroy K., Gerdes S., Anantha S., Osterman A., Begley T.P. Chem. Biol. 10:1195-1204(2003) [PubMed: 14700627] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
[3]	"Crystal structure and mechanism of tryptophan 2,3-dioxygenase, a heme enzyme involved in tryptophan catabolism and in quinolinate biosynthesis." Zhang Y., Kang S.A., Mukherjee T., Bale S., Crane B.R., Begley T.P., Ealick S.E. Biochemistry 46:145-155(2007) [PubMed: 17198384] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 19-299 IN COMPLEX WITH HEME, FUNCTION, CATALYTIC ACTIVITY, HOMOTETRAMERIZATION, MUTAGENESIS OF PHE-68; TYR-130; ARG-134 AND THR-271.

Cross-references

Sequence databases

EMBLGenBankDDBJ

CP000352 Genomic DNA. Translation: ABF09526.1.

RefSeq

YP_584795.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2NOX	X-ray	2.40	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P	19-299	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q1LK00.

Genome annotation databases

GeneID

4039476.

GenomeReviews

Gene locus Rmet_2651 in contig CP000352_GR.

KEGG

rme:Rmet_2651.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

Q1LK00.

OMA

MKLILHE.

Enzyme and pathway databases

BioCyc

RMET266264:RMET_2651-MON.

Family and domain databases

InterPro

IPR017485. Trp_2-3-dOase_bac.
IPR004981. Trp_2_3_dOase.
[Graphical view]

PANTHER

PTHR10138. Trp_2_3_dOase. 1 hit.

Pfam

PF03301. Trp_dioxygenase. 1 hit.
[Graphical view]

TIGRFAMs

TIGR03036. trp_2_3_diox. 1 hit.

ProtoNet

Search...

Entry information

Entry name

T23O_RALME

Accession

Primary (citable) accession number: Q1LK00

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	May 30, 2006
Last modified:	November 3, 2009
This is version 26 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)