T23O_AEDAE
ID T23O_AEDAE Reviewed; 393 AA.
AC Q17P71; Q8WSB3;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Tryptophan 2,3-dioxygenase {ECO:0000255|HAMAP-Rule:MF_03020};
DE Short=TDO {ECO:0000255|HAMAP-Rule:MF_03020};
DE EC=1.13.11.11 {ECO:0000255|HAMAP-Rule:MF_03020};
DE AltName: Full=Tryptamin 2,3-dioxygenase {ECO:0000255|HAMAP-Rule:MF_03020};
DE AltName: Full=Tryptophan oxygenase {ECO:0000255|HAMAP-Rule:MF_03020};
DE Short=TO {ECO:0000255|HAMAP-Rule:MF_03020};
DE Short=TRPO {ECO:0000255|HAMAP-Rule:MF_03020};
DE AltName: Full=Tryptophan pyrrolase {ECO:0000255|HAMAP-Rule:MF_03020};
DE AltName: Full=Tryptophanase {ECO:0000255|HAMAP-Rule:MF_03020};
GN ORFNames=AAEL000428;
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17212352; DOI=10.1002/arch.20159;
RA Li J.S., Han Q., Fang J., Rizzi M., James A.A., Li J.;
RT "Biochemical mechanisms leading to tryptophan 2,3-dioxygenase activation.";
RL Arch. Insect Biochem. Physiol. 64:74-87(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVPib12;
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
CC -!- FUNCTION: Heme-dependent dioxygenase that catalyzes the oxidative
CC cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-
CC tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage
CC of the indole moiety. {ECO:0000255|HAMAP-Rule:MF_03020,
CC ECO:0000269|PubMed:17212352}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tryptophan + O2 = N-formyl-L-kynurenine;
CC Xref=Rhea:RHEA:24536, ChEBI:CHEBI:15379, ChEBI:CHEBI:57912,
CC ChEBI:CHEBI:58629; EC=1.13.11.11; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03020, ECO:0000269|PubMed:17212352};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03020};
CC Note=Binds 1 heme group per subunit. {ECO:0000255|HAMAP-Rule:MF_03020};
CC -!- ACTIVITY REGULATION: Stimulated by low concentrations of hydrogen
CC peroxide (5 uM), ascorbate (0.1-0.3 mM), and sodium hydrosulfite (0.1
CC mM). Inhibited by high concentrations of hydrogen peroxide (0.1 mM),
CC ascorbate (10 mM), and sodium hydrosulfite (1 mM).
CC {ECO:0000269|PubMed:17212352}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:17212352};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:17212352};
CC -!- PATHWAY: Amino-acid degradation; L-tryptophan degradation via
CC kynurenine pathway; L-kynurenine from L-tryptophan: step 1/2.
CC {ECO:0000255|HAMAP-Rule:MF_03020}.
CC -!- PATHWAY: Pigment biosynthesis; ommochrome biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03020}.
CC -!- SUBUNIT: Homotetramer. Dimer of dimers. {ECO:0000255|HAMAP-
CC Rule:MF_03020}.
CC -!- SIMILARITY: Belongs to the tryptophan 2,3-dioxygenase family.
CC {ECO:0000255|HAMAP-Rule:MF_03020}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF325458; AAL37360.1; -; mRNA.
DR EMBL; CH477193; EAT48562.1; -; Genomic_DNA.
DR RefSeq; XP_001656460.1; XM_001656410.1.
DR AlphaFoldDB; Q17P71; -.
DR SMR; Q17P71; -.
DR STRING; 7159.AAEL000428-PA; -.
DR GeneID; 5577377; -.
DR KEGG; aag:5577377; -.
DR VEuPathDB; VectorBase:AAEL000428; -.
DR eggNOG; KOG3906; Eukaryota.
DR HOGENOM; CLU_045599_1_1_1; -.
DR InParanoid; Q17P71; -.
DR OMA; WRWRNDH; -.
DR OrthoDB; 237272at2759; -.
DR PhylomeDB; Q17P71; -.
DR BRENDA; 1.13.11.52; 149.
DR UniPathway; UPA00271; -.
DR UniPathway; UPA00333; UER00453.
DR Proteomes; UP000008820; Chromosome 3.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004833; F:tryptophan 2,3-dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0006727; P:ommochrome biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IDA:UniProtKB.
DR HAMAP; MF_01972; T23O; 1.
DR InterPro; IPR037217; Trp/Indoleamine_2_3_dOase-like.
DR InterPro; IPR004981; Trp_2_3_dOase.
DR PANTHER; PTHR10138; PTHR10138; 1.
DR Pfam; PF03301; Trp_dioxygenase; 1.
DR SUPFAM; SSF140959; SSF140959; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Heme; Iron; Metal-binding; Oxidoreductase; Reference proteome;
KW Tryptophan catabolism.
FT CHAIN 1..393
FT /note="Tryptophan 2,3-dioxygenase"
FT /id="PRO_0000360077"
FT BINDING 56..60
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03020"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03020"
FT BINDING 312
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03020"
FT BINDING 327
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03020"
FT CONFLICT 293
FT /note="Q -> R (in Ref. 1; AAL37360)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 393 AA; 45412 MW; 6DF3EEF489EBC2F9 CRC64;
MSCPVGNHNG DPQGGQRLGS EAGMLYGEYL MLDKVLSAQR MLSVESNKPV HDEHLFIVTH
QAYELWFKQI IFELDSIRSL FSTEHMEESR TLEILKRLNR IVMILKLLVD QVPILETMTP
LDFMDFRDFL SPASGFQSLQ FRLLENKLGV KTEHRVKYNQ KYSEVFASDP CAIERLSITE
SEPSLADLVQ KWLERTPGLE TNGFNFWGKF EESVEQLLAD QEASAMEEEH ENVKNYRLMD
IEKRREVYKS IFDASVHDAL VARGDRRFTH RALQGAIMIT FYRDEPRFSQ PHQLLMLLMD
IDSLITKWRY NHVIMVQRMI GSQQLGTGGS SGYQYLRSTL SDRYKVFIDL FNLSTFLIPR
GSIPPLTCEM QKALNLAWGS PVHQAKQINY AAK
