T23O_CAEBR
ID T23O_CAEBR Reviewed; 404 AA.
AC A8X7X9;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
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 Name=tdo-2 {ECO:0000312|WormBase:CBG09046};
GN ORFNames=CBG09046 {ECO:0000312|WormBase:CBG09046};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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 (By similarity). Involved in regulation of protein
CC homeostasis, longevity and reproducive life span. Specifically
CC regulates proteotoxicity due to age-related aggregation of proteins
CC like alpha-synuclein, via its effects on tryptophan metabolism (By
CC similarity). {ECO:0000250|UniProtKB:Q09474, ECO:0000255|HAMAP-
CC Rule:MF_03020}.
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};
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 -!- 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 -!- 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}.
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DR EMBL; HE601284; CAP28740.1; -; Genomic_DNA.
DR RefSeq; XP_002641185.1; XM_002641139.1.
DR AlphaFoldDB; A8X7X9; -.
DR SMR; A8X7X9; -.
DR STRING; 6238.CBG09046; -.
DR PRIDE; A8X7X9; -.
DR EnsemblMetazoa; CBG09046.1; CBG09046.1; WBGene00030713.
DR GeneID; 8583178; -.
DR KEGG; cbr:CBG_09046; -.
DR CTD; 8583178; -.
DR WormBase; CBG09046; CBP02210; WBGene00030713; Cbr-tdo-2.
DR eggNOG; KOG3906; Eukaryota.
DR HOGENOM; CLU_045599_1_1_1; -.
DR InParanoid; A8X7X9; -.
DR OMA; WRWRNDH; -.
DR OrthoDB; 896211at2759; -.
DR UniPathway; UPA00333; UER00453.
DR Proteomes; UP000008549; Chromosome III.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004833; F:tryptophan 2,3-dioxygenase activity; IBA:GO_Central.
DR GO; GO:0019442; P:tryptophan catabolic process to acetyl-CoA; IBA:GO_Central.
DR GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IEA:UniProtKB-UniPathway.
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 3: Inferred from homology;
KW Dioxygenase; Heme; Iron; Metal-binding; Oxidoreductase; Reference proteome;
KW Tryptophan catabolism.
FT CHAIN 1..404
FT /note="Tryptophan 2,3-dioxygenase"
FT /id="PRO_0000360076"
FT BINDING 70..74
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03020"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03020"
FT BINDING 328
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 342
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03020"
SQ SEQUENCE 404 AA; 46862 MW; B648B49A4E18D250 CRC64;
MACPYMNGGD TLPHRVTFME GGEECQQGVN KVEMGFGQTY PEYLQLDKIL TAQKLKSEAD
GQRVDDEHLF IVIHQAHELW FKQIIFDLDI VRKLLNNTIV DETKTLKIVS GLDRIVKILS
LLTEQITLLD TMSPLDFVDF RKYLTPASGF QSLQFRILEN KLGVKQERRI KYNAQHYKNV
FNDDDLKALN TTEDEKSLLT LIESWLERTP GLKSTSEDEG FWSKYESSVN KYLSDLAKQA
EDPSNTEEIK KQLRAEYSKT SDAFQSILDP RQHEQHIRNG NRLLSHDATK GAMMIYFYRD
MPRFSQPYQI LTFLMDIDSL FTKWRYNHVL LVQRMLGAKQ GTGGSSGYMY LRSTVSDRYK
VFLDLFNLST WLIPREYIPM LSPRMVKTLS EHSNLSHSQS SESE
