T23OA_DANRE
ID T23OA_DANRE Reviewed; 406 AA.
AC A7MBU6; A7E2J5;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Tryptophan 2,3-dioxygenase A {ECO:0000255|HAMAP-Rule:MF_03020};
DE Short=TDO-A {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 A {ECO:0000255|HAMAP-Rule:MF_03020};
DE AltName: Full=Tryptophan oxygenase A {ECO:0000255|HAMAP-Rule:MF_03020};
DE Short=TO-A {ECO:0000255|HAMAP-Rule:MF_03020};
DE Short=TRPO-A {ECO:0000255|HAMAP-Rule:MF_03020};
DE AltName: Full=Tryptophan pyrrolase A {ECO:0000255|HAMAP-Rule:MF_03020};
DE AltName: Full=Tryptophanase A {ECO:0000255|HAMAP-Rule:MF_03020};
GN Name=tdo2a {ECO:0000255|HAMAP-Rule:MF_03020}; Synonyms=tdo2;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Intestine;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; BC150376; AAI50377.1; -; mRNA.
DR EMBL; BC151920; AAI51921.1; -; mRNA.
DR RefSeq; NP_001096086.1; NM_001102616.2.
DR AlphaFoldDB; A7MBU6; -.
DR SMR; A7MBU6; -.
DR STRING; 7955.ENSDARP00000096367; -.
DR PaxDb; A7MBU6; -.
DR PeptideAtlas; A7MBU6; -.
DR Ensembl; ENSDART00000105590; ENSDARP00000096367; ENSDARG00000071429.
DR Ensembl; ENSDART00000186059; ENSDARP00000157202; ENSDARG00000109773.
DR GeneID; 100008541; -.
DR KEGG; dre:100008541; -.
DR CTD; 100008541; -.
DR ZFIN; ZDB-GENE-030131-1187; tdo2a.
DR eggNOG; KOG3906; Eukaryota.
DR GeneTree; ENSGT00390000008593; -.
DR HOGENOM; CLU_045599_1_1_1; -.
DR InParanoid; A7MBU6; -.
DR OMA; MLFIVVH; -.
DR OrthoDB; 896211at2759; -.
DR PhylomeDB; A7MBU6; -.
DR TreeFam; TF105827; -.
DR Reactome; R-DRE-71240; Tryptophan catabolism.
DR UniPathway; UPA00333; UER00453.
DR PRO; PR:A7MBU6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 14.
DR Bgee; ENSDARG00000071429; Expressed in liver and 15 other tissues.
DR ExpressionAtlas; A7MBU6; differential.
DR GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004833; F:tryptophan 2,3-dioxygenase activity; ISS:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:0019442; P:tryptophan catabolic process to acetyl-CoA; IBA:GO_Central.
DR GO; GO:0019441; P:tryptophan catabolic process to kynurenine; ISS: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 2: Evidence at transcript level;
KW Dioxygenase; Heme; Iron; Metal-binding; Oxidoreductase; Reference proteome;
KW Tryptophan catabolism.
FT CHAIN 1..406
FT /note="Tryptophan 2,3-dioxygenase A"
FT /id="PRO_0000360075"
FT BINDING 71..75
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03020"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03020"
FT BINDING 327
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 341
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03020"
FT CONFLICT 144
FT /note="E -> G (in Ref. 1; AAI50377)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="S -> R (in Ref. 1; AAI50377)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="S -> T (in Ref. 1; AAI51921)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 406 AA; 48045 MW; 49DEA8A593CCBF32 CRC64;
MSGCPYFQRK FLSTSKQHLK EEENDEAQTG INKASKGGLI YGDYLQLDKI VTSQVLQSEL
KGNKIHDEHL FIVTHQAYEL WFKQVLWELD SVREIFISGH VRDERNMLKV NTRIHRIVMI
FRLLLDQFAV LETMTALDFY DFREYLSPAS GFQSLQFRLL ENKIGVPHNQ RVPYNRRHYR
DNFRDQESEL LLHSEQEPTL LQLVEQWLER TPGLEEDGFN FWGKLEKNIF EGLRREKEHI
EQKPASERKE EMLAELIKQR DIFLSLFDEK RHDHLVSTGQ RRLSYKALQG ALMIYFYREE
PRFQVPFQLL TSLMDIDTLM TKWRYNHVCM VHRMIGSKDG TGGSSGYQYL RSTVSDRYKV
FVDLFNLATF LIPRDWVPKL DPSEHTFLYM AECCDSSYCS SSDDSD
