T23O_BOVIN
ID T23O_BOVIN Reviewed; 406 AA.
AC Q2KIQ5;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=TDO2 {ECO:0000255|HAMAP-Rule:MF_03020};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) 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; BC112550; AAI12551.1; -; mRNA.
DR RefSeq; NP_001039778.1; NM_001046313.1.
DR AlphaFoldDB; Q2KIQ5; -.
DR SMR; Q2KIQ5; -.
DR STRING; 9913.ENSBTAP00000014690; -.
DR PaxDb; Q2KIQ5; -.
DR PRIDE; Q2KIQ5; -.
DR Ensembl; ENSBTAT00000014690; ENSBTAP00000014690; ENSBTAG00000011062.
DR GeneID; 530397; -.
DR KEGG; bta:530397; -.
DR CTD; 6999; -.
DR VEuPathDB; HostDB:ENSBTAG00000011062; -.
DR VGNC; VGNC:35712; TDO2.
DR eggNOG; KOG3906; Eukaryota.
DR GeneTree; ENSGT00390000008593; -.
DR HOGENOM; CLU_045599_1_1_1; -.
DR InParanoid; Q2KIQ5; -.
DR OMA; WRWRNDH; -.
DR OrthoDB; 896211at2759; -.
DR TreeFam; TF105827; -.
DR UniPathway; UPA00333; UER00453.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000011062; Expressed in liver and 22 other tissues.
DR ExpressionAtlas; Q2KIQ5; baseline.
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; Phosphoprotein;
KW Reference proteome; Tryptophan catabolism.
FT CHAIN 1..406
FT /note="Tryptophan 2,3-dioxygenase"
FT /id="PRO_0000247474"
FT BINDING 72..76
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03020"
FT BINDING 144
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"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21643"
SQ SEQUENCE 406 AA; 47708 MW; D68CD8A6BC59A882 CRC64;
MSGCPFLGKS FGYAFKPLSA QGSEEDKSQA GVNRASKGGL IYGNYLQLEK VLNAQELQSE
MKGNKIHDEH LFIITHQAYE LWFKQILWEL DSVREIFQNG HVRDERNMLK VITRMHRVVV
ILKLLVQQFS VLETMTALDF NDFREYLSPA SGFQSLQFRL LENKIGVLQS LRVPYNRRHY
RDNFRGKDNE LLLKSEQERT LLQLVEAWLE RTPGLEPHGF NFWGKLEKNI VKGLEEEFTK
IQAKEESEEK EEQMAEFQKQ KEVLLSLFDE KRHEHLLSKG ERRLSYKALQ GALMIYFYRE
EPRFQVPFQL LTFLMDVDSL MTKWRYNHVC LVHRMLGSKA GTGGSSGYQY LRSTVSDRYK
VFVDLFNLST YLVPRHWIPK MNPVIHKFLY TAEYCDSSYF SSDESD
