T23OB_DANRE
ID T23OB_DANRE Reviewed; 407 AA.
AC Q7SY53;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Tryptophan 2,3-dioxygenase B {ECO:0000255|HAMAP-Rule:MF_03020};
DE Short=TDO-B {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 B {ECO:0000255|HAMAP-Rule:MF_03020};
DE AltName: Full=Tryptophan oxygenase B {ECO:0000255|HAMAP-Rule:MF_03020};
DE Short=TO-B {ECO:0000255|HAMAP-Rule:MF_03020};
DE Short=TRPO-B {ECO:0000255|HAMAP-Rule:MF_03020};
DE AltName: Full=Tryptophan pyrrolase B {ECO:0000255|HAMAP-Rule:MF_03020};
DE AltName: Full=Tryptophanase B {ECO:0000255|HAMAP-Rule:MF_03020};
GN Name=tdo2b {ECO:0000255|HAMAP-Rule:MF_03020}; Synonyms=tdo2, tdo2l;
GN ORFNames=zgc:63488;
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 STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2003) 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; BC055123; AAH55123.1; -; mRNA.
DR RefSeq; NP_956150.1; NM_199856.1.
DR AlphaFoldDB; Q7SY53; -.
DR SMR; Q7SY53; -.
DR STRING; 7955.ENSDARP00000035102; -.
DR PaxDb; Q7SY53; -.
DR PRIDE; Q7SY53; -.
DR GeneID; 334082; -.
DR KEGG; dre:334082; -.
DR CTD; 334082; -.
DR ZFIN; ZDB-GENE-030131-6014; tdo2b.
DR eggNOG; KOG3906; Eukaryota.
DR InParanoid; Q7SY53; -.
DR OrthoDB; 896211at2759; -.
DR PhylomeDB; Q7SY53; -.
DR UniPathway; UPA00333; UER00453.
DR PRO; PR:Q7SY53; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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..407
FT /note="Tryptophan 2,3-dioxygenase B"
FT /id="PRO_0000247475"
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"
SQ SEQUENCE 407 AA; 47422 MW; 8EA9740C0D4F3912 CRC64;
MSGCPFLGGT LQLLSSNPRQ AEEEDGSQGG VNKAAKGGII YGDYLQLDKV LNAQVLQSEQ
KGNKIHDEHL FIVTHQAYEL WFKQILWELD SVRDLFIKKH VRDERNMLKV VSRIHRITMI
FKLLVDQFAV LETMTALDFF DFREYLSPAS GFQSLQFRLL EQKIGVADHL RVPYNRRHYR
DNFHGEESET LLSSEQEPTL LQLVEQWLER TPGLEKDGFN FWGKLQANIE EGLKREKHQV
EKMEDTEVKQ ELLEDLNKQM ETFTALFDSK RHEHLLSKGE RRLSYKALQG ALMINFYREE
PRFQVPFQLL TALMEIDTLM TKWRYNHVCM VHRMIGSKAG TGGSSGYHYL RSTVSDRYKV
FVDLFNLATF LVPRSWVPKL NPNIHKFPYT AECYDSSYNS CSSEDSD
