T23O_ERYLH
ID T23O_ERYLH Reviewed; 263 AA.
AC Q2N5X1;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Tryptophan 2,3-dioxygenase {ECO:0000255|HAMAP-Rule:MF_01972};
DE Short=TDO {ECO:0000255|HAMAP-Rule:MF_01972};
DE EC=1.13.11.11 {ECO:0000255|HAMAP-Rule:MF_01972};
DE AltName: Full=Tryptamin 2,3-dioxygenase {ECO:0000255|HAMAP-Rule:MF_01972};
DE AltName: Full=Tryptophan oxygenase {ECO:0000255|HAMAP-Rule:MF_01972};
DE Short=TO {ECO:0000255|HAMAP-Rule:MF_01972};
DE Short=TRPO {ECO:0000255|HAMAP-Rule:MF_01972};
DE AltName: Full=Tryptophan pyrrolase {ECO:0000255|HAMAP-Rule:MF_01972};
DE AltName: Full=Tryptophanase {ECO:0000255|HAMAP-Rule:MF_01972};
GN Name=kynA {ECO:0000255|HAMAP-Rule:MF_01972}; OrderedLocusNames=ELI_14140;
OS Erythrobacter litoralis (strain HTCC2594).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=314225;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2594;
RX PubMed=19168610; DOI=10.1128/jb.00026-09;
RA Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.;
RT "Complete genome sequence of Erythrobacter litoralis HTCC2594.";
RL J. Bacteriol. 191:2419-2420(2009).
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_01972}.
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_01972};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01972};
CC Note=Binds 1 heme group per subunit. {ECO:0000255|HAMAP-Rule:MF_01972};
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_01972}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01972}.
CC -!- SIMILARITY: Belongs to the tryptophan 2,3-dioxygenase family.
CC {ECO:0000255|HAMAP-Rule:MF_01972}.
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DR EMBL; CP000157; ABC64920.1; -; Genomic_DNA.
DR RefSeq; WP_011415742.1; NC_007722.1.
DR AlphaFoldDB; Q2N5X1; -.
DR SMR; Q2N5X1; -.
DR STRING; 314225.ELI_14140; -.
DR EnsemblBacteria; ABC64920; ABC64920; ELI_14140.
DR KEGG; eli:ELI_14140; -.
DR eggNOG; COG3483; Bacteria.
DR HOGENOM; CLU_063240_0_0_5; -.
DR OMA; WRWRNDH; -.
DR OrthoDB; 1660023at2; -.
DR UniPathway; UPA00333; UER00453.
DR Proteomes; UP000008808; Chromosome.
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: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; 2.
DR Pfam; PF03301; Trp_dioxygenase; 2.
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..263
FT /note="Tryptophan 2,3-dioxygenase"
FT /id="PRO_0000360114"
FT BINDING 32..36
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
FT BINDING 221
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_01972"
FT BINDING 235
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
SQ SEQUENCE 263 AA; 30341 MW; 35222157E9DEDA18 CRC64;
MAQDVTYSSY LDLDRILAAQ HPVSGAHDEM LFIIVHQASE LWLKLCLHEL FAARDCIAAD
NLRPSFKMLS RVARAQTQLI QSWDVLSTMT PHDYSQIRPH LGRSSGFQSP QYRMMEFLLG
GRNPDMVAMH EPTPEIATAL REELARTSLY DEAIRLLSRR GFAIPDEVLA RKLDEVWVRS
EEVEAAWAEI YRDPQQHWDL YELAEKLVDL EYHFQRWRFG HLKTVERIIG FKRGTGGTKG
VPYLEGVLKQ AFFPELLSVR TAI
