ID   D7CCR7_STRBB            Unreviewed;       280 AA.
AC   D7CCR7;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=Tryptophan 2,3-dioxygenase {ECO:0000256|HAMAP-Rule:MF_01972};
DE            Short=TDO {ECO:0000256|HAMAP-Rule:MF_01972};
DE            EC=1.13.11.11 {ECO:0000256|HAMAP-Rule:MF_01972};
DE   AltName: Full=Tryptamin 2,3-dioxygenase {ECO:0000256|HAMAP-Rule:MF_01972};
DE   AltName: Full=Tryptophan oxygenase {ECO:0000256|HAMAP-Rule:MF_01972};
DE            Short=TO {ECO:0000256|HAMAP-Rule:MF_01972};
DE            Short=TRPO {ECO:0000256|HAMAP-Rule:MF_01972};
DE   AltName: Full=Tryptophan pyrrolase {ECO:0000256|HAMAP-Rule:MF_01972};
DE   AltName: Full=Tryptophanase {ECO:0000256|HAMAP-Rule:MF_01972};
GN   Name=tdo {ECO:0000313|EMBL:ADI08798.1};
GN   Synonyms=kynA {ECO:0000256|HAMAP-Rule:MF_01972};
GN   OrderedLocusNames=SBI_05678 {ECO:0000313|EMBL:ADI08798.1};
OS   Streptomyces bingchenggensis (strain BCW-1).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI08798.1, ECO:0000313|Proteomes:UP000000377};
RN   [1] {ECO:0000313|EMBL:ADI08798.1, ECO:0000313|Proteomes:UP000000377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCW-1 {ECO:0000313|EMBL:ADI08798.1,
RC   ECO:0000313|Proteomes:UP000000377};
RX   PubMed=20581206; DOI=10.1128/JB.00596-10;
RA   Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L.,
RA   Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X.,
RA   Xiang W.S.;
RT   "Genome sequence of the milbemycin-producing bacterium Streptomyces
RT   bingchenggensis.";
RL   J. Bacteriol. 192:4526-4527(2010).
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:0000256|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:0000256|HAMAP-
CC         Rule:MF_01972};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01972};
CC       Note=Binds 1 heme group per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01972}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01972}.
CC   -!- SIMILARITY: Belongs to the tryptophan 2,3-dioxygenase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01972}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01972}.
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DR   EMBL; CP002047; ADI08798.1; -; Genomic_DNA.
DR   RefSeq; WP_014178262.1; NC_016582.1.
DR   AlphaFoldDB; D7CCR7; -.
DR   STRING; 749414.SBI_05678; -.
DR   KEGG; sbh:SBI_05678; -.
DR   PATRIC; fig|749414.3.peg.5863; -.
DR   eggNOG; COG3483; Bacteria.
DR   HOGENOM; CLU_063240_0_0_11; -.
DR   UniPathway; UPA00333; UER00453.
DR   Proteomes; UP000000377; Chromosome.
DR   GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004833; F:tryptophan 2,3-dioxygenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.20.58.480; -; 1.
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; TRYPTOPHAN 2,3-DIOXYGENASE; 1.
DR   PANTHER; PTHR10138:SF0; TRYPTOPHAN 2,3-DIOXYGENASE; 1.
DR   Pfam; PF03301; Trp_dioxygenase; 2.
DR   SUPFAM; SSF140959; Indolic compounds 2,3-dioxygenase-like; 1.
PE   3: Inferred from homology;
KW   Dioxygenase {ECO:0000256|HAMAP-Rule:MF_01972, ECO:0000313|EMBL:ADI08798.1};
KW   Heme {ECO:0000256|HAMAP-Rule:MF_01972};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01972};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01972};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01972};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000377};
KW   Tryptophan catabolism {ECO:0000256|HAMAP-Rule:MF_01972}.
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01972"
FT   BINDING         238
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:0000256|HAMAP-Rule:MF_01972"
FT   BINDING         252
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01972"
SQ   SEQUENCE   280 AA;  31295 MW;  055168D4364F2952 CRC64;
     MSHQPAPHEA EPDTPNLDFQ GTTPYEDYVQ ASVLTHLQHP LSDDPGEMVF LVTTQVMELW
     FTVIVHEWQT AAQALREDDL PTALAALKRS TYELESLNAS WKPLAHLTPG QFNSYRSALG
     EGSGFQSAMY RRMEFLLGEK SASMLVPHRG APRVHGELEK ALTEPSLYDE VLGYLARQGY
     AVPESVLDRD PTRRYEPDAA VERVWQEIYS GPDDTAPARL GEALTEVAEL VWRWRNDHLV
     ATRRAMGAKA GTGGSAGVAW LEKRATKNVF PELWTARSHV
//