ID   C6WFN6_ACTMD            Unreviewed;       299 AA.
AC   C6WFN6;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   02-SEP-2026, entry version 85.
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=kynA {ECO:0000256|HAMAP-Rule:MF_01972};
GN   OrderedLocusNames=Amir_2024 {ECO:0000313|EMBL:ACU35971.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064
OS   / NCIMB 13271 / NRRL B-12336 / IMRU 3971 / 101).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU35971.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU35971.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064 / NCIMB 13271 /
RC   NRRL B-12336 / IMRU 3971 / 101 {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D., Goodwin L.,
RA   Pitluck S., Rohde M., Goker M., Pati A., Ivanova N., Mavromatis K.,
RA   Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.C., Brettin T.,
RA   Detter J.C., Han C., Chain P., Tindall B.J., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(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: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; CP001630; ACU35971.1; -; Genomic_DNA.
DR   RefSeq; WP_015800860.1; NC_013093.1.
DR   AlphaFoldDB; C6WFN6; -.
DR   STRING; 446462.Amir_2024; -.
DR   KEGG; ami:Amir_2024; -.
DR   eggNOG; COG3483; Bacteria.
DR   HOGENOM; CLU_063240_0_0_11; -.
DR   OrthoDB; 9776847at2; -.
DR   UniPathway; UPA00333; UER00453.
DR   Proteomes; UP000002213; Chromosome.
DR   GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004833; F:L-tryptophan 2,3-dioxygenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006569; P:L-tryptophan catabolic process; IEA:UniProtKB-ARBA.
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; 1.
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:ACU35971.1};
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:UP000002213};
KW   Tryptophan catabolism {ECO:0000256|HAMAP-Rule:MF_01972}.
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         134
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01972"
FT   BINDING         257
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         271
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01972"
SQ   SEQUENCE   299 AA;  33145 MW;  254FD049836D8BAC CRC64;
     MTAPGRNGSA QASPGTGDAE HDVRVMAPDG CPITDVTGTS TPYIDYQSID VLLSLQRPRS
     DTPAELTFYV IGQVKELLFK LIHEELERTR ALIDGDSVAE AAANLRRVRR VVELLNETWN
     VLSTLTPNEF NGFRDVLGKA SGLQSYMYRM VEYALGNKVA ALAQPHRQVP HVHAQVQRAL
     REPSVYDAAL RLLARRGAAL PESVLDRDFS RPYEPNGAVE RAWADVYRGN AATDPLPQLA
     EALMDVAEGF SRWRSLHLLT VERVIGFKPG TGGTEGAGWL RRVAEHRFFP ELWTCRGLL
//