ID   T23O_ALTMD              Reviewed;         362 AA.
AC   B4RUH2; F2G4T0;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
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};
GN   OrderedLocusNames=MADE_1006210;
OS   Alteromonas mediterranea (strain DSM 17117 / CIP 110805 / LMG 28347 / Deep
OS   ecotype).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX   NCBI_TaxID=1774373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17117 / CIP 110805 / LMG 28347 / Deep ecotype;
RX   PubMed=18670397; DOI=10.1038/ismej.2008.74;
RA   Ivars-Martinez E., Martin-Cuadrado A.-B., D'Auria G., Mira A., Ferriera S.,
RA   Johnson J., Friedman R., Rodriguez-Valera F.;
RT   "Comparative genomics of two ecotypes of the marine planktonic copiotroph
RT   Alteromonas macleodii suggests alternative lifestyles associated with
RT   different kinds of particulate organic matter.";
RL   ISME J. 2:1194-1212(2008).
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; CP001103; AEA97384.1; -; Genomic_DNA.
DR   RefSeq; WP_012517726.1; NC_011138.3.
DR   AlphaFoldDB; B4RUH2; -.
DR   SMR; B4RUH2; -.
DR   PRIDE; B4RUH2; -.
DR   EnsemblBacteria; AEA97384; AEA97384; MADE_1006210.
DR   KEGG; amc:MADE_1006210; -.
DR   HOGENOM; CLU_045599_1_1_6; -.
DR   OMA; MLFIVVH; -.
DR   UniPathway; UPA00333; UER00453.
DR   Proteomes; UP000001870; 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; 1.
DR   Pfam; PF03301; Trp_dioxygenase; 1.
DR   SUPFAM; SSF140959; SSF140959; 1.
PE   3: Inferred from homology;
KW   Dioxygenase; Heme; Iron; Metal-binding; Oxidoreductase;
KW   Tryptophan catabolism.
FT   CHAIN           1..362
FT                   /note="Tryptophan 2,3-dioxygenase"
FT                   /id="PRO_0000360079"
FT   BINDING         40..44
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
FT   BINDING         111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
FT   BINDING         297
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         311
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
SQ   SEQUENCE   362 AA;  42791 MW;  955EDB34A2D407A2 CRC64;
     MKKNIEPCYY GDYLQLDKIL GAQDLQSEKY GDGAHEEMLF IIVHQVYELW FKQVLHELNA
     VIDTFNQEAV KDQQLTQVVH RLQRIIQIQK LMNDQIAIME TMTPQQFLSF RDYLVPASGF
     QSIQFKRLEI SLGLKREFRI DFDKQSFYNR LTDKDRALLE NLENKPSLFE LVDKWLSRMP
     LLKTEDFDFW QYYKDAADEM LKDDHHTVST SDMLSDTEKR QEIKDLQATM ENFDALFNET
     QFEKLRGEGK FRLSHNALLS ALFIKQYSEE PIFNLPFQLI TALTEIDEQL TIWRYRHAMM
     VQRMLGTKIG TGGSSGHHYL KKTTESNRIY LDFFNMATFL LPKSALPDLP ESVRRRLGFY
     LQ