位置:首页 > 蛋白库 > T23O_DROER
T23O_DROER
ID   T23O_DROER              Reviewed;         379 AA.
AC   B3NVC6;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Tryptophan 2,3-dioxygenase {ECO:0000255|HAMAP-Rule:MF_03020};
DE            Short=TDO {ECO:0000255|HAMAP-Rule:MF_03020};
DE            EC=1.13.11.11 {ECO:0000255|HAMAP-Rule:MF_03020};
DE   AltName: Full=Protein vermilion {ECO:0000255|HAMAP-Rule:MF_03020};
DE   AltName: Full=Tryptamin 2,3-dioxygenase {ECO:0000255|HAMAP-Rule:MF_03020};
DE   AltName: Full=Tryptophan oxygenase {ECO:0000255|HAMAP-Rule:MF_03020};
DE            Short=TO {ECO:0000255|HAMAP-Rule:MF_03020};
DE            Short=TRPO {ECO:0000255|HAMAP-Rule:MF_03020};
DE   AltName: Full=Tryptophan pyrrolase {ECO:0000255|HAMAP-Rule:MF_03020};
DE   AltName: Full=Tryptophanase {ECO:0000255|HAMAP-Rule:MF_03020};
GN   Name=v {ECO:0000255|HAMAP-Rule:MF_03020}; ORFNames=GG18380;
OS   Drosophila erecta (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7220;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14021-0224.01;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
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   -!- PATHWAY: Pigment biosynthesis; ommochrome biosynthesis.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CH954180; EDV46114.1; -; Genomic_DNA.
DR   RefSeq; XP_001977187.1; XM_001977151.2.
DR   AlphaFoldDB; B3NVC6; -.
DR   SMR; B3NVC6; -.
DR   STRING; 7220.FBpp0136926; -.
DR   EnsemblMetazoa; FBtr0138434; FBpp0136926; FBgn0110596.
DR   GeneID; 6551492; -.
DR   KEGG; der:6551492; -.
DR   eggNOG; KOG3906; Eukaryota.
DR   HOGENOM; CLU_045599_1_1_1; -.
DR   OMA; WRWRNDH; -.
DR   OrthoDB; 896211at2759; -.
DR   PhylomeDB; B3NVC6; -.
DR   UniPathway; UPA00271; -.
DR   UniPathway; UPA00333; UER00453.
DR   Proteomes; UP000008711; Unassembled WGS sequence.
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:0006727; P:ommochrome biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:1901216; P:positive regulation of neuron death; IEA:EnsemblMetazoa.
DR   GO; GO:0051289; P:protein homotetramerization; IEA:EnsemblMetazoa.
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..379
FT                   /note="Tryptophan 2,3-dioxygenase"
FT                   /id="PRO_0000360875"
FT   BINDING         57..61
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03020"
FT   BINDING         128
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03020"
FT   BINDING         312
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         327
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03020"
SQ   SEQUENCE   379 AA;  44460 MW;  14BC94B4F2FD60E8 CRC64;
     MSCPYAGNGN DHDDSAVPLT TEVGKIYGEY LMLDKLLDAQ CMLSEEDKRP VHDEHLFIIT
     HQAYELWFKQ IIFEFDSIRD MLDAEVIDET KTLEIVKRLN RVVLILKLLV DQVPILETMT
     PLDFMDFRKY LAPASGFQSL QFRLIENKLG VLTEQRVRYN QKYSDVFSDE EARNSIRNSE
     KDPSLLELVQ RWLERTPGLE ESGFNFWAKF QESVDRFLEA QVQSAMMEPV EKAKNYRLMD
     IEKRREVYRS IFDPAVHDAL VRRGDRRFSH RALQGAIMIT FYRDEPRFSQ PHQLLTLLMD
     IDSLITKWRY NHVIMVQRMI GSQQLGTGGS SGYQYLRSTL SDRYKVFLDL FNLSTFLIPR
     EAIPPLDETI RRKLVHKSV
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024