ID   T23O_DROME              Reviewed;         379 AA.
AC   P20351; Q9VZ50;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   04-NOV-2008, entry version 71.
DE   RecName: Full=Tryptophan 2,3-dioxygenase;
DE            Short=TO;
DE            EC=1.13.11.11;
DE   AltName: Full=Tryptophan pyrrolase;
DE   AltName: Full=Protein vermilion;
GN   Name=v; ORFNames=CG5163;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX   MEDLINE=90205819; PubMed=2108317;
RA   Searles L.L., Ruth R.S., Pret A.-M., Fridell R.A., Ali A.J.;
RT   "Structure and transcription of the Drosophila melanogaster vermilion
RT   gene and several mutant alleles.";
RL   Mol. Cell. Biol. 10:1423-1431(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RX   MEDLINE=22426069; PubMed=12537572;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Head;
RX   MEDLINE=22426066; PubMed=12537569;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
RA   George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA   Rubin G.M., Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC   -!- FUNCTION: During larval life controls the level of potentially
CC       harmful free tryptophan in the hemolymph by converting it to
CC       kynurenine, and during adult development the same reaction is the
CC       first step in the ommochrome biosynthetic pathway.
CC   -!- CATALYTIC ACTIVITY: L-tryptophan + O(2) = N-formyl-L-kynurenine.
CC   -!- COFACTOR: Heme (By similarity).
CC   -!- PATHWAY: Pigment biosynthesis; ommochrome biosynthesis.
CC   -!- DEVELOPMENTAL STAGE: High in late larvae and in adult.
CC   -!- SIMILARITY: Belongs to the tryptophan 2,3-dioxygenase family.
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DR   EMBL; M34147; AAA29014.1; -; Genomic_DNA.
DR   EMBL; AE014298; AAF47978.1; -; Genomic_DNA.
DR   EMBL; AY051478; AAK92902.1; -; mRNA.
DR   PIR; A34780; A34780.
DR   RefSeq; NP_511113.1; -.
DR   UniGene; Dm.7748; -.
DR   Ensembl; CG2155; Drosophila melanogaster.
DR   GeneID; 32026; -.
DR   KEGG; dme:Dmel_CG2155; -.
DR   NMPDR; fig|7227.3.peg.17334; -.
DR   FlyBase; FBgn0003965; v.
DR   BioCyc; DMEL-XXX-02:DMEL-XXX-02-001405-MON; -.
DR   NextBio; 776434; -.
DR   ArrayExpress; P20351; -.
DR   GermOnline; CG2155; Drosophila melanogaster.
DR   GO; GO:0004833; F:tryptophan 2,3-dioxygenase activity; TAS:FlyBase.
DR   GO; GO:0048072; P:compound eye pigmentation; TAS:FlyBase.
DR   GO; GO:0006727; P:ommochrome biosynthetic process; IMP:FlyBase.
DR   GO; GO:0006569; P:tryptophan catabolic process; TAS:FlyBase.
DR   InterPro; IPR004981; Trp_2_3_dOase.
DR   PANTHER; PTHR10138; Trp_2_3_dOase; 1.
DR   Pfam; PF03301; Trp_dioxygenase; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Dioxygenase; Heme; Iron; Metal-binding;
KW   Oxidoreductase.
FT   CHAIN         1    379       Tryptophan 2,3-dioxygenase.
FT                                /FTId=PRO_0000065780.
SQ   SEQUENCE   379 AA;  44421 MW;  E9E4C1B1C86D687F CRC64;
     MSCPYAGNGN DHDDSAVPLT TEVGKIYGEY LMLDKLLDAQ CMLSEEDKRP VHDEHLFIIT
     HQAYELWFKQ IIFEFDSIRD MLDAEVIDET KTLEIVKRLN RVVLILKLLV DQVPILETMT
     PLDFMDFRKY LAPASGFQSL QFRLIENKLG VLTEQRVRYN QKYSDVFSDE EARNSIRNSE
     KDPSLLELVQ RWLERTPGLE ESGFNFWAKF QESVDRFLEA QVQSAMEEPV EKAKNYRLMD
     IEKRREVYRS IFDPAVHDAL VRRGDRRFSH RALQGAIMIT FYRDEPRFSQ PHQLLTLLMD
     IDSLITKWRY NHVIMVQRMI GSQQLGTGGS SGYQYLRSTL SDRYKVFLDL FNLSTFLIPR
     EAIPPLDETI RKKLINKSV
//