KMO_DROME
ID KMO_DROME Reviewed; 465 AA.
AC A1Z746; Q27577; Q8SYV3; Q9BMM9;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Kynurenine 3-monooxygenase {ECO:0000255|HAMAP-Rule:MF_03018};
DE EC=1.14.13.9 {ECO:0000255|HAMAP-Rule:MF_03018};
DE AltName: Full=Kynurenine 3-hydroxylase {ECO:0000255|HAMAP-Rule:MF_03018};
DE AltName: Full=Protein cinnabar;
GN Name=cn {ECO:0000255|HAMAP-Rule:MF_03018}; ORFNames=CG1555;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Canton-S;
RX PubMed=8921860; DOI=10.1016/0378-1119(96)00291-0;
RA Warren W.D., Phillips A.M., Howells A.J.;
RT "Drosophila melanogaster contains both X-linked and autosomal homologues of
RT the gene encoding calcineurin B.";
RL Gene 177:149-153(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11238412; DOI=10.1093/genetics/157.3.1285;
RA Yang H.P., Tanikawa A.Y., Kondrashov A.S.;
RT "Molecular nature of 11 spontaneous de novo mutations in Drosophila
RT melanogaster.";
RL Genetics 157:1285-1292(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX 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., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., 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., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., 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., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
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., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-398.
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form
CC 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic
CC acid. {ECO:0000255|HAMAP-Rule:MF_03018}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-kynurenine + NADPH + O2 = 3-hydroxy-L-kynurenine +
CC H2O + NADP(+); Xref=Rhea:RHEA:20545, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:57959, ChEBI:CHEBI:58125, ChEBI:CHEBI:58349;
CC EC=1.14.13.9; Evidence={ECO:0000255|HAMAP-Rule:MF_03018};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03018};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC L-kynurenine: step 1/3. {ECO:0000255|HAMAP-Rule:MF_03018}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03018}.
CC Membrane {ECO:0000255|HAMAP-Rule:MF_03018}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03018}.
CC -!- SIMILARITY: Belongs to the aromatic-ring hydroxylase family. KMO
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03018}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC47351.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAK07882.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAL48918.1; Type=Miscellaneous discrepancy; Note=A mutation exists in the sequenced strain which affects the 3' end of the sequence.; Evidence={ECO:0000305};
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DR EMBL; U56245; AAC47351.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF317319; AAK07882.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE013599; AAF59196.4; -; Genomic_DNA.
DR EMBL; AY071296; AAL48918.1; ALT_SEQ; mRNA.
DR RefSeq; NP_523651.4; NM_078927.3.
DR AlphaFoldDB; A1Z746; -.
DR SMR; A1Z746; -.
DR BioGRID; 61593; 1.
DR STRING; 7227.FBpp0088005; -.
DR PaxDb; A1Z746; -.
DR PRIDE; A1Z746; -.
DR EnsemblMetazoa; FBtr0344723; FBpp0311059; FBgn0000337.
DR GeneID; 35724; -.
DR KEGG; dme:Dmel_CG1555; -.
DR UCSC; CG1555-RA; d. melanogaster.
DR CTD; 35724; -.
DR FlyBase; FBgn0000337; cn.
DR VEuPathDB; VectorBase:FBgn0000337; -.
DR eggNOG; KOG2614; Eukaryota.
DR InParanoid; A1Z746; -.
DR PhylomeDB; A1Z746; -.
DR Reactome; R-DME-71240; Tryptophan catabolism.
DR UniPathway; UPA00253; UER00328.
DR BioGRID-ORCS; 35724; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 35724; -.
DR PRO; PR:A1Z746; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0000337; Expressed in adult eye primordium (Drosophila) and 7 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0004502; F:kynurenine 3-monooxygenase activity; ISS:UniProtKB.
DR GO; GO:0016174; F:NAD(P)H oxidase H2O2-forming activity; IBA:GO_Central.
DR GO; GO:0034354; P:'de novo' NAD biosynthetic process from tryptophan; IEA:UniProtKB-UniRule.
DR GO; GO:0043420; P:anthranilate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0048072; P:compound eye pigmentation; TAS:FlyBase.
DR GO; GO:0070189; P:kynurenine metabolic process; IMP:UniProtKB.
DR GO; GO:0019674; P:NAD metabolic process; ISS:UniProtKB.
DR GO; GO:0006727; P:ommochrome biosynthetic process; IMP:FlyBase.
DR GO; GO:1901216; P:positive regulation of neuron death; IMP:FlyBase.
DR GO; GO:0019805; P:quinolinate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006569; P:tryptophan catabolic process; TAS:FlyBase.
DR Gene3D; 3.50.50.60; -; 1.
DR HAMAP; MF_01971; Kynurenine_monooxygenase; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR027545; Kynurenine_monooxygenase.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 2: Evidence at transcript level;
KW FAD; Flavoprotein; Membrane; Mitochondrion; Monooxygenase; NADP;
KW Oxidoreductase; Pyridine nucleotide biosynthesis; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..465
FT /note="Kynurenine 3-monooxygenase"
FT /id="PRO_0000361914"
FT TRANSMEM 405..427
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03018"
FT TRANSMEM 440..462
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03018"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 21
FT /note="R -> M (in Ref. 2; AAK07882)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="Q -> E (in Ref. 2; AAK07882 and 5; AAL48918)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="Q -> H (in Ref. 2; AAK07882)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="V -> E (in Ref. 2; AAK07882)"
FT /evidence="ECO:0000305"
FT CONFLICT 197..198
FT /note="NN -> HL (in Ref. 5; AAL48918)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="A -> P (in Ref. 2; AAK07882)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 465 AA; 52882 MW; B44B6D22537353C0 CRC64;
MSPGIVSQEV NGRQEPTEAA RDERHGRRRR VAVIGAGLVG SLAALNFARM GNHVDLYEYR
EDIRQALVVQ GRSINLALSQ RGRKALAAVG LEQEVLATAI PMRGRMLHDV RGNSSVVLYD
PINNQCLYSV GRRQLNEVLL NACDKLPNIR CHFEHKLTSA NLREGSMEFR NPAKEAVAAH
ADLIVGCDGA FSSVRQNNVR LPGFNYSQEY IETGYLELCI PSKSGDFQMP ANYLHIWPRN
TFMMIALPNQ DKSFTVTLSM PFEIFAGIQN QNDLLEFFKL NFRDALPLIG EQQLIKDFFK
TRPQFLVSIK CRPYHYADKA LILGDAAHAM VPYYGQGMNA GMEDVTLLTD ILAKQLPLDE
TLALFTESRW QDAFAICDLA MYNYVEMRDL TKRWTFRLRK WLDTLLFRLF PGWIPLYNSV
SFSSMPYRQC IANRKWQDQL LKRIFGATFL AAIVTGGAIY AQRFL
