ID   KMO_ANOGA               Reviewed;         486 AA.
AC   Q7Q6A7;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 2.
DT   25-MAY-2022, entry version 113.
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};
GN   Name=kh; ORFNames=AGAP005948;
OS   Anopheles gambiae (African malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PEST;
RX   PubMed=12364791; DOI=10.1126/science.1076181;
RA   Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA   Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA   Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA   Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA   Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA   Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA   Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA   Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA   Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA   Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA   Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA   Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA   McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA   O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA   Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA   Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA   Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA   Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA   Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA   Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA   Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA   Collins F.H., Hoffman S.L.;
RT   "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL   Science 298:129-149(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   ---------------------------------------------------------------------------
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; AAAB01008960; EAA11712.2; -; Genomic_DNA.
DR   RefSeq; XP_315983.2; XM_315983.4.
DR   AlphaFoldDB; Q7Q6A7; -.
DR   SMR; Q7Q6A7; -.
DR   STRING; 7165.AGAP005948-PA; -.
DR   PaxDb; Q7Q6A7; -.
DR   GeneID; 1276617; -.
DR   KEGG; aga:AgaP_AGAP005948; -.
DR   CTD; 1276617; -.
DR   VEuPathDB; VectorBase:AGAP005948; -.
DR   eggNOG; KOG2614; Eukaryota.
DR   HOGENOM; CLU_023210_0_1_1; -.
DR   InParanoid; Q7Q6A7; -.
DR   OMA; REFMFIA; -.
DR   OrthoDB; 462247at2759; -.
DR   PhylomeDB; Q7Q6A7; -.
DR   UniPathway; UPA00253; UER00328.
DR   Proteomes; UP000007062; Chromosome 2L.
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:0070189; P:kynurenine metabolic process; IBA:GO_Central.
DR   GO; GO:0019674; P:NAD metabolic process; ISS:UniProtKB.
DR   GO; GO:0019805; P:quinolinate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006569; P:tryptophan catabolic process; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   FAD; Flavoprotein; Membrane; Mitochondrion; Monooxygenase; NADP;
KW   Oxidoreductase; Pyridine nucleotide biosynthesis; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..486
FT                   /note="Kynurenine 3-monooxygenase"
FT                   /id="PRO_0000361913"
FT   TRANSMEM        401..424
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03018"
FT   TRANSMEM        437..459
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03018"
SQ   SEQUENCE   486 AA;  55010 MW;  5A5F80A34C8FAB97 CRC64;
     MATASDSKYK RTNTNGMQHQ PLDVAIVGGG LVGSLLALHL GKKGHEVNLY EYREDIRTAE
     LVIGRSINLA LSARGRRALA EVGLEDALLN HGIPMSGRML HDVNGKCKIV PYDANTNQCI
     YSVGRKHLNE VLLNAAEKYP NIHLHFNHKL VSANLDEGNL SMVDPVTKDV KSARADLIVG
     CDGAYSAVRK EIVKRPRYDF SQTYIEHGYL ELCIPPTAGG EFAMPHNYLH IWPRGQFMMI
     ALPNQDRTWT VTLFMPFTQF HSITDQGLLL DFFRQHFPDA IELIGRERLV KDFFKTKAQP
     LVMIKCRPYH IGAKALIIGD AAHAMVPFYG QGMNAGFEDC SVLTELFNQY GTDLARILPE
     FSEKRWEDAH AICDLAMYNY IEMRDLVTKR SYLLRKKLDE LLFWMMPNTW VPLYNSVSFS
     HMRYSKCIAN RAWQDKILTR VLYGASIASV AAIGGLCYRH VTMGHLERLS TRILSTFQLL
     KPKASV