KMO_AEDAE
ID KMO_AEDAE Reviewed; 476 AA.
AC Q86PM2; Q16XF6; Q86PM3; Q8WSB2;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 25-MAY-2022, entry version 103.
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=AAEL008879;
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Liverpool;
RA Fang J., Li J.;
RT "Isolation and characterization of kynurenine monooxygenase gene of Aedes
RT aegypti.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=Rockefeller;
RX PubMed=12974953; DOI=10.1046/j.1365-2583.2003.00433.x;
RA Han Q., Calvo E., Marinotti O., Fang J., Rizzi M., James A.A., Li J.;
RT "Analysis of the wild-type and mutant genes encoding the enzyme kynurenine
RT monooxygenase of the yellow fever mosquito, Aedes aegypti.";
RL Insect Mol. Biol. 12:483-490(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVPib12;
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
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, ECO:0000269|PubMed:12974953}.
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 ECO:0000269|PubMed:12974953};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03018};
CC -!- ACTIVITY REGULATION: Inhibited by pyridoxal phosphate and chloride
CC ions. {ECO:0000269|PubMed:12974953}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.89 mM for L-kynurenine {ECO:0000269|PubMed:12974953};
CC KM=0.82 mM for NADPH {ECO:0000269|PubMed:12974953};
CC Vmax=3550 nmol/min/mg enzyme toward L-kynurenine
CC {ECO:0000269|PubMed:12974953};
CC Vmax=3821 nmol/min/mg enzyme toward NADPH
CC {ECO:0000269|PubMed:12974953};
CC pH dependence:
CC Optimum pH is between 7.0 and 7.5. {ECO:0000269|PubMed:12974953};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:12974953};
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86PM2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86PM2-2; Sequence=VSP_036237;
CC -!- SIMILARITY: Belongs to the aromatic-ring hydroxylase family. KMO
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03018}.
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DR EMBL; AF325508; AAL37368.1; -; mRNA.
DR EMBL; AY194224; AAO27575.1; -; mRNA.
DR EMBL; AY194225; AAO27576.1; -; mRNA.
DR EMBL; CH477539; EAT39312.1; -; Genomic_DNA.
DR EMBL; CH477539; EAT39313.1; -; Genomic_DNA.
DR RefSeq; XP_001653516.1; XM_001653466.1.
DR RefSeq; XP_001653517.1; XM_001653467.1.
DR AlphaFoldDB; Q86PM2; -.
DR SMR; Q86PM2; -.
DR STRING; 7159.AAEL008879-PA; -.
DR GeneID; 5571188; -.
DR KEGG; aag:5571188; -.
DR VEuPathDB; VectorBase:AAEL008879; -.
DR eggNOG; KOG2614; Eukaryota.
DR HOGENOM; CLU_023210_0_1_1; -.
DR InParanoid; Q86PM2; -.
DR OMA; REFMFIA; -.
DR OrthoDB; 462247at2759; -.
DR PhylomeDB; Q86PM2; -.
DR BRENDA; 1.14.13.9; 149.
DR UniPathway; UPA00253; UER00328.
DR Proteomes; UP000008820; Unassembled WGS sequence.
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:0004502; F:kynurenine 3-monooxygenase activity; IDA:UniProtKB.
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:0019674; P:NAD metabolic process; IDA: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 1: Evidence at protein level;
KW Alternative splicing; FAD; Flavoprotein; Membrane; Mitochondrion;
KW Monooxygenase; NADP; Oxidoreductase; Pyridine nucleotide biosynthesis;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..476
FT /note="Kynurenine 3-monooxygenase"
FT /id="PRO_0000361912"
FT TRANSMEM 397..420
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03018"
FT TRANSMEM 433..455
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03018"
FT VAR_SEQ 379..432
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12974953"
FT /id="VSP_036237"
FT CONFLICT 13
FT /note="L -> S (in Ref. 1; AAL37368)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="N -> H (in Ref. 1; AAL37368)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="T -> A (in Ref. 1; AAL37368)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="K -> Q (in Ref. 1; AAL37368)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="V -> F (in Ref. 1; AAL37368)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="V -> A (in Ref. 1; AAL37368)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="Q -> E (in Ref. 1; AAL37368)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="V -> F (in Ref. 1; AAL37368)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="C -> S (in Ref. 1; AAL37368)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 54232 MW; DC41758284BC6C6F CRC64;
MTAQYKQTNT NGLTARNLNV AVVGGGLVGS LFALHLGKKG HTVDLYEYRE DIRTAELVIG
RSINLALSAR GRKALAEVGL EDALLQHGIP MKGRMLHDLK GNRKIVPYDA NTNQCIYSVG
RKHLNEVLLD AAEKYPNIHL YFNKKLQSAN LDEGEMSFID PTTKESTHTK ADLIVGCDGA
YSAVRKEIVK RPGYDYSQTY IEHGYLELCI PPTKDGDFAM PHNYLHIWPR GKFMMIALPN
QDRTWTVTLF MPFTNFNSIK CDGDLLKFFR TYFPDAIDLI GRERLVKDFF KTRPQSLVMI
KCKPYNVGGK AVIIGDAAHA MVPFYGQGMN AGFEDCTVLT ELFNQHGSDV DRILAEFSDT
RWEDAHSICD LAMYNYVEMR DLVTKRSYLF RKKLDELLYW MLPNTWVPLY NSVSFSHMRY
SKCIANRKWQ DKILTRVLYC CSITAVAAAG YFGYKYGNMD LVQHYSSSVL QLLKLK
