(data stored in ACNUC5340 zone)

HOGENOM: AEDAE_2824_PE18

ID   AEDAE_2824_PE18                      STANDARD;      PRT;   476 AA.
AC   AEDAE_2824_PE18; Q86PM2; Q16XF6; Q86PM3; Q8WSB2;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Kynurenine 3-monooxygenase; EC=1.14.13 9;AltName:
DE   Full=Kynurenine 3-hydroxylase; (AEDAE_2824.PE18).
GN   Name=kh; ORFNames=AAEL008879;
OS   AEDES AEGYPTI.
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera;
OC   Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae; Culicinae;
OC   Culicini; Aedes.
OX   NCBI_TaxID=7159;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS AEDAE_2824.PE18.
CC       Aedes aegypti supercontig supercont1.354 AaegL1  sequence 1..1201341
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:KMO_AEDAE
CC   -!- FUNCTION: Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to
CC       form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of
CC       quinolinic acid (By similarity).
CC   -!- CATALYTIC ACTIVITY: L-kynurenine + NADPH + O(2) = 3-hydroxy-L-
CC       kynurenine + NADP(+) + H(2)O.
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- ENZYME REGULATION: Inhibited by pyridoxal phosphate and chloride
CC       ions.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.89 mM for L-kynurenine;
CC         KM=0.82 mM for NADPH;
CC         Vmax=3550 nmol/min/mg enzyme toward L-kynurenine;
CC         Vmax=3821 nmol/min/mg enzyme toward NAPDH;
CC       pH dependence:
CC         Optimum pH is between 7.0 and 7.5;
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius;
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate
CC       from L-kynurenine: step 1/3.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). Membrane;
CC       Multi-pass membrane protein (Potential).
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.
CC   -!- GENE_FAMILY: HOG000251788 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Aedes_aegypti;AAEL008879;AAEL008879-RA;AAEL008879-PA.
DR   EMBL; AF325508; - ;
DR   EMBL; AY194224; - ;
DR   EMBL; AY194225; - ;
DR   EMBL; CH477539; - ;
DR   UniProtKB/Swiss-Prot; Q86PM2; Q16XF6; Q86PM3; Q8WSB2; -.
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   UniGene; Aae.5570; -.
DR   ProteinModelPortal; Q86PM2; -.
DR   EnsemblMetazoa; AAEL008879-RA; AAEL008879-PA; AAEL008879.
DR   GeneID; 5571188; -.
DR   KEGG; aag:AaeL_AAEL008879; -.
DR   eggNOG; inNOG08413; -.
DR   GeneTree; EMGT00050000009966; -.
DR   InParanoid; Q86PM2; -.
DR   OMA; YFPDAIP; -.
DR   OrthoDB; EOG4K6DKV; -.
DR   PhylomeDB; Q86PM2; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR   GO; GO:0004502; F:kynurenine 3-monooxygenase activity; IDA:UniProtKB.
DR   GO; GO:0019674; P:NAD metabolic process; IDA:UniProtKB.
DR   GO; GO:0019363; P:pyridine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR002938; mOase_FAD-bd.
DR   InterPro; IPR003042; Rng_hydrolase-like.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   HOGENOMDNA; AEDAE_2824.PE18; -.
KW   AAEL0088793; AAEL008879-PA ; Q86PM2; AF325508; AY194224; AY194225;
KW   CH477539;
KW   Alternative splicing; FAD; Flavoprotein; Membrane; Mitochondrion;
KW   Monooxygenase; NADP; Oxidoreductase; Pyridine nucleotide biosynthesis;
KW   Transmembrane; Transmembrane helix.
SQ   SEQUENCE   476 AA;  UNKNOWN MW;  UNKNOWN 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
//

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