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Q86PM2 (KMO_AEDAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kynurenine 3-monooxygenase
EC=1.14.13.9
Alternative name(s):
Kynurenine 3-hydroxylase
Gene names
Name:kh
ORF Names:AAEL008879
OrganismAedes aegypti (Yellowfever mosquito) (Culex aegypti)
Taxonomic identifier7159 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Nematocera › Culicoidea › Culicidae › Culicinae › Aedini › Aedes › Stegomyia

Protein attributes

Sequence length476 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid By similarity. Ref.2

Catalytic activity

L-kynurenine + NADPH + O2 = 3-hydroxy-L-kynurenine + NADP+ + H2O. Ref.2

Cofactor

FAD By similarity.

Enzyme regulation

Inhibited by pyridoxal phosphate and chloride ions. Ref.2

Pathway

Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 1/3.

Subcellular location

Mitochondrion By similarity. Membrane; Multi-pass membrane protein Potential.

Sequence similarities

Belongs to the aromatic-ring hydroxylase family. KMO subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=0.89 mM for L-kynurenine Ref.2

KM=0.82 mM for NADPH

Vmax=3550 nmol/min/mg enzyme toward L-kynurenine

Vmax=3821 nmol/min/mg enzyme toward NAPDH

pH dependence:

Optimum pH is between 7.0 and 7.5.

Temperature dependence:

Optimum temperature is 40 degrees Celsius.

Ontologies

Keywords
   Biological processPyridine nucleotide biosynthesis
   Cellular componentMembrane
Mitochondrion
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   LigandFAD
Flavoprotein
NADP
   Molecular functionMonooxygenase
Oxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processNAD metabolic process

Inferred from direct assay Ref.2. Source: UniProtKB

pyridine nucleotide biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrial outer membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular functionkynurenine 3-monooxygenase activity

Inferred from direct assay Ref.2. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q86PM2-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q86PM2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     379-432: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 476476Kynurenine 3-monooxygenase
PRO_0000361912

Regions

Transmembrane397 – 42024Helical; Potential
Transmembrane433 – 45422Helical; Potential

Natural variations

Alternative sequence379 – 43254Missing in isoform 2.
VSP_036237

Experimental info

Sequence conflict131L → S in AAL37368. Ref.1
Sequence conflict1131N → H in AAL37368. Ref.1
Sequence conflict1691T → A in AAL37368. Ref.1
Sequence conflict2601K → Q in AAL37368. Ref.1
Sequence conflict2861V → F in AAL37368. Ref.1
Sequence conflict3121V → A in AAL37368. Ref.1
Sequence conflict3451Q → E in AAL37368. Ref.1
Sequence conflict4071V → F in AAL37368. Ref.1
Sequence conflict4411C → S in AAL37368. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 10, 2009. Version 2.
Checksum: DC41758284BC6C6F

FASTA47654,232
        10         20         30         40         50         60 
MTAQYKQTNT NGLTARNLNV AVVGGGLVGS LFALHLGKKG HTVDLYEYRE DIRTAELVIG 

        70         80         90        100        110        120 
RSINLALSAR GRKALAEVGL EDALLQHGIP MKGRMLHDLK GNRKIVPYDA NTNQCIYSVG 

       130        140        150        160        170        180 
RKHLNEVLLD AAEKYPNIHL YFNKKLQSAN LDEGEMSFID PTTKESTHTK ADLIVGCDGA 

       190        200        210        220        230        240 
YSAVRKEIVK RPGYDYSQTY IEHGYLELCI PPTKDGDFAM PHNYLHIWPR GKFMMIALPN 

       250        260        270        280        290        300 
QDRTWTVTLF MPFTNFNSIK CDGDLLKFFR TYFPDAIDLI GRERLVKDFF KTRPQSLVMI 

       310        320        330        340        350        360 
KCKPYNVGGK AVIIGDAAHA MVPFYGQGMN AGFEDCTVLT ELFNQHGSDV DRILAEFSDT 

       370        380        390        400        410        420 
RWEDAHSICD LAMYNYVEMR DLVTKRSYLF RKKLDELLYW MLPNTWVPLY NSVSFSHMRY 

       430        440        450        460        470 
SKCIANRKWQ DKILTRVLYC CSITAVAAAG YFGYKYGNMD LVQHYSSSVL QLLKLK

« Hide

Isoform 2 [UniParc].

Checksum: 8B5F1C72D89EF4D0
Show »

FASTA42247,492

References

« Hide 'large scale' references
[1]"Isolation and characterization of kynurenine monooxygenase gene of Aedes aegypti."
Fang J., Li J.
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: Liverpool.
[2]"Analysis of the wild-type and mutant genes encoding the enzyme kynurenine monooxygenase of the yellow fever mosquito, Aedes aegypti."
Han Q., Calvo E., Marinotti O., Fang J., Rizzi M., James A.A., Li J.
Insect Mol. Biol. 12:483-490(2003) [PubMed: 12974953] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: Rockefeller.
[3]"Genome sequence of Aedes aegypti, a major arbovirus vector."
Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J., Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F., Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P. expand/collapse author list , Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L., Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J., Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E., El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I., Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H., Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S., Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P., Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J., Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W., Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O., Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R., Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B., Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T., Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.
Science 316:1718-1723(2007) [PubMed: 17510324] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LVPib12.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF325508 mRNA. Translation: AAL37368.1.
AY194224 mRNA. Translation: AAO27575.1.
AY194225 mRNA. Translation: AAO27576.1.
CH477539 Genomic DNA. Translation: EAT39312.1.
CH477539 Genomic DNA. Translation: EAT39313.1.
RefSeqXP_001653516.1. XM_001653466.1.
XP_001653517.1. XM_001653467.1.
UniGeneAae.5570.

3D structure databases

ProteinModelPortalQ86PM2.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaAAEL008879-RA; AAEL008879-PA; AAEL008879.
GeneID5571188.
KEGGaag:AaeL_AAEL008879.

Phylogenomic databases

eggNOGinNOG08413.
GeneTreeEMGT00050000009966.
InParanoidQ86PM2.
OMAYFPDAIP.
OrthoDBEOG4K6DKV.
PhylomeDBQ86PM2.

Family and domain databases

InterProIPR002938. mOase_FAD-bd.
IPR003042. Rng_hydrolase-like.
[Graphical view]
KOK00486.
PfamPF01494. FAD_binding_3. 1 hit.
[Graphical view]
PRINTSPR00420. RNGMNOXGNASE.
ProtoNetSearch...

Entry information

Entry nameKMO_AEDAE
AccessionPrimary (citable) accession number: Q86PM2
Secondary accession number(s): Q16XF6, Q86PM3, Q8WSB2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: February 10, 2009
Last modified: January 25, 2012
This is version 48 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents