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Reviewed, UniProtKB/Swiss-Prot Q751I2 (KMO_ASHGO)

Last modified November 3, 2009. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Kynurenine 3-monooxygenase
    EC=1.14.13.9
Alternative name(s):
    Kynurenine 3-hydroxylase
    Biosynthesis of nicotinic acid protein 4
Gene names
Name: BNA4
Ordered Locus Names: AGL276W
OrganismAshbya gossypii (Yeast) (Eremothecium gossypii) [Complete proteome]
Taxonomic identifier33169 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeEremothecium

Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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.

Catalytic activity

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

Cofactor

FAD By similarity.

Pathway

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

Subcellular location

Mitochondrion By similarity.

Sequence similarities

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

Ontologies

Keywords
   Biological processPyridine nucleotide biosynthesis
   Cellular componentMitochondrion
   LigandFAD
Flavoprotein
NADP
   Molecular functionMonooxygenase
Oxidoreductase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

pyridine nucleotide biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionkynurenine 3-monooxygenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 466466Kynurenine 3-monooxygenase
PRO_0000361915

Amino acid modifications

Modified residue71Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q751I2-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 5D79B03EA4BE8D9B

FASTA46652,142
        10         20         30         40         50         60 
MGEKGESVAV IGAGLVGCLA ALAFAKKGYE VSLFDYRSDP RLATTTDRNL RSINLAISAR 

        70         80         90        100        110        120 
GIEGLKAVDD ELAARVLRDM LPMHGRMIHN LAGKQEPQEY GLFGESVNSI DRGVLNNALL 

       130        140        150        160        170        180 
DEVSAQEHIQ AQFGHKLVKA NFNHGATQQL LFAVEGKTVQ LEFDFVVGCD GAYSTTRQQM 

       190        200        210        220        230        240 
QRFDRMDFSQ EYMDCFYLEL YIPPTPEFSE RFGGPFAISP QHLHIWPRHN FMLIALPNKD 

       250        260        270        280        290        300 
GSFTSTFFGP WSLLDRLDTR EQLAAFLTTN FADAMELIGL DNAIRAFQEN TKGALMCVEC 

       310        320        330        340        350        360 
RPYHLPGGKA ILLGDAAHAM VPFYGQGMNC GFEDVRVLMG LLDDYAGDRT AAFAKYTASR 

       370        380        390        400        410        420 
HRDLVSIIQL AKNNYRDMSH NVVSSWHRAK RSLNNVLGRT FRGTWLPLYT MVSFRADIPY 

       430        440        450        460 
HKAVEVDRRQ AAILSLVQSA LLSLAALGGF KGLLLLYRWI KQVRRV 

« Hide

References

[1]"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome."
Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.
Science 304:304-307(2004) [PubMed: 15001715] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10895 / NRRL Y-1056 / CBS 109.51.

Cross-references

Sequence databases

AE016820 Genomic DNA. Translation: AAS54215.1.
RefSeqNP_986391.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ751I2.

Genome annotation databases

GeneID4622684.
GenomeReviewsGene locus AGL276W in contig AE016820_GR.
KEGGago:AGOS_AGL276W.
NMPDRfig|33169.1.peg.4036.

Organism-specific databases

AGDAGL276W.

Phylogenomic databases

HOGENOMQ751I2.
OMALHAIMPS.

Family and domain databases

InterProIPR006076. FAD-dep_OxRdtase.
IPR003042. Rng_hydrolase-like.
[Graphical view]
PfamPF01266. DAO. 1 hit.
[Graphical view]
PRINTSPR00420. RNGMNOXGNASE.
ProtoNetSearch...

Entry information

Entry nameKMO_ASHGO
AccessionPrimary (citable) accession number: Q751I2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: July 5, 2004
Last modified: November 3, 2009
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents