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Q0V5K1 (KMO_PHANO) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 38. 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·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):
Biosynthesis of nicotinic acid protein 4
Kynurenine 3-hydroxylase
Gene names
Name:BNA4
ORF Names:SNOG_00713
OrganismPhaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume blotch fungus) (Septoria nodorum)
Taxonomic identifier321614 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesPleosporomycetidaePleosporalesPleosporineaePhaeosphaeriaceaePhaeosphaeria

Protein attributes

Sequence length482 AA.
Sequence statusComplete.
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
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processpyridine 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 – 482482Kynurenine 3-monooxygenase
PRO_0000361931

Sequences

Sequence LengthMass (Da)Tools
Q0V5K1 [UniParc].

Last modified February 10, 2009. Version 3.
Checksum: 821B2728F8744B02

FASTA48254,203
        10         20         30         40         50         60 
MPQKIVVVGA GPVGSLAALY AAVRGHDVEI YELRSDLRNS EHSSNISQSI NLALSERGIN 

        70         80         90        100        110        120 
SLRKTGLPDL ADAVLAETFP MHGRMIHVRK HGQYVRQAQA YDAHGRNLLA MDRTGLNKTL 

       130        140        150        160        170        180 
LDHLNSMPNV TFFFHRKLVS VDFRKKLAWF ENRTKTDPAK SDDIEVSFDL MIGADGAHSA 

       190        200        210        220        230        240 
VRYHLMKFVP MSYQQEYIDK LWCQFHVPPS DKGDFRIPPN YLHIWPQDDA MFIALPNLDK 

       250        260        270        280        290        300 
SFTSTLFLTR SGFEELVASG KVVEYFDEKF PGVVPELITE DELRKQFNEH DHFPLISIKC 

       310        320        330        340        350        360 
SPYHFGSTGV IVGDSAHAMV PFYGQGMNAG LEDVRVLFEI LDKYPGDQAK ALSEYSEQRT 

       370        380        390        400        410        420 
PDAQTINDLA LGNYREMASD VKKPLYLLRK WIEEKLYIYV PSAGWATQYS RVTFSNMRYS 

       430        440        450        460        470        480 
EVQAAAQRQA KILNGIVGVT TLSLIGSAAL WLGRTGGLQQ AKQNILRSIC LLAQQAQKVT 


KG 

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References

[1]"Dothideomycete-plant interactions illuminated by genome sequencing and EST analysis of the wheat pathogen Stagonospora nodorum."
Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L., Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E., Torriani S.F.F., McDonald B.A., Oliver R.P.
Plant Cell 19:3347-3368(2007) [PubMed: 18024570] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SN15 / ATCC MYA-4574 / FGSC 10173.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH445325 Genomic DNA. Translation: EAT92208.2.
RefSeqXP_001791390.1. XM_001791338.1.

3D structure databases

ProteinModelPortalQ0V5K1.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5968074.
KEGGpno:SNOG_00713.

Phylogenomic databases

OrthoDBEOG4QG0P2.

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_PHANO
AccessionPrimary (citable) accession number: Q0V5K1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: February 10, 2009
Last modified: November 16, 2011
This is version 38 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families