Skip Header

Contribute Send feedback
Read comments (?) or add your own

A1CT23 (KMO_ASPCL) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 33. 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:ACLA_081480
OrganismAspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1) [Complete proteome]
Taxonomic identifier344612 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaemitosporic TrichocomaceaeAspergillus

Protein attributes

Sequence length512 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
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 – 512512Kynurenine 3-monooxygenase
PRO_0000361916

Sequences

Sequence LengthMass (Da)Tools
A1CT23 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 5B1C7AC98065CD1B

FASTA51258,083
        10         20         30         40         50         60 
MADTVRKPQK VVIVGAGPVG SLAALYAAAR GDEVEVYELR GDLRDPSTIP LNFTKSINLA 

        70         80         90        100        110        120 
LSERGINAMK HSNREELTKN VLRDTIPMYG RMIHGKDRGQ LWEAAQAYDV HGRAINAVDR 

       130        140        150        160        170        180 
STLNNALLDE LEHTPNVKLF FNHKLTGADF RANKAWFERR VPGEAPLPNS ANRVPEIEVD 

       190        200        210        220        230        240 
FDFMLGADGA HSAVRYHMMK FARVDYQQEY IDTLWCEFRI APTENGEFRI SPNHLHIWPG 

       250        260        270        280        290        300 
REFMFIALPS ADKSFTCTLF APAVHYTYLA SSPQKLLDFF DVHFPGVSPE LIPPADLQEQ 

       310        320        330        340        350        360 
FATNPHLPLI SLKCKPHHFG SSVAIVGDAA HAVLPFYGQG LNAGLEDIRV LFEVLDKHSV 

       370        380        390        400        410        420 
YDLDASHEAR REAREKAFQA YTDQRCADTH AINDLSKENY VEMRWGVKTP LYKLRKSIEE 

       430        440        450        460        470        480 
ILDRYVPSLG WQTQYSRVSF SNQRYSDVIK LARRQGTVLG LGLGSTFITA VGVAGYMMWK 

       490        500        510 
NPKQYSPLCF MRYCLRHVSH IWVKFFRNTA YA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS027060 Genomic DNA. Translation: EAW06460.1.
RefSeqXP_001267886.1. XM_001267885.1.

3D structure databases

ProteinModelPortalA1CT23.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1CT23.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADACLAT00007583; CADACLAP00007392; CADACLAG00007583.
GeneID4700205.
KEGGact:ACLA_081480.

Phylogenomic databases

GeneTreeEFGT00050000002229.
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_ASPCL
AccessionPrimary (citable) accession number: A1CT23
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: January 23, 2007
Last modified: December 14, 2011
This is version 33 of the entry and version 1 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