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Reviewed, UniProtKB/Swiss-Prot A3LNF8 (KMO_PICST)

Last modified November 3, 2009. Version 23. 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
ORF Names: PICST_40545
OrganismPichia stipitis (Yeast) [Complete proteome]
Taxonomic identifier4924 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaePichia

Protein attributes

Sequence length478 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
   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

tRNA processing

Inferred from electronic annotation. Source: InterPro

   Cellular componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionFAD binding

Inferred from electronic annotation. Source: InterPro

kynurenine 3-monooxygenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 478478Kynurenine 3-monooxygenase
PRO_0000361932

Sequences

Sequence LengthMass (Da)Tools
A3LNF8-1 [UniParc].

Last modified July 24, 2007. Version 2.
Checksum: 3F983C198687AEAE

FASTA47854,389
        10         20         30         40         50         60 
MSVLESVDTS NRHQGVGIVG AGLVGCLAAL AFAAKGYSVT LFELRPDPKT VDASERNLRS 

        70         80         90        100        110        120 
INLAVSNRGI RALKYVDDAM ADRILEHIIP MKGRMIHDTT GTKQESQLYG LFGESINSID 

       130        140        150        160        170        180 
RGFLNDCLLA EMRHSDDINV LFNHKLVQLD HLMREDETPT MTFVDTRDNK AEPKTFEFDY 

       190        200        210        220        230        240 
IVGADGAHSQ FRYQMQRSMR MDFQQKYIDM QYLELYIPPN TLEGATSKFS IDPNHLHIWP 

       250        260        270        280        290        300 
RHNFMLIALA NKDGSFTSTF FSPWSVIESI KSAQEWVVFF KKNFPDAYKL MGDDHLISVY 

       310        320        330        340        350        360 
ESNPRGTLMQ VTAYPYHNPT GRAIIIGDAA HSMVPFYGQG MNCGFEDVRV LMELIDTNHG 

       370        380        390        400        410        420 
NVTKSFKQYS DARKKDLDAI CKLALDNYHE MSSKVTSPLY LIRKKLDYTL GKYANGTLFQ 

       430        440        450        460        470 
WLPLYTMISF RDDIPYAKAI AIEKRQATIL NRVQIVSLTA LALYGAVKAA QCWDRFRR 

« Hide

References

[1]"Genome sequence of the lignocellulose-bioconverting and xylose-fermenting yeast Pichia stipitis."
Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A., Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S., Passoth V., Richardson P.M.
Nat. Biotechnol. 25:319-326(2007) [PubMed: 17334359] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 58785 / CBS 6054 / IFO 10063 / NRRL Y-11545.

Cross-references

Sequence databases

CP000496 Genomic DNA. Translation: ABN64850.2.
RefSeqXP_001382879.2.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA3LNF8.

Genome annotation databases

GeneID4836628.
GenomeReviewsGene locus BNA4 in contig CP000496_GR.
KEGGpic:PICST_40545.

Phylogenomic databases

OMALHAIMPS.

Family and domain databases

InterProIPR002218. GIDA-rel.
IPR003042. Rng_hydrolase-like.
[Graphical view]
PfamPF01134. GIDA. 1 hit.
[Graphical view]
PRINTSPR00420. RNGMNOXGNASE.
ProtoNetSearch...

Entry information

Entry nameKMO_PICST
AccessionPrimary (citable) accession number: A3LNF8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: July 24, 2007
Last modified: November 3, 2009
This is version 23 of the entry and version 2 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