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Q5A7M3 (KMO_CANAL) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:CaO19.12898, CaO19.5443
OrganismCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) [Reference proteome]
Taxonomic identifier237561 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length456 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. HAMAP-Rule MF_03018

Catalytic activity

L-kynurenine + NADPH + O2 = 3-hydroxy-L-kynurenine + NADP+ + H2O. HAMAP-Rule MF_03018

Cofactor

FAD By similarity. HAMAP-Rule MF_03018

Pathway

Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 1/3. HAMAP-Rule MF_03018

Subcellular location

Mitochondrion outer membrane By similarity HAMAP-Rule MF_03018.

Sequence similarities

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

Ontologies

Keywords
   Biological processPyridine nucleotide biosynthesis
   Cellular componentMembrane
Mitochondrion
Mitochondrion outer membrane
   LigandFAD
Flavoprotein
NADP
   Molecular functionMonooxygenase
Oxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process'de novo' NAD biosynthetic process from tryptophan

Inferred from sequence alignment PubMed 17425674. Source: CGD

anthranilate metabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

cellular response to starvation

Inferred from mutant phenotype PubMed 12773383. Source: CGD

filamentous growth

Inferred from mutant phenotype PubMed 12773383. Source: CGD

filamentous growth of a population of unicellular organisms in response to biotic stimulus

Inferred from mutant phenotype PubMed 12773383. Source: CGD

filamentous growth of a population of unicellular organisms in response to starvation

Inferred from mutant phenotype PubMed 12773383. Source: CGD

quinolinate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tryptophan catabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentmitochondrial outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay PubMed 19824013. Source: CGD

   Molecular_functionflavin adenine dinucleotide binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

kynurenine 3-monooxygenase activity

Inferred from sequence alignment PubMed 17425674. Source: CGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 456456Kynurenine 3-monooxygenase HAMAP-Rule MF_03018
PRO_0000361924

Sequences

Sequence LengthMass (Da)Tools
Q5A7M3 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: 4374754457385ED4

FASTA45651,534
        10         20         30         40         50         60 
MSEEESQKTI GIVGAGLVGC LAALAFAKKG YDVTLFEYRP DPRTVDSSKR NLRSINLAVS 

        70         80         90        100        110        120 
SRGIRALQYV DPAMADRILE HVIPMKGRMI HDITGTKQES QVYGLNGESI NSIDRSFLNN 

       130        140        150        160        170        180 
CLLDELDKSN VKILFKHKLV KLDTSNACRM TFIDGHNDAK TSTFDFVVGC DGAHSQFRYH 

       190        200        210        220        230        240 
LQKTMRMDYS QKYIDMQYLE LYIPPSEDAN NKFSIDANHL HIWPRHNFML IALANKDGSF 

       250        260        270        280        290        300 
TSTFFSPWSV IEGISSSQEF VEFFRHNFPD AVGLIGEDAL SSAFKSNPRG SLMQVSCYPY 

       310        320        330        340        350        360 
SNGKGIILGD AAHSMVPFYG QGMNCGFEDV RILMELIDTN NGDIEEAFKQ YSAARKNDLD 

       370        380        390        400        410        420 
AICKLALDNY YEMSSKVVDI GYLIKKKLDY TLGKIFKNKW LPLYTMISFR DDIPYAKAIE 

       430        440        450 
IEKRQNRIMN NVGLGVLGTA AVYGLVKLGQ YWNRRQ 

« Hide

References

[1]"The diploid genome sequence of Candida albicans."
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S.
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC5314 / ATCC MYA-2876.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AACQ01000050 Genomic DNA. Translation: EAK98864.1.
AACQ01000051 Genomic DNA. Translation: EAK98764.1.
RefSeqXP_717721.1. XM_712628.1.
XP_717815.1. XM_712722.1.

3D structure databases

ProteinModelPortalQ5A7M3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5476.CAL0005260.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3640528.
3640686.
KEGGcal:CaO19.12898.
cal:CaO19.5443.

Organism-specific databases

CGDCAL0005260. orf19.5443.

Phylogenomic databases

eggNOGCOG0654.
KOK00486.
OrthoDBEOG7QVMC6.

Enzyme and pathway databases

UniPathwayUPA00253; UER00328.

Family and domain databases

HAMAPMF_01971. Kynurenine_monooxygenase.
InterProIPR027545. Kynurenine_monooxygenase.
IPR002938. mOase_FAD-bd.
IPR003042. Rng_hydrolase-like.
[Graphical view]
PfamPF01494. FAD_binding_3. 1 hit.
[Graphical view]
PRINTSPR00420. RNGMNOXGNASE.
ProtoNetSearch...

Entry information

Entry nameKMO_CANAL
AccessionPrimary (citable) accession number: Q5A7M3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: April 26, 2005
Last modified: June 11, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Candida albicans

Candida albicans: entries and gene names