Reviewed, UniProtKB/Swiss-Prot Q4WN75 (KMO_ASPFU)

Names and origin

Protein names

Recommended 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:	AFUA_6G07340

Organism

Aspergillus fumigatus (Sartorya fumigata) [Complete proteome]

Taxonomic identifier

5085 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	512 AA.
Sequence status	Complete.
Protein existence	Inferred 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 process	Pyridine nucleotide biosynthesis
Cellular component	Mitochondrion
Ligand	FAD Flavoprotein NADP
Molecular function	Monooxygenase Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW pyridine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	kynurenine 3-monooxygenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 512	512	Kynurenine 3-monooxygenase		PRO_0000361918

Sequences

	Sequence		Length	Mass (Da)
	Q4WN75-1 [UniParc]. Last modified July 5, 2005. Version 1. Checksum: 0CACA1B38B85140D	FASTA	512	58,088
	10 20 30 40 50 60 MADTVRKKQK LVVVGAGPVG SLAALYAAAR GDEVEIYELR GDLRDPSTVP LNFTKSINLA 70 80 90 100 110 120 LSERGITAMK HSNREDLVNN VLRDTIPMHG RMIHGRDRGK LWEAAQAYDV HGRAINAVDR 130 140 150 160 170 180 STLNNALLDE LECTPNVKLF FNHKLTGADF NARKAWFERR VPGEAPLPNS ANRVPEIEVD 190 200 210 220 230 240 FDFMIGADGA HSAARYHMMK FARVDYQQEY IDTLWCEFRI PPTEDGDFRI SPNHLHIWPG 250 260 270 280 290 300 REFMFIALPS ADKSFTCTLF APAAHYKHLG SSPQNLVESF KDHFPGVCPE LISPEDLQEQ 310 320 330 340 350 360 FTTNPHLPLI SLKCKPHHYN SSIVIVGDAA HAVLPFYGQG LNAGLEDIRV LFECLDKHGS 370 380 390 400 410 420 YNLDASPDAR REARAKAFQA YTDQRCADTH AINDLSKQNY LEMRWGVKTP LYKLRKSVEE 430 440 450 460 470 480 ALDRYVPSLG WQTQYSRVSF SNQRYSDVIR SARWQGRILA LGLATTLIST VGVIAYVFWK 490 500 510 KPRQYSPLSL LRYSWRRLSS IWVTMFRTIA YA

References

[1]

"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus." Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W. Nature 438:1151-1156(2005) [PubMed: 16372009] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAHF01000006 Genomic DNA. Translation: EAL88589.1.
RefSeq	XP_750627.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q4WN75.
Genome annotation databases
GeneID	3508717.
KEGG	afm:AFUA_6G07340.
Phylogenomic databases
eggNOG	fuNOG06151.
HOGENOM	HBG430104.
OMA	HWQKKVI.
OrthoDB	EOG9C2JSV.
PhylomeDB	Q4WN75.
Family and domain databases
InterPro	IPR002938. mOase_FAD_bd. IPR003042. Rng_hydrolase-like. [Graphical view]
Pfam	PF01494. FAD_binding_3. 1 hit. [Graphical view]
PRINTS	PR00420. RNGMNOXGNASE.
ProtoNet	Search...

Entry information

Entry name

KMO_ASPFU

Accession

Primary (citable) accession number: Q4WN75

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 10, 2009
Last sequence update:	July 5, 2005
Last modified:	February 9, 2010
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)