Reviewed, UniProtKB/Swiss-Prot A2QMH1 (KMO2_ASPNC)

Names and origin

Protein names

Recommended name:
    Kynurenine 3-monooxygenase 2
    EC=1.14.13.9
Alternative name(s):
    Kynurenine 3-hydroxylase 2
    Biosynthesis of nicotinic acid protein 4-2

Gene names

Name:	bna4-2
ORF Names:	An07g02080

Organism

Aspergillus niger (strain CBS 513.88 / FGSC A1513) [Complete proteome]

Taxonomic identifier

425011 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	488 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Sequence caution	The sequence CAK48109.1 differs from that shown. Reason: Erroneous gene model prediction.

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 – 488	488	Kynurenine 3-monooxygenase 2		PRO_0000361920

Sequences

	Sequence		Length	Mass (Da)
	A2QMH1-1 [UniParc]. Last modified February 10, 2009. Version 2. Checksum: 1ECDC152F1D73E34	FASTA	488	54,798
	10 20 30 40 50 60 MTADGKIVIV GGGPVGSLAA LYASHYHDNV EVYELRDERQ NPAGASPLLQ KSINFTLSER 70 80 90 100 110 120 GIRALEKSGR TDLLRAIMRT AIPMHGRMVH GRMVHGRSVS GKLQETFHQY DVHGNSLYSL 130 140 150 160 170 180 DRKALNIALR QELDATPNVK MFFHHKLIRA DMNTRKVWFE QREDPSTSTS PSTSSTPKEV 190 200 210 220 230 240 PFDFLIGADG AHSTTRQQIM RYTPLDYQQQ YADTVWCELR IPPTEKTNSF RLPPNYLHIW 250 260 270 280 290 300 PGGEYMFCAF PCPDQSFNCI LFAPASRLDA LKSSPPATLF DFFDTHFPGV CPDLISQSSL 310 320 330 340 350 360 SQQFYQSPHL PLIGIKCSPH HLGSAAVIIG DAAHAMFPFY GQGLNAGMED VRILFDLLDE 370 380 390 400 410 420 HRVFGHGKSL DKDHARAAAL TEYSNQRVRD AHAIHDLSRR NYLELRGGVN SPVYKARKFV 430 440 450 460 470 480 EEALQRYVPL LGWRTLYSRV SFSDQRYSEV VVKNELQGWV LLLMSGLGVL LHVLVFGALG GAFLGLKR

References

[1]

"Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88." Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M. , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H. Nat. Biotechnol. 25:221-231(2007) [PubMed: 17259976] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AM270121 Genomic DNA. Translation: CAK48109.1. Sequence problems.
RefSeq	XP_001391294.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4981475.
GenomeReviews	Gene locus bna4-2 in contig AM270986_GR.
KEGG	ang:An07g02080.
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

KMO2_ASPNC

Accession

Primary (citable) accession number: A2QMH1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 10, 2009
Last sequence update:	February 10, 2009
Last modified:	September 22, 2009
This is version 19 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)