Reviewed, UniProtKB/Swiss-Prot A2QJI5 (KYNU2_ASPNC)

Names and origin

Protein names

Recommended name:
    Kynureninase 2
    EC=3.7.1.3
Alternative name(s):
    L-kynurenine hydrolase 2
    Biosynthesis of nicotinic acid protein 5-2

Gene names

Name:	bna5-2
ORF Names:	An04g07200

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	463 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively By similarity.
Catalytic activity	L-kynurenine + H2O = anthranilate + L-alanine. L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine.
Cofactor	Pyridoxal phosphate By similarity.
Pathway	Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1. Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 2/3.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the kynureninase family.

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	NAD biosynthetic process Inferred from electronic annotation. Source: InterPro tryptophan catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	kynureninase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 463	463	Kynureninase 2		PRO_0000356968
Regions
	Region	162 – 165	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	134	1	Pyridoxal phosphate; via amide nitrogen By similarity
	Binding site	135	1	Pyridoxal phosphate By similarity
	Binding site	247	1	Pyridoxal phosphate By similarity
	Binding site	250	1	Pyridoxal phosphate By similarity
	Binding site	272	1	Pyridoxal phosphate By similarity
	Binding site	312	1	Pyridoxal phosphate By similarity
	Binding site	340	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	273	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A2QJI5-1 [UniParc]. Last modified March 6, 2007. Version 1. Checksum: 69BFF4F248B8AB07	FASTA	463	51,300
	10 20 30 40 50 60 MSKSNGVSLA FPAEAATKEY AASLDSSDRL AAFREKFIVP SKANIASKKL AKPGLSPESC 70 80 90 100 110 120 IYFCGNSLGI QPKATAKYLE AQLDTWSSIG VGGHFTDLEG SPLKQWQLLS EQAADSMSKI 130 140 150 160 170 180 VGAKPEEVAA MGTLTTNLHL LLASFYKPTQ TKHKILMDWK AFPSDHYAIE SHIAWHDLDP 190 200 210 220 230 240 KESMVLIGPD EGEYEISTQK IFSYIDKHAD EAAMILLPGI QYYTGQLFDI QKITKYAHSR 250 260 270 280 290 300 NMVVGWDLAH AFANVELKLH DWNVDFAAWC TYKYGNAGPG AMGGLFVHEQ HGEVDYSAGE 310 320 330 340 350 360 DAPKFRHRLT GWYGGDRSVR FKMDNKFKPI PGAGGFQISN PSAIDLACLC AALSVFDETS 370 380 390 400 410 420 MADLRRKSLK LTAYLEFLLL RDYEEESRPF SIITPKDPEA RGAQLSLLLK PGLLQNVAQK 430 440 450 460 LQEAGIVCDK REPGVVRVAP VPLYNSFSEV WTFVKIFKDA LQQ

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	AM270081 Genomic DNA. Translation: CAK44720.1.
RefSeq	XP_001402081.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4991124.
GenomeReviews	Gene locus bna5-2 in contig AM270983_GR.
KEGG	ang:An04g07200.
Family and domain databases
InterPro	IPR000192. Aminotrans_V/Cys_dSase. IPR010111. Kynureninase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHER	PTHR14084. Kynureninase. 1 hit.
Pfam	PF00266. Aminotran_5. 1 hit. [Graphical view]
TIGRFAMs	TIGR01814. kynureninase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

KYNU2_ASPNC

Accession

Primary (citable) accession number: A2QJI5

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	March 6, 2007
Last modified:	September 22, 2009
This is version 17 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)