Reviewed, UniProtKB/Swiss-Prot Q2UJE8 (KYNU2_ASPOR)

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:	AO090003001247

Organism

Aspergillus oryzae [Complete proteome]

Taxonomic identifier

5062 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	468 AA.
Sequence status	Complete.
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 – 468	468	Kynureninase 2		PRO_0000356970
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)
	Q2UJE8-1 [UniParc]. Last modified January 24, 2006. Version 1. Checksum: 1FA4063ABD51773C	FASTA	468	51,623
	10 20 30 40 50 60 MSNVKSSKPV FPENAGSNEY AASLDAADPL ASFRDKFIIP SKANINSKKL AKPGLSSDPC 70 80 90 100 110 120 IYFCGNSLGI QPKATAKYLE AQLDTWSSIG VSGHFVDLEG SPLKQWQLLS EQAAASMSKI 130 140 150 160 170 180 VGAQAEEVAA MGTLTANLHL LLASFYKPTP TKHKILLDWK AFPSDHYAIE SHLAWHNLDP 190 200 210 220 230 240 KQSMVLIGPD EGEYEISTEK ILSYIDEHAE SAALILLPGI QYYTGQLFDI QKITAYAQSR 250 260 270 280 290 300 DLTVGWDLAH AYGNVELKLH DWDVDFAAWC TYKYGNAGPG AMGGLFVHER HGRVDYSEGE 310 320 330 340 350 360 DAPKFRHRLT GWYGGDRSVR FKMDNNFKPI PGAGGWQLSN PSAIDLACLC ASLSVFDETS 370 380 390 400 410 420 MAELRKKSVM LTAYLEHLLL KDTTDETRPF RIVTPADPEA RGAQLSVLLK PGLLQNVSQK 430 440 450 460 LQEGGIVCDK REPGVVRVAP TPLYNTFTDV WKFVSYFKAA LDEPELKN

References

[1]

"Genome sequencing and analysis of Aspergillus oryzae." Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E. , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H. Nature 438:1157-1161(2005) [PubMed: 16372010] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 42149 / RIB 40.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP007155 Genomic DNA. Translation: BAE58317.1.
RefSeq	XP_001820319.1.
3D structure databases
SMR	Q2UJE8. Positions 14-462.
ModBase	Search...
Genome annotation databases
GeneID	5992302.
GenomeReviews	Gene locus bna5-2 in contig AP007155_GR.
KEGG	aor:AO090003001247.
Phylogenomic databases
OrthoDB	EOG9RZ0G9.
PhylomeDB	Q2UJE8.
Family and domain databases
InterPro	IPR000192. Aminotrans_V/Cys_dSase. IPR010111. Kynureninase. IPR015424. PyrdxlP-dep_Trfase_major_dom. 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_ASPOR

Accession

Primary (citable) accession number: Q2UJE8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	January 24, 2006
Last modified:	February 9, 2010
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)