Reviewed, UniProtKB/Swiss-Prot Q0CZX6 (KYNU2_ASPTN)

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:	ATEG_00758

Organism

Aspergillus terreus (strain NIH 2624 / FGSC A1156) [Complete proteome]

Taxonomic identifier

341663 [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_0000356972
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)
	Q0CZX6-1 [UniParc]. Last modified October 17, 2006. Version 1. Checksum: 402C2BC2BD9A167A	FASTA	463	51,310
	10 20 30 40 50 60 MSENNCSKPS FPDNAASKEY AASLDAADPL ASFRDQFIIP SKANIACKRL AKPNLSPEPC 70 80 90 100 110 120 IYFCGNSLGI QPKATAKYLE AQLDTWSSIG VCGHFTNLED SPMKSWQLLA EQAAESMSKI 130 140 150 160 170 180 VGADPAEVAA MGTLTANLHL LMASFYKPTA TKHKILMDWK AFPSDHYAIE SHIAWHNLDP 190 200 210 220 230 240 KESMVLIGPD EGEYEISTDK ILSYIDQHAE DAALLLLPGI QYYTGQLFDI PKITEYAKSR 250 260 270 280 290 300 NLVVGWDLAH AYGNVELKLH DWNVDFAAWC TYKYGNAGPG AMAGLFVHDK HGQVDYSQGE 310 320 330 340 350 360 DSPKFRHRLT GWYGGDRSVR FKMDNKFKPI PGAGGFQISN PSAIDLSCLC AALSVFDQTS 370 380 390 400 410 420 VSELRRKSLK LTAYLEYLLL KDTTEDSRPF RIITPTNPEA RGAQLSLLLK PGLLQGVSER 430 440 450 460 LQDAGIICDK REPGVVRVAP VPLYNTYSEV WEFVQQFRAA LQL

References

[1]

"Annotation of the Aspergillus terreus NIH2624 genome." Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M., Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K. , Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R., Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J., Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W., Nierman W.C., Milne T., Madden K. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CH476594 Genomic DNA. Translation: EAU39404.1.
RefSeq	XP_001210844.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4355513.
Family and domain databases
InterPro	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.
TIGRFAMs	TIGR01814. kynureninase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

KYNU2_ASPTN

Accession

Primary (citable) accession number: Q0CZX6

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	October 17, 2006
Last modified:	September 22, 2009
This is version 13 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)