Reviewed, UniProtKB/Swiss-Prot Q0CPB0 (KYNU1_ASPTN)

Names and origin

Protein names

Recommended name:
    Kynureninase 1
    EC=3.7.1.3
Alternative name(s):
    L-kynurenine hydrolase 1
    Biosynthesis of nicotinic acid protein 5-1

Gene names

Name:	bna5-1
ORF Names:	ATEG_04474

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	483 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 – 483	483	Kynureninase 1		PRO_0000356971
Regions
	Region	175 – 178	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	147	1	Pyridoxal phosphate; via amide nitrogen By similarity
	Binding site	148	1	Pyridoxal phosphate By similarity
	Binding site	261	1	Pyridoxal phosphate By similarity
	Binding site	264	1	Pyridoxal phosphate By similarity
	Binding site	286	1	Pyridoxal phosphate By similarity
	Binding site	326	1	Pyridoxal phosphate By similarity
	Binding site	354	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	287	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0CPB0-1 [UniParc]. Last modified October 17, 2006. Version 1. Checksum: 6BCC62116EAB97BD	FASTA	483	54,112
	10 20 30 40 50 60 MGSRLHLRDI KHGPPLPYHD DIRAFTKEYA ESLDAQDPLR KFRDEFIIPS KKDLKRTVLA 70 80 90 100 110 120 ADENTDDSTD PRCIYLCGNS LGLQPRSTRK YIDRYLRTWA IKGVTGHFTP HDDQLLPPFV 130 140 150 160 170 180 DVDVAGAKLM APVVGALESE VAVMDTLTTN LHLLMASFYR PTQERYKIII EGKAFPSDHY 190 200 210 220 230 240 AVESQIRHHN REPSEAMVLI EPEDPKHPIL TTDQILRVID ENASSAALIL LSAIQFYTGQ 250 260 270 280 290 300 YFDIKTITAH AQSKGIIVGW DCAHAAGNVD LQLHDWNVDF AAWCNYKYLN SGPGGMAGLF 310 320 330 340 350 360 VHERHGHVES KNGAQNEGFR PRLSGWWGGD KETRFLMDNN FRPQVGAAGF QLSNPSVLDM 370 380 390 400 410 420 NAVVASLEIF SRASMEKIRQ KSLHLTGYLE HLLVTYPLDA PPEEKPFTII TPSNPAERGA 430 440 450 460 470 480 QLSLRLGPGL LEKVLEVLEE QGVIIDERKP DVIRVAPAPL YNTYAELSSS GIHIAYSSYN QYS

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	CH476599 Genomic DNA. Translation: EAU34921.1.
RefSeq	XP_001213652.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4320432.
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

KYNU1_ASPTN

Accession

Primary (citable) accession number: Q0CPB0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	October 17, 2006
Last modified:	September 22, 2009
This is version 14 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)