Reviewed, UniProtKB/Swiss-Prot B0XS72 (KYNU1_ASPFC)

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:	AFUB_026170

Organism

Aspergillus fumigatus (strain CEA10 / CBS 144.89 / FGSC A1163) (Sartorya fumigata) [Complete proteome]

Taxonomic identifier

451804 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	509 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 – 509	509	Kynureninase 1		PRO_0000356963
Regions
	Region	197 – 200	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	169	1	Pyridoxal phosphate; via amide nitrogen By similarity
	Binding site	170	1	Pyridoxal phosphate By similarity
	Binding site	283	1	Pyridoxal phosphate By similarity
	Binding site	286	1	Pyridoxal phosphate By similarity
	Binding site	308	1	Pyridoxal phosphate By similarity
	Binding site	349	1	Pyridoxal phosphate By similarity
	Binding site	377	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	309	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	B0XS72-1 [UniParc]. Last modified April 8, 2008. Version 1. Checksum: FAB6BF3A24F37D13	FASTA	509	57,148
	10 20 30 40 50 60 MGSRLHVQVI HGGPPLPYKD DIRAFGKEYA EQLDAQDPLR RFRDEFIIPS KKDLKRKTLF 70 80 90 100 110 120 PNDGMYSCGH PICFANTSCA CVHAAETEET SDEKCIYLCG NSLGLQPRST RKYIDHYLRT 130 140 150 160 170 180 WATKGVTGHF VPHDDQLLPP FVDVDEAGAK LMAPIVGALK SEVAVMGTLT ANLHLLMASF 190 200 210 220 230 240 YRPTPERNKI IIEGKAFPSD HYAVESQIRH HNLDPKDAMV LIEPEDLDRP ILDTKYILRV 250 260 270 280 290 300 IDENAHSTAL ILLPAIQFYT GQYFDIQRIT AHAQSKGILV GWDCAHAAGN VDLRLHDWNV 310 320 330 340 350 360 DFAAWCTYKY LNAGPGGMAA LFVHERHGRV DIEQAASGKE AFHPRFSGWW GGDKQTRFLM 370 380 390 400 410 420 NNHFVPQQGA AGFQLSNPSV LDMNAVVASL ELFNQTSMAE IRKKSLNLTG YLEHLLLRDP 430 440 450 460 470 480 QTENSEKRPF SIITPSNPAE RGAQLSIRLQ PGLLDRVLES LNEDAVIIDE RKPDVIRVAP 490 500 APLYNTYAEV WRFAQLFHLA CDKALCGRK

References

[1]

"Genomic islands in the pathogenic filamentous fungus Aspergillus fumigatus." Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M. , Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R., Jiang B., Denning D.W., Nierman W.C. PLoS Genet. 4:E1000046-E1000046(2008) [PubMed: 18404212] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	DS499595 Genomic DNA. Translation: EDP54558.1.
3D structure databases
ModBase	Search...
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_ASPFC

Accession

Primary (citable) accession number: B0XS72

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	April 8, 2008
Last modified:	September 22, 2009
This is version 9 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)