Reviewed, UniProtKB/Swiss-Prot A1DGW4 (KYNU1_NEOFI)

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:	NFIA_085760

Organism

Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181) (Aspergillus fischerianus) [Complete proteome]

Taxonomic identifier

331117 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Neosartorya

Protein attributes

Sequence length	487 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 – 487	487	Kynureninase 1		PRO_0000356979
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	327	1	Pyridoxal phosphate By similarity
	Binding site	355	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	287	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1DGW4-1 [UniParc]. Last modified January 23, 2007. Version 1. Checksum: 831F18F1EC3CAAC7	FASTA	487	55,160
	10 20 30 40 50 60 MGSRLHVQEI QGGPPLPYED DIRAFCKEYA ELLDAHDPLR RFRDEFIVPS KKDLKRKTLF 70 80 90 100 110 120 PNDETEETSD EECIYLCGNS LGLQPRSTRK YIEYYLRTWA TKGVTGHFVP HDDQLLPPFV 130 140 150 160 170 180 NVDEAGAKLM APIVGALKSE VAVMGTLTAN LHLLMASFYR PTRERYKIII EGKAFPSDHY 190 200 210 220 230 240 AVESQIRHHN LDPKDAMVLI ESDDLDRPIL DTEYILRVID ENAHSTALIL LSAIQFYTGQ 250 260 270 280 290 300 YFDIQRITAH AQSKGILVGW DCAHAAGNVD LRLHDWNVDF AAWCTYKYLN AGPGGMAALF 310 320 330 340 350 360 VHERHGRVDM EQAASGKEAF HPRFSGWWGG DKQTRFLMNN HFVPQQGAAG FQLSNPSVLD 370 380 390 400 410 420 MNAVVASLEL FNQTSMAEIR KKSLNLTGYL EHLLLRDPQT ESSEKRPFSI ITPSNPAERG 430 440 450 460 470 480 AQLSIRLQPG LLDRVLESLD EDAVIIDERK PDVIRVAPAP LYNTYVEVWR FAQLFHLACD KALRGRE

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	DS027696 Genomic DNA. Translation: EAW18621.1.
RefSeq	XP_001260518.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4587076.
KEGG	nfi:NFIA_085760.
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_NEOFI

Accession

Primary (citable) accession number: A1DGW4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	January 23, 2007
Last modified:	September 22, 2009
This is version 15 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)