A5DTF4 (KYNU_LODEL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Kynureninase
EC=3.7.1.3

Alternative name(s):
Biosynthesis of nicotinic acid protein 5
L-kynurenine hydrolase

Gene names

Name:	BNA5
ORF Names:	LELG_00640

Organism

Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus) [Complete proteome]

Taxonomic identifier

379508 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Lodderomyces

Protein attributes

Sequence length	461 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 – 461	461	Kynureninase		PRO_0000360869
Regions
	Region	142 – 145	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	114	1	Pyridoxal phosphate; via amide nitrogen By similarity
	Binding site	115	1	Pyridoxal phosphate By similarity
	Binding site	228	1	Pyridoxal phosphate By similarity
	Binding site	231	1	Pyridoxal phosphate By similarity
	Binding site	253	1	Pyridoxal phosphate By similarity
	Binding site	288	1	Pyridoxal phosphate By similarity
	Binding site	316	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	254	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A5DTF4 [UniParc]. Last modified June 12, 2007. Version 1. Checksum: EB63A54FFB82D793	FASTA	461	52,331
	10 20 30 40 50 60 MSSDKAKAFD AQFPTYKSEF QIPTFESLGI QNSKYSPETN SIYLCGNSLG LMPRNTTELI 70 80 90 100 110 120 NRELQAWSSR GVEAHFNHSH PQGTDWVDID LPLLPLLAPL VGAKQNEVAV MGSLTSNLNA 130 140 150 160 170 180 LLIHFYKPKG KRTKILFEKQ AFPSDYYAFL NIVQVFGYDA SHLIQIEIPK GETYIKTETI 190 200 210 220 230 240 LDVFDKYEDE IAIVCLPGIQ YYTGQFFDIA KITKHVKTSA PDVVVGWDLA HAVGNVPLSL 250 260 270 280 290 300 HDWGVDFAAW CSYKYLNAGP GAIAGIFVNE KYTEQNKPEN YKPRLAGWWG NNSSQRFQML 310 320 330 340 350 360 EKFDPIASAL SYRQLNPSVL DCVALKSSLE IFNKVGGMLS LRDKSLAMTQ FLQDILTKSN 370 380 390 400 410 420 YYIEQGETDV NKFGFKIITP LDPNQRGCQL SLLFQPHRDE KKQNVMERVF EYLHQHAIIC 430 440 450 460 DERRPDVIRL APLPLYNTFE ETRIGATRLL EALEAIKDDY I

References

[1]

"Evolution of pathogenicity and sexual reproduction in eight Candida genomes." Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S., Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I., Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C., Fitzpatrick D.A., de Groot P.W.J. , Harris D., Hoyer L.L., Hube B., Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D., Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T., Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C., Birren B.W., Kellis M., Cuomo C.A. Nature 459:657-662(2009) [PubMed: 19465905] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CH981524 Genomic DNA. Translation: EDK42462.1.
RefSeq	XP_001528120.1. XM_001528070.1.
3D structure databases
ProteinModelPortal	A5DTF4.
ModBase	Search...
Protein-protein interaction databases
STRING	A5DTF4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5235575.
KEGG	lel:LELG_00640.
Phylogenomic databases
OMA	WGHELAT.
OrthoDB	EOG4TB7KQ.
Family and domain databases
InterPro	IPR000192. Aminotrans_V/Cys_dSase. IPR010111. Kynureninase. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Gene3D	G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 2 hits.
KO	K01556.
PANTHER	PTHR14084. Kynureninase. 1 hit.
Pfam	PF00266. Aminotran_5. 1 hit. [Graphical view]
PIRSF	PIRSF038800. KYNU. 1 hit.
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMs	TIGR01814. Kynureninase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

KYNU_LODEL

Accession

Primary (citable) accession number: A5DTF4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	June 12, 2007
Last modified:	November 16, 2011
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program