Q0UIN2 (KYNU1_PHANO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Kynureninase 1
EC=3.7.1.3

Alternative name(s):
Biosynthesis of nicotinic acid protein 5-1
L-kynurenine hydrolase 1

Gene names

Name:	BNA5-1
ORF Names:	SNOG_08382

Organism

Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume blotch fungus) (Septoria nodorum)

Taxonomic identifier

321614 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Dothideomycetes › Pleosporomycetidae › Pleosporales › Pleosporineae › Phaeosphaeriaceae › Phaeosphaeria

Protein attributes

Sequence length	506 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 Reference 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 – 506	506	Kynureninase 1		PRO_0000356982
Regions
	Region	169 – 172	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	141	1	Pyridoxal phosphate; via amide nitrogen By similarity
	Binding site	142	1	Pyridoxal phosphate By similarity
	Binding site	254	1	Pyridoxal phosphate By similarity
	Binding site	257	1	Pyridoxal phosphate By similarity
	Binding site	279	1	Pyridoxal phosphate By similarity
	Binding site	334	1	Pyridoxal phosphate By similarity
	Binding site	362	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	280	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0UIN2 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 065722108D062DF3	FASTA	506	55,984
	10 20 30 40 50 60 MSQTTNSYDS FQDADLCSAA FAEKQDEKDK LTKLREDFYI PTKGDLINKK YGFQKSGNNA 70 80 90 100 110 120 KGHENGKCIY FCGNSLGLQP TRTKEYINRY LDTWASKGVF GHFTDYEGGL PPWLHIDDAV 130 140 150 160 170 180 KEQTSKIVGA LPSEVVIMET LTANLHLLMS SFYRPTKDRW KIIIEGKAFP SDHYAALSQI 190 200 210 220 230 240 AHHDLDPSAL ITIEPPSSSA PYLSNEHILS VISKHAATTA LVLLPGIQFY SGQFFDIELI 250 260 270 280 290 300 TRHCRALGIT VGWDLAHAVG NVPLKLHDWN VDFAAWCNYK YMSGGPGVIG GAFVHERHGT 310 320 330 340 350 360 VGETAPTTTP DGTNGNPKTI SDESLTYRPR LSGWWGNDKS SRFTMDNKFV PIPGASGYQL 370 380 390 400 410 420 SNPSALDMTS VMASLDVFAL TTMDALRERS IRLTGYLEAR LLRYPGGEPP YTIITPTNPA 430 440 450 460 470 480 ERGAQLSVML RPGMLDSVLH HLEKEGVVVD ERKPDVLRIA PAPLYNTFRD VHDFIGIFHE 490 500 ACRKALVKPA EAPKHSEGVP KAIQTT

References

[1]

"Dothideomycete-plant interactions illuminated by genome sequencing and EST analysis of the wheat pathogen Stagonospora nodorum." Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L., Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E., Torriani S.F.F., McDonald B.A., Oliver R.P. Plant Cell 19:3347-3368(2007) [PubMed: 18024570] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SN15 / ATCC MYA-4574 / FGSC 10173.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CH445336 Genomic DNA. Translation: EAT84658.1.
RefSeq	XP_001798697.1. XM_001798645.1.
3D structure databases
ProteinModelPortal	Q0UIN2.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SNOT_08382; SNOT_08382; SNOG_08382.
GeneID	5975595.
KEGG	pno:SNOG_08382.
Phylogenomic databases
OMA	WGHELAT.
OrthoDB	EOG4TB7KQ.
PhylomeDB	Q0UIN2.
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

KYNU1_PHANO

Accession

Primary (citable) accession number: Q0UIN2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	September 5, 2006
Last modified:	November 16, 2011
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program