A7TR79 (KYNU_VANPO) 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:	Kpol_1029p21

Organism

Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294) (Kluyveromyces polysporus) [Complete proteome]

Taxonomic identifier

436907 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Vanderwaltozyma

Protein attributes

Sequence length	455 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 – 455	455	Kynureninase		PRO_0000360873
Regions
	Region	122 – 125	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	94	1	Pyridoxal phosphate; via amide nitrogen By similarity
	Binding site	95	1	Pyridoxal phosphate By similarity
	Binding site	208	1	Pyridoxal phosphate By similarity
	Binding site	211	1	Pyridoxal phosphate By similarity
	Binding site	233	1	Pyridoxal phosphate By similarity
	Binding site	275	1	Pyridoxal phosphate By similarity
	Binding site	303	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	234	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A7TR79 [UniParc]. Last modified October 2, 2007. Version 1. Checksum: 066B64E94CDA5EFE	FASTA	455	51,982
	10 20 30 40 50 60 MGIPVNSENV NDETEGDVAG KEVYYLCGNS LGLMPKDTKE TVTRELDAWR DRAVESHFKH 70 80 90 100 110 120 PTDTSWVDID LPVVPLLAPI VGGKNEEVAV MNTLTANLNS LLVSFYRPTK KRFKIVFEKK 130 140 150 160 170 180 AFPSDYYAFY NQCRLHNFDP NECILQISAR PNETFLRTED ILKVIEENNE SIALVCLPGI 190 200 210 220 230 240 QYYSGQLFEI ERITKFAHQY PEIIVGWDLA HAVGNVPLKL HDWGVDFACW CSYKYLNSGP 250 260 270 280 290 300 GSIGGLFIHE KWHHSALKFG DDVNHDEYRP RLAGWWGNNN EKRFQMLEKF EPIKGALGFR 310 320 330 340 350 360 QSNPSVLDVV CLQSSLKIFQ KYGGVENLRL KSLKLTKYLI NQLQKSPYYH PKKQSSKEEL 370 380 390 400 410 420 GFRIITPIQN ESQYGAQISI QLTPSRLTGK NKDTMEIVFE YMHRHGVVVD ERKPNVIRIS 430 440 450 PVPLYNTFQD VFTTVAILNS ALDSVKKSIK ALKSN

References

[1]

"Independent sorting-out of thousands of duplicated gene pairs in two yeast species descended from a whole-genome duplication." Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H. Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007) [PubMed: 17494770] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 22028 / DSM 70294.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DS480471 Genomic DNA. Translation: EDO15247.1.
RefSeq	XP_001643105.1. XM_001643055.1.
3D structure databases
ProteinModelPortal	A7TR79.
ModBase	Search...
Protein-protein interaction databases
STRING	A7TR79.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5543316.
KEGG	vpo:Kpol_1029p21.
Phylogenomic databases
OrthoDB	EOG4TB7KQ.
PhylomeDB	A7TR79.
Family and domain databases
InterPro	IPR000192. Aminotrans_V/Cys_dSase. IPR010111. Kynureninase. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
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_VANPO

Accession

Primary (citable) accession number: A7TR79

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	October 2, 2007
Last modified:	December 14, 2011
This is version 28 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program