Reviewed, UniProtKB/Swiss-Prot A4UBV5 (KYNU_MAGGR)

Names and origin

Protein names

Recommended name:
    Kynureninase
    EC=3.7.1.3
Alternative name(s):
    L-kynurenine hydrolase
    Biosynthesis of nicotinic acid protein 5

Gene names

Name:	BNA5
ORF Names:	MGG_10969

Organism

Magnaporthe grisea (Rice blast fungus) (Pyricularia grisea) [Complete proteome]

Taxonomic identifier

148305 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Magnaporthales › Magnaporthaceae › Magnaporthe

Protein attributes

Sequence length	510 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 – 510	510	Kynureninase		PRO_0000360870
Regions
	Region	207 – 210	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	179	1	Pyridoxal phosphate; via amide nitrogen By similarity
	Binding site	180	1	Pyridoxal phosphate By similarity
	Binding site	291	1	Pyridoxal phosphate By similarity
	Binding site	294	1	Pyridoxal phosphate By similarity
	Binding site	316	1	Pyridoxal phosphate By similarity
	Binding site	350	1	Pyridoxal phosphate By similarity
	Binding site	378	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	317	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A4UBV5-1 [UniParc]. Last modified May 15, 2007. Version 1. Checksum: 6327C915CE6E527B	FASTA	510	55,892
	10 20 30 40 50 60 MAATQKSLCA IPADPIEFPA DANTLDYARS EDAKCPIRHM REHFIFPTRA SLKKKALDGR 70 80 90 100 110 120 LPVNFELSGP MLDPIAYPPN HAKPGETATA QNGTSNTNDD NVTPAVYFCG NSLGLQPKAT 130 140 150 160 170 180 RDHINAQLET WASIGVHGHF TSWDNSPLKS WQDMAADCAA QSASVVGASP DEIAIMNTLT 190 200 210 220 230 240 ANLHFMMASF YRPTEKRHKI ISEWKPFPSD TYAIASQIQW HGFDTATSLV ELHPDENYYI 250 260 270 280 290 300 STEKILATID EHAESTALLL LPGIQYWSGQ LFDMPLITAH ARAKGIVVGW DLAHAVGNVP 310 320 330 340 350 360 LSLHDWDVDF AIWCTYKYLN AGPGAIAGAF VHERHGKVDS DGFKLRLSGW YGNNKATRFN 370 380 390 400 410 420 MAKDFDPTPG AQGWVVSNPS GIDLASLGAA LSVYNLTTPA DLRKKSLWLT AYAEHLLNGI 430 440 450 460 470 480 LKDEAASSAG DGKKPAFRII TPSNKNERGA QLSVLLREGL LDVVGEKMEA AGVVCDRRKP 490 500 510 DVMRVAPVPM YNSYEDVWRC VDALRKAVMS

References

[1]

"The genome sequence of the rice blast fungus Magnaporthe grisea." Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K., Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D., Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S., Soanes D.M. , Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M., Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E., Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W. Nature 434:980-986(2005) [PubMed: 15846337] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 70-15 / FGSC 8958.

Cross-references

Sequence databases
EMBLGenBankDDBJ	DS231523 Genomic DNA. Translation: EDK06606.1.
RefSeq	XP_361892.1.
UniGene	Mgr.14510
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2677723.
KEGG	mgr:MGG_10969.
NMPDR	fig|242507.1.peg.3632.
Phylogenomic databases
OMA	WQPLSGW.
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

KYNU_MAGGR

Accession

Primary (citable) accession number: A4UBV5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	May 15, 2007
Last modified:	November 3, 2009
This is version 22 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)