Reviewed, UniProtKB/Swiss-Prot A6RSP5 (KYNU_BOTFB)

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:	BC1G_03468

Organism

Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea) [Complete proteome]

Taxonomic identifier

332648 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Leotiomycetes › Helotiales › Sclerotiniaceae › Botryotinia

Protein attributes

Sequence length	475 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 – 475	475	Kynureninase		PRO_0000360867
Regions
	Region	170 – 173	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	142	1	Pyridoxal phosphate; via amide nitrogen By similarity
	Binding site	143	1	Pyridoxal phosphate By similarity
	Binding site	255	1	Pyridoxal phosphate By similarity
	Binding site	258	1	Pyridoxal phosphate By similarity
	Binding site	280	1	Pyridoxal phosphate By similarity
	Binding site	320	1	Pyridoxal phosphate By similarity
	Binding site	348	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	281	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A6RSP5-1 [UniParc]. Last modified August 21, 2007. Version 1. Checksum: 42BFAB823F77B9F2	FASTA	475	52,872
	10 20 30 40 50 60 MGSIAKEEQP STKVEKPTFS SKANTLEFAQ SLDAKDHMRR FRDQYIIPSK ANIKTKKLAK 70 80 90 100 110 120 PGLSDEPSIY FCGNSLGLQP KCVQEYLQAH LDTWSSIAVH GHFRDLEDSP LTQWQLLAEH 130 140 150 160 170 180 AAKQCAPIVG AKASEVAIMG TLTTNLHLLM ASFYTPTPEK SKIIMEWKAF PSDHYAIESQ 190 200 210 220 230 240 IRGHGYNPEE AMVMIAPDEG SYEISTEKIL RTIDEHASTT ALLLLPGIQY YTGQLFDIKT 250 260 270 280 290 300 ITAYAQSKGL TVGWDLAHAA GNVPLQLHDW NVDFAVWCTY KYMNAGPGSI AGAYVHERHG 310 320 330 340 350 360 EVDYSEGEEK PKYRHRLMGW YGGDQSCRFL MNNKFRPSPG ASGYQVSNPS VVDLTSLCAA 370 380 390 400 410 420 LSIFNQTSMA EISQKTLHLT AYLEHLLLST NSSDSPAFRI ITPSDPSARG TQLSVLLKPG 430 440 450 460 470 RLETLSDMLE EAGIVADKRK PDVIRVAPVP LYNTYEDVWN FVQIFNKALE KCEEA

References

[1]

"Annotation of the Botryotinia fuckeliana B05.10 genome." Birren B.W., Galagan J.E., Lander E.S., Devon K., Nusbaum C., Cuomo C., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K., Pushparaj V. , DeCaprio D., Crawford M., Koehrsen M., Engels R., Montgomery P., Pearson M., Howarth C., Alvarado L., Kodira C.D., Zeng Q., Yandava C., O'Leary S., Amedeo P., Briggs S., Baker S., Goff S., Hohn T., Hutchison D., Lam S., Martin C., Miguel T., Rose M., Turgeon B.G., Wu G., Yoder O., Zheng L. Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CH476854 Genomic DNA. Translation: EDN20078.1.
RefSeq	XP_001557886.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5438547.
KEGG	bfu:BC1G_03468.
Phylogenomic databases
OMA	WQPLSGW.
Family and domain databases
InterPro	IPR000192. Aminotrans_V/Cys_dSase. 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.
Pfam	PF00266. Aminotran_5. 1 hit. [Graphical view]
TIGRFAMs	TIGR01814. kynureninase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

KYNU_BOTFB

Accession

Primary (citable) accession number: A6RSP5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	August 21, 2007
Last modified:	November 3, 2009
This is version 17 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)