Reviewed, UniProtKB/Swiss-Prot Q750P5 (KYNU_ASHGO)

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
Ordered Locus Names:	AGL098W

Organism

Ashbya gossypii (Yeast) (Eremothecium gossypii) [Complete proteome]

Taxonomic identifier

33169 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	447 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 – 447	447	Kynureninase		PRO_0000218661
Regions
	Region	134 – 137	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	106	1	Pyridoxal phosphate; via amide nitrogen By similarity
	Binding site	107	1	Pyridoxal phosphate By similarity
	Binding site	220	1	Pyridoxal phosphate By similarity
	Binding site	223	1	Pyridoxal phosphate By similarity
	Binding site	245	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	246	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q750P5-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 6C0AA0A05795D63A	FASTA	447	49,069
	10 20 30 40 50 60 MEKARALEEQ WPGARDAFHV PSYASLGLGD QTAAVRYLCG HSLGCMPRKT RGSVEAELSA 70 80 90 100 110 120 WSARAVEAHV RHPGGTEWVN TDLPLVPQMA RMVGASQQEV AVMGSLTANL NALLVAFYRP 130 140 150 160 170 180 RGRRTKILLE KQVFPSDFHA FWNQAALHGL DPAATLVQVA PRAGEHTLRT EDIVPAIETH 190 200 210 220 230 240 RAELALVCLP GVQYYTGQLL DMASIVAAAR REPSIVVGFD LAHAVGNVQL QLHEWGADFA 250 260 270 280 290 300 CWCSYKYLNA GPGGIAGLFV HEHHHGGTLP RLTGWWGTNA ATRFEMRQTY DPLPDALGFR 310 320 330 340 350 360 QSNPSVLDVA ALRASLEVFE DFGGMERVRA RSLALTGYLY ELLTQSVFYR PEVGADGVGF 370 380 390 400 410 420 TILTPANPAE RGAQLSLLFW PHSDDPDKNT MPRVFADLRQ NGVLGDERHP DVIRLTPCAL 430 440 YNTFMEVFES VQLLNAALER LAPESAV

References

[1]

"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome." Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P. Science 304:304-307(2004) [PubMed: 15001715] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016820 Genomic DNA. Translation: AAS54393.1.
RefSeq	NP_986569.1.
3D structure databases
SMR	Q750P5. Positions 4-439.
ModBase	Search...
Protein-protein interaction databases
STRING	Q750P5.
Genome annotation databases
GeneID	4622868.
GenomeReviews	Gene locus AGL098W in contig AE016820_GR.
KEGG	ago:AGOS_AGL098W.
NMPDR	fig|33169.1.peg.4214.
Organism-specific databases
AGD	AGL098W.
Phylogenomic databases
eggNOG	fuNOG06509.
HOGENOM	HBG523016.
OMA	DECIVGL.
OrthoDB	EOG9RZ0G9.
Enzyme and pathway databases
BRENDA	3.7.1.3. 279361.
Family and domain databases
InterPro	IPR000192. Aminotrans_V/Cys_dSase. IPR010111. Kynureninase. IPR015424. PyrdxlP-dep_Trfase_major_dom. 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_ASHGO

Accession

Primary (citable) accession number: Q750P5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 9, 2004
Last sequence update:	July 5, 2004
Last modified:	February 9, 2010
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)