A5DM91 (KYNU_PICGU) 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:	PGUG_04392

Organism

Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii) [Complete proteome]

Taxonomic identifier

294746 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Meyerozyma

Protein attributes

Sequence length	445 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 – 445	445	Kynureninase		PRO_0000360871
Regions
	Region	132 – 135	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	104	1	Pyridoxal phosphate; via amide nitrogen By similarity
	Binding site	105	1	Pyridoxal phosphate By similarity
	Binding site	216	1	Pyridoxal phosphate By similarity
	Binding site	219	1	Pyridoxal phosphate By similarity
	Binding site	241	1	Pyridoxal phosphate By similarity
	Binding site	276	1	Pyridoxal phosphate By similarity
	Binding site	304	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	242	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A5DM91 [UniParc]. Last modified July 22, 2008. Version 2. Checksum: C0B61477246C40C5	FASTA	445	50,662
	10 20 30 40 50 60 MSAQLDKEYP TFRHLFEVPT LKSLNISSDT NESIYLCGNS LGLMPKSTRK AINDELDTWA 70 80 90 100 110 120 QQGVEGHFSH PERTPWVDID LPLLPLMAPI VGAKESEVAV MGSLTSNLNA MLMSFYKPKG 130 140 150 160 170 180 KRTKILFEKH AFPSDYYAFL NIVQLFGYDE SHLIQVAVQD GATYLRTEDI IFEIENNAEE 190 200 210 220 230 240 LALVCFPGIQ YYTGQFFDIK SITKAAQDHG ICVGWDLAHA VGNVPLNLHD WNVDFAVWCS 250 260 270 280 290 300 YKYLNSGPGA MAGIFVHQRH TENNSKTSYN PRLAGWWGNN AQERFQMKEE FNPINSALSY 310 320 330 340 350 360 RQSNPSVIDT VAVKASLKVF QEANGIQFLR EKSIKMTQFL QDLLTQSQYY INQNEKPTKL 370 380 390 400 410 420 GFQILTPLDP NQRGCQLSLL FHPHYDEKSK NIMEQVNKYL HNRGIVCDER RPDVIRVAPT 430 440 PLYNTFAEIE YAVKSLNEAL NQIEN

References

[1]

"Evolution of pathogenicity and sexual reproduction in eight Candida genomes." Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S., Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I., Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C., Fitzpatrick D.A., de Groot P.W.J. , Harris D., Hoyer L.L., Hube B., Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D., Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T., Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C., Birren B.W., Kellis M., Cuomo C.A. Nature 459:657-662(2009) [PubMed: 19465905] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CH408159 Genomic DNA. Translation: EDK40294.2.
RefSeq	XP_001483663.1. XM_001483613.1.
3D structure databases
ProteinModelPortal	A5DM91.
ModBase	Search...
Protein-protein interaction databases
STRING	A5DM91.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5125646.
KEGG	pgu:PGUG_04392.
Phylogenomic databases
OrthoDB	EOG4TB7KQ.
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_PICGU

Accession

Primary (citable) accession number: A5DM91

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	July 22, 2008
Last modified:	December 14, 2011
This is version 29 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program