Reviewed, UniProtKB/Swiss-Prot Q59QC4 (KYNU_CANAL)

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:	CaO19.394, CaO19.8024

Organism

Candida albicans (Yeast)

Taxonomic identifier

5476 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	461 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
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 – 461	461	Kynureninase		PRO_0000356973
Regions
	Region	142 – 145	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	114	1	Pyridoxal phosphate; via amide nitrogen By similarity
	Binding site	115	1	Pyridoxal phosphate By similarity
	Binding site	228	1	Pyridoxal phosphate By similarity
	Binding site	231	1	Pyridoxal phosphate By similarity
	Binding site	253	1	Pyridoxal phosphate By similarity
	Binding site	288	1	Pyridoxal phosphate By similarity
	Binding site	316	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	254	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q59QC4-1 [UniParc]. Last modified April 26, 2005. Version 1. Checksum: C96FCFF707B7CEDB	FASTA	461	52,384
	10 20 30 40 50 60 MSLAEAKKLD KKFPTFKNEF AIPTFGSLGI KNNKYESSTE SIYLCGNSLG LMPKNTKKAI 70 80 90 100 110 120 NDELNAWVER GVESHFNHPD KSLTPWVDID LPLLPLIAPI VGAKENEVAV MGSLTANLNA 130 140 150 160 170 180 LLIHFYKPEG KRTKILFEKQ AFPSDYYAFL NIVKLFGYDE KHLIQLEVQP GETYIKTERI 190 200 210 220 230 240 IKAIDENSDE LALVCFPGIQ YYTGQFFKIE EITKYAKEKS QQIKVGWDLA HAVGNVPLNL 250 260 270 280 290 300 HDWGVDFAAW CSYKYLNSGP GAIGGIFVHE KYTIENKKSS FVPRLAGWWG NNSQERFKML 310 320 330 340 350 360 EEFDPINSAL SYRQSNPSVL DVVAVKSSLE VYAKVGGVSK LREKSVALTQ FLQDLLTNSK 370 380 390 400 410 420 YYIPQSSTSN SKFGFKILTP LNPAERGCQL SIMFQPHFDE KDKNVMERVN AYLHDHAIIC 430 440 450 460 DERRPDVIRL APLPLYNTFE ETFIAVQRLF EALDNISKEY M

References

[1]

"The diploid genome sequence of Candida albicans." Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S. Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed: 15123810] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SC5314.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AACQ01000176 Genomic DNA. Translation: EAK92703.1. AACQ01000177 Genomic DNA. Translation: EAK92674.1.
RefSeq	XP_711882.1. XP_711911.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3646483. 3646492.
KEGG	cal:CaO19.394. cal:CaO19.8024.
Organism-specific databases
CGD	CAL0004950. orf19.394.
Phylogenomic databases
OMA	NFPTDVY.
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_CANAL

Accession

Primary (citable) accession number: Q59QC4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	April 26, 2005
Last modified:	November 3, 2009
This is version 26 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)