Q9RYH5 (KYNU_DEIRA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Kynureninase
EC=3.7.1.3

Alternative name(s):
L-kynurenine hydrolase

Gene names

Name:	kynU
Ordered Locus Names:	DR_A0338

Organism

Deinococcus radiodurans

Taxonomic identifier

1299 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus

Protein attributes

Sequence length	410 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.
Sequence similarities	Belongs to the kynureninase family.

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Ligand	Pyridoxal phosphate
Molecular function	Hydrolase
Technical term	Complete proteome Reference 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: InterPro
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 – 410	410	Kynureninase		PRO_0000357003
Regions
	Region	135 – 138	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	108	1	Pyridoxal phosphate; via amide nitrogen By similarity
	Binding site	109	1	Pyridoxal phosphate By similarity
	Binding site	205	1	Pyridoxal phosphate By similarity
	Binding site	208	1	Pyridoxal phosphate By similarity
	Binding site	230	1	Pyridoxal phosphate By similarity
	Binding site	260	1	Pyridoxal phosphate By similarity
	Binding site	286	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	231	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9RYH5 [UniParc]. Last modified December 16, 2008. Version 2. Checksum: 50177666F0EA98F0	FASTA	410	43,890
	10 20 30 40 50 60 MTTLLPALDL AQLDALDARD PLAHKRAEFD LPGDIIYLDG NSLGALPRRV PARLSQVATE 70 80 90 100 110 120 EWGHHLIRSW TRNAEAAQDW MALPDRVAAK LAPLLGAGAH EVAVGDSTSV NTFKALAAAL 130 140 150 160 170 180 RLSGRRVILS DADNFPTDLY VAQGLARLLG DVEVRTAPGD EMTQHFTDDV GVVLLTEVDY 190 200 210 220 230 240 RTGRRLDMRA ITAAAHARGI VTVWDLAHSA GAFAVDLGGA GADFAIGCGY KFLNGGPGAP 250 260 270 280 290 300 AFLYVAERHL DRAEVVLSGW MGHADPFEMA RAYAPAPGAR RFVVGTPQVL SLSALDAALD 310 320 330 340 350 360 VFGDVDLGAL REKSLSLTDT FIRLMEPLAE QYPLELVTPL AHAERGSQVS YRHPHAQQVM 370 380 390 400 410 AQLIECGIVG DFRTPDILRF GFTPLYLSHG DVGRAVAGIA AVLDELEGPA

References

[1]

"Genome sequence of the radioresistant bacterium Deinococcus radiodurans R1." White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D., Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L., Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M., Vamathevan J.J., Lam P. , McDonald L.A., Utterback T.R., Zalewski C., Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D., Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M. Science 286:1571-1577(1999) [PubMed: 10567266] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE001825 Genomic DNA. Translation: AAF12444.1.
PIR	F75588.
RefSeq	NP_285661.1. NC_001264.1.
3D structure databases
ProteinModelPortal	Q9RYH5.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1799657.
GenomeReviews	Gene locus DR_A0338 in contig AE001825_GR.
KEGG	dra:DR_A0338.
NMPDR	fig|243230.1.peg.3151.
PATRIC	21633722. VBIDeiRad64572_3230.
TIGR	DR_A0338.
Phylogenomic databases
HOGENOM	HBG523016.
OMA	RGSQVSF.
PhylomeDB	Q9RYH5.
ProtClustDB	CLSK2460391.
Enzyme and pathway databases
BioCyc	DRAD243230:DR_A0338-MONOMER.
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. 2 hits.
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_DEIRA

Accession

Primary (citable) accession number: Q9RYH5

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	December 16, 2008
Last modified:	January 25, 2012
This is version 63 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program