Q63WP4 (KYNU_BURPS) 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:	BPSL0847

Organism

Burkholderia pseudomallei (Pseudomonas pseudomallei)

Taxonomic identifier

28450 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length	416 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 – 416	416	Kynureninase		PRO_0000357002
Regions
	Region	129 – 132	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	97	1	Pyridoxal phosphate; via amide nitrogen By similarity
	Binding site	98	1	Pyridoxal phosphate By similarity
	Binding site	201	1	Pyridoxal phosphate By similarity
	Binding site	204	1	Pyridoxal phosphate By similarity
	Binding site	226	1	Pyridoxal phosphate By similarity
	Binding site	256	1	Pyridoxal phosphate By similarity
	Binding site	282	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	227	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q63WP4 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: E48A23344B20B27E	FASTA	416	45,898
	10 20 30 40 50 60 MKTREEALAL DRDDPLAPLR EQFALPAGVI YLDGNSLGAQ PRAAAARAQQ VIGAEWGEGL 70 80 90 100 110 120 IRSWNTAGWF ALPRRLGDRL APLIGAADGE VAITDTISIN LFKLLAAMLR HQARHAPKRR 130 140 150 160 170 180 VIVSERSNFP TDLYIAQGLI AQFDRDYELR LIDDPADLPD ALDDETAVAM ITHVNYRTGY 190 200 210 220 230 240 MHDMPSVTQT VRQAGALMLW DLAHSAGAVP VDLNGALADG AVGCTYKYLN GGPGSPAFVW 250 260 270 280 290 300 VPKRHQRAFE QPLSGWWGHR APFAMQPAFE PDPGIARFLC GTQPIVSMSM VECGLDVFAQ 310 320 330 340 350 360 TDMHAIRRKS LALTDAFVAL VESRCAGQPL KLVTPRAHHQ RGSQASFEHP HGYEVMQALI 370 380 390 400 410 ARGVIGDYRE PRILRFGFTP LYTRFVDVWD AVETLRDILD TEAWRAPEFA TRAAVT

References

[1]

"Genomic plasticity of the causative agent of melioidosis, Burkholderia pseudomallei." Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M., Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F., Challis G.L. , Cherevach I., Chillingworth T., Cronin A., Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J. Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004) [PubMed: 15377794] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K96243.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX571965 Genomic DNA. Translation: CAH34839.1.
RefSeq	YP_107472.1. NC_006350.1.
3D structure databases
ProteinModelPortal	Q63WP4.
SMR	Q63WP4. Positions 3-404.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3092669.
GenomeReviews	Gene locus BPSL0847 in contig BX571965_GR.
KEGG	bps:BPSL0847.
NMPDR	fig|272560.3.peg.3113.
PATRIC	19261367. VBIBurPse99623_0913.
Phylogenomic databases
HOGENOM	HBG523016.
OMA	RGSQVSF.
ProtClustDB	CLSK866997.
Enzyme and pathway databases
BioCyc	BPSE272560:BPSL0847-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_BURPS

Accession

Primary (citable) accession number: Q63WP4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	October 25, 2004
Last modified:	January 25, 2012
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program