Q81CK0 (KYNU_BACCR) 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:	BC_2759

Organism

Bacillus cereus (strain ATCC 14579 / DSM 31)

Taxonomic identifier

226900 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	428 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 – 428	428	Kynureninase		PRO_0000356990
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	213	1	Pyridoxal phosphate By similarity
	Binding site	216	1	Pyridoxal phosphate By similarity
	Binding site	238	1	Pyridoxal phosphate By similarity
	Binding site	267	1	Pyridoxal phosphate By similarity
	Binding site	295	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	239	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q81CK0 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 39B9A789AE41714F	FASTA	428	48,754
	10 20 30 40 50 60 MYKEPFQPTY EYALECDKHD ELKDFQTEFY KKEGTIYLDG NSLGLLSKRA EKSLLTLLDS 70 80 90 100 110 120 WKEYGIDGWT EGEHPWFFLS EKLGKLTAPL IGALPEETIV TGSTTTNIHQ VIATFYEPKG 130 140 150 160 170 180 IRTKILADEL TFPSDIYALQ SQIRLKGLDP EEHLVRVKSR DGRTLSEEDI IHAMEDDIAL 190 200 210 220 230 240 ILLPSVLYRS GQILDMKRLT TEAHKRGIHI GFDLCHSIGS IPHHFKDWDV DFAVWCNYKY 250 260 270 280 290 300 LNAGPGSVAG LYVNSKHFNR LPGLSGWFSS RKDKQFDMEH TLTAADHAGA YQIGTPHVLS 310 320 330 340 350 360 TAPLIGSLEI FKDAGIERLR EKSLHITRYM LNLIGHELKD FEFTIGNPLE DEKRGGHIYL 370 380 390 400 410 420 EHAEAARICK ALKANGVIPD FRAPNGVRLA PVALYNTYEE VWKSVQILKK IMKNEEYKQF ENKREVVA

References

[1]

"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis." Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C. Nature 423:87-91(2003) [PubMed: 12721630] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 14579 / DSM 31.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016877 Genomic DNA. Translation: AAP09712.1.
RefSeq	NP_832511.1. NC_004722.1.
3D structure databases
ProteinModelPortal	Q81CK0.
ModBase	Search...
Protein-protein interaction databases
STRING	Q81CK0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000031852; EBBACP00000031058; EBBACG00000031843.
GeneID	1205107.
GenomeReviews	Gene locus BC_2759 in contig AE016877_GR.
KEGG	bce:BC2759.
PATRIC	32601419. VBIBacCer54481_2814.
Phylogenomic databases
eggNOG	COG3844.
GeneTree	EBGT00050000000895.
HOGENOM	HBG523016.
OMA	TAEAHKR.
PhylomeDB	Q81CK0.
ProtClustDB	CLSK904618.
Enzyme and pathway databases
BioCyc	BCER226900:BC_2759-MONOMER.
Family and domain databases
InterPro	IPR000192. Aminotrans_V/Cys_dSase. IPR010111. Kynureninase. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Gene3D	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_BACCR

Accession

Primary (citable) accession number: Q81CK0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	June 1, 2003
Last modified:	January 25, 2012
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program