Q63AJ0 (KYNU_BACCZ) 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:	BCE33L2488

Organism

Bacillus cereus (strain ZK / E33L) [Complete proteome] [HAMAP]

Taxonomic identifier

288681 [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
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_0000356991
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)
	Q63AJ0 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: 3BCB80FD356D4BD4	FASTA	428	48,707
	10 20 30 40 50 60 MYKEPFQPTY EYALECDKHD ELKDFQTEFY KKEGTIYLDG NSLGLLSKRA EKSLLTLLDS 70 80 90 100 110 120 WKEYGIDGWT EGEHPWFFLS EKLGELTAPL IGALPEETIV TGSTTTNIHQ VIATFYEPKG 130 140 150 160 170 180 IRTKILADEL TFPSDIYALQ SQIRLKGLDP DEHLVRVKSR DGRTLSEDDI IQAMTDDIAL 190 200 210 220 230 240 ILLPSVLYRS GQILDMKRLT AEAHKRGIHI GFDLCHSIGS IPHHFKEWDV DFAIWCNYKY 250 260 270 280 290 300 LNAGPGGVAG LYVNKKHFNR PPGLSGWFSS RKDKQFDMEH TLTAADHAGA YQIGTPHVLS 310 320 330 340 350 360 TAPLIGSLEI FKDAGIERLR EKSLHITRYM LNLIDHELKD FGFTIGNPFE DEKRGGHIYL 370 380 390 400 410 420 EHAEAARICK ALKANGVIPD FRAPNGVRLA PVALYNTYEE VWQSVMILKK IMKDEEYKQF ENKREVVA

References

[1]

"Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis." Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Hill K.K., Hitchcock P. , Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Brettin T.S., Gilna P. J. Bacteriol. 188:3382-3390(2006) [PubMed: 16621833] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ZK / E33L.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000001 Genomic DNA. Translation: AAU17771.1.
RefSeq	YP_084077.1. NC_006274.1.
3D structure databases
ProteinModelPortal	Q63AJ0.
ModBase	Search...
Protein-protein interaction databases
STRING	Q63AJ0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000040158; EBBACP00000039059; EBBACG00000040149.
GeneID	3022624.
GenomeReviews	Gene locus BCE33L2488 in contig CP000001_GR.
KEGG	bcz:BCZK2488.
PATRIC	18888598. VBIBacCer95304_2637.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG3844.
GeneTree	EBGT00050000000895.
HOGENOM	HBG523016.
OMA	TAEAHKR.
PhylomeDB	Q63AJ0.
ProtClustDB	CLSK904618.
Enzyme and pathway databases
BioCyc	BCER288681:BCE33L2488-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_BACCZ

Accession

Primary (citable) accession number: Q63AJ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	October 25, 2004
Last modified:	January 25, 2012
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program